##################################################### # Mutual Folding Induced by Binding (MFIB) database # # Version: 09-08-2024 # # Source: https://mfib.pbrg.hu/ # ##################################################### [Entry] [Entry number]=1 [Entry name]=Bacterial antidote ParD [PDB ID]=2an7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:17656583). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P22995 [UniProt boundaries chain A]=1-83 [UniProt coverage chain A]=100% [Name chain A]=Antitoxin ParD [UniProt sequence chain A]=MSRLTIDMTDQQHQSLKALAALQGKTIKQYALERLFPGDADADQAWQELKTMLGNRINDGLAGKVSTKSVGEILDEELSGDRA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P22995 [UniProt boundaries chain B]=1-83 [UniProt coverage chain B]=100% [Name chain B]=Antitoxin ParD [UniProt sequence chain B]=MSRLTIDMTDQQHQSLKALAALQGKTIKQYALERLFPGDADADQAWQELKTMLGNRINDGLAGKVSTKSVGEILDEELSGDRA [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF2120001 [Entry] [Entry number]=2 [Entry name]=Helicobacter pylori HP0222 [PDB ID]=1x93 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Transcriptional regulator, RHH-like, CopG [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:15723352). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2120002,MF2120003 [UniProt ID chain A]=O25010 [UniProt boundaries chain A]=31-73 [UniProt coverage chain A]=58% [Name chain A]=CopG family transcriptional regulator [UniProt sequence chain A]=MEKTENTDETRLRGTKNKLGRKPKADANKKTRAVSLYFSDEQYQKLEKMANEEEESVGSYIKRYILKALRKIE [Source organism chain A]=Helicobacter pylori [UniProt ID chain B]=O25010 [UniProt boundaries chain B]=31-73 [UniProt coverage chain B]=58% [Name chain B]=CopG family transcriptional regulator [UniProt sequence chain B]=MEKTENTDETRLRGTKNKLGRKPKADANKKTRAVSLYFSDEQYQKLEKMANEEEESVGSYIKRYILKALRKIE [Source organism chain B]=Helicobacter pylori [ExpTech]=NMR [Resolution]=N/A [Source organism]=Helicobacter pylori [Accession]=MF2120002 [Entry] [Entry number]=3 [Entry name]=Helicobacter pylori JHP0511 (HP0564) [PDB ID]=2k1o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Transcriptional regulator, RHH-like, CopG [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:18623065). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2120002,MF2120003 [UniProt ID chain A]=Q9ZLR7 [UniProt boundaries chain A]=21-74 [UniProt coverage chain A]=66% [Name chain A]=Putative [UniProt sequence chain A]=MELGNKNIKPGRKRVAVDELKRNFSVTFYLSKEEHDVLRRLADEEVESVNSFVKRHILKTIIYKKGTNQDSSINCDSSSRL [Source organism chain A]=Helicobacter pylori [UniProt ID chain B]=Q9ZLR7 [UniProt boundaries chain B]=21-74 [UniProt coverage chain B]=66% [Name chain B]=Putative [UniProt sequence chain B]=MELGNKNIKPGRKRVAVDELKRNFSVTFYLSKEEHDVLRRLADEEVESVNSFVKRHILKTIIYKKGTNQDSSINCDSSSRL [Source organism chain B]=Helicobacter pylori [ExpTech]=NMR [Resolution]=N/A [Source organism]=Helicobacter pylori [Accession]=MF2120003 [Entry] [Entry number]=4 [Entry name]=ParG [PDB ID]=1p94 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:14622405). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9KJ82 [UniProt boundaries chain A]=1-76 [UniProt coverage chain A]=100% [Name chain A]=Plasmid partition protein ParG [UniProt sequence chain A]=MSLEKAHTSVKKMTFGENRDLERVVTAPVSSGKIKRVNVNFDEEKHTRFKAACARKGTSITDVVNQLVDNWLKENE [Source organism chain A]=Salmonella newport [UniProt ID chain B]=Q9KJ82 [UniProt boundaries chain B]=1-76 [UniProt coverage chain B]=100% [Name chain B]=Plasmid partition protein ParG [UniProt sequence chain B]=MSLEKAHTSVKKMTFGENRDLERVVTAPVSSGKIKRVNVNFDEEKHTRFKAACARKGTSITDVVNQLVDNWLKENE [Source organism chain B]=Salmonella newport [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella newport [Accession]=MF2120004 [Entry] [Entry number]=5 [Entry name]=Human parathyroid hormone [PDB ID]=1et1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P01270 [UniProt boundaries chain A]=32-65 [UniProt coverage chain A]=29% [Name chain A]=Parathyroid hormone [UniProt sequence chain A]=MIPAKDMAKVMIVMLAICFLTKSDGKSVKKRSVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFVALGAPLAPRDAGSQRPRKKEDNVLVESHEKSLGEADKADVNVLTKAKSQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P01270 [UniProt boundaries chain B]=32-65 [UniProt coverage chain B]=29% [Name chain B]=Parathyroid hormone [UniProt sequence chain B]=MIPAKDMAKVMIVMLAICFLTKSDGKSVKKRSVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFVALGAPLAPRDAGSQRPRKKEDNVLVESHEKSLGEADKADVNVLTKAKSQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=0.90 [Source organism]=Homo sapiens [Accession]=MF2100001 [Entry] [Entry number]=6 [Entry name]=Human ribosomal protein P1-P2 heterodimer [PDB ID]=4beh [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=60s Acidic ribosomal protein [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100002,MF2200001 [UniProt ID chain A]=P05386 [UniProt boundaries chain A]=1-114 [UniProt coverage chain A]=100% [Name chain A]=Large ribosomal subunit protein P1 [UniProt sequence chain A]=MASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P05387 [UniProt boundaries chain B]=1-115 [UniProt coverage chain B]=100% [Name chain B]=Large ribosomal subunit protein P2 [UniProt sequence chain B]=MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2200001 [Entry] [Entry number]=7 [Entry name]=Dimerization domain of ribosomal protein P2 [PDB ID]=2w1o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=60s Acidic ribosomal protein [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100002,MF2200001 [UniProt ID chain A]=P05387 [UniProt boundaries chain A]=1-69 [UniProt coverage chain A]=60% [Name chain A]=Large ribosomal subunit protein P2 [UniProt sequence chain A]=MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P05387 [UniProt boundaries chain B]=1-69 [UniProt coverage chain B]=60% [Name chain B]=Large ribosomal subunit protein P2 [UniProt sequence chain B]=MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2100002 [Entry] [Entry number]=8 [Entry name]=Nuclear receptor coactivators CBP and ACTR [PDB ID]=1kbh [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Nuclear receptor coactivator,Creb binding [Evidence level]=Direct evidence [Evidence text]=The interacting monomers have been described to undergo mutual synergistic folding upon binding (PMID:11823864). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00343 covers 93% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP00348 covers 100% of the sequence present in the structure [Similar structures]=MF2201001,MF2201003 [UniProt ID chain A]=Q9Y6Q9 [UniProt boundaries chain A]=1045-1091 [UniProt coverage chain A]=3% [Name chain A]=Nuclear receptor coactivator 3 [UniProt sequence chain A]=MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNGVSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGEDLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDRHGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLADPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNIMISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKESSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVSSSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGNVVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQEKDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLKSSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGSSMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPTLPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQVSHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMNQMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTAGGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQPDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQFAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P45481 [UniProt boundaries chain B]=2059-2117 [UniProt coverage chain B]=2% [Name chain B]=Histone lysine acetyltransferase CREBBP [UniProt sequence chain B]=MAENLLDGPPNPKRAKLSSPGFSANDNTDFGSLFDLENDLPDELIPNGELSLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSTNMASLGAMGKSPLNQGDSSTPNLPKQAASTSGPTPPASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPYPAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTGTTSPFGQPFSQTGGQQMGATGVNPQLASKQSMVNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGAGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPMSIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPEVKVEAKEEEENSSNDTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQNTALIAPHQIQGRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETPEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVNMSPAGFPNVARTQPPTIVSAGKPTNQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRANINNGMPPGRAGMGTPGSQMTPVGLNVPRPNQVSGPVMSSMPPGQWQQAPIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPGHNPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNSASLAGGMAGHSQFQQPQGPGGYAPAMQQQRMQQHLPIQGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSMDQGHLGNPEQSAMLPQLNTPNRSALSSELSLVGDTTGDTLEKFVEGL [Source organism chain B]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF2201001 [Entry] [Entry number]=9 [Entry name]=L27 (Lin-2, Lin-7) domain complex (rat) [PDB ID]=1rso [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=L27 domains [Subclass]=L27_1 type [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a heterotetrameric L27 complex (PMID:15048107). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=Q62696 [UniProt boundaries chain A]=4-63 [UniProt coverage chain A]=6% [Name chain A]=Disks large homolog 1 [UniProt sequence chain A]=MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVISIFQSNLFQALIDIQEFYEVTLLDNPKCVDHSKQCEPVQPGNPWESGSLSSAAVTSESLPGGLSPPVEKYRYQDEEVLPSERISPQVPNEVLGPELVHVSEKSLSEIENVHGFVSHSHISPIKPTEAVPPSSPIVPVTPALPVPAESPVVLPSTPQANPPPVLVNTDSLETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEADVRDVTHSKAVEALKEAGSIVRLYVKRRKAFRKNHEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNSVCLEEVTHEEAVTALKNTSDFVYLKAAKPTSMYINDGYAPPDITNSSSQSVDNHVSPSSYLGQTPASPARYSPISKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLRETMMNSSVSSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRGDKGEIPDDMGSKGLKHVTSNASDSESSYHEYGCSKGGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRVNDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVRAVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTDEQARKTFERAVRLEQEFTEHFTAIVQGDTLEDIYNQVKQIIEEQSGPYIWVPAKEKL [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=Q62915 [UniProt boundaries chain B]=339-394 [UniProt coverage chain B]=6% [Name chain B]=Peripheral plasma membrane protein CASK [UniProt sequence chain B]=MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHHVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNADLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPERFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFPPFVVFIAAPTITPGLNEDESLQRLQKESDVLQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY [Source organism chain B]=Rattus norvegicus [UniProt ID chain C]=Q62696 [UniProt boundaries chain C]=4-63 [UniProt coverage chain C]=6% [Name chain C]=Disks large homolog 1 [UniProt sequence chain C]=MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVISIFQSNLFQALIDIQEFYEVTLLDNPKCVDHSKQCEPVQPGNPWESGSLSSAAVTSESLPGGLSPPVEKYRYQDEEVLPSERISPQVPNEVLGPELVHVSEKSLSEIENVHGFVSHSHISPIKPTEAVPPSSPIVPVTPALPVPAESPVVLPSTPQANPPPVLVNTDSLETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEADVRDVTHSKAVEALKEAGSIVRLYVKRRKAFRKNHEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNSVCLEEVTHEEAVTALKNTSDFVYLKAAKPTSMYINDGYAPPDITNSSSQSVDNHVSPSSYLGQTPASPARYSPISKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLRETMMNSSVSSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRGDKGEIPDDMGSKGLKHVTSNASDSESSYHEYGCSKGGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRVNDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVRAVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTDEQARKTFERAVRLEQEFTEHFTAIVQGDTLEDIYNQVKQIIEEQSGPYIWVPAKEKL [Source organism chain C]=Rattus norvegicus [UniProt ID chain D]=Q62915 [UniProt boundaries chain D]=339-394 [UniProt coverage chain D]=6% [Name chain D]=Peripheral plasma membrane protein CASK [UniProt sequence chain D]=MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHHVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNADLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPERFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFPPFVVFIAAPTITPGLNEDESLQRLQKESDVLQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY [Source organism chain D]=Rattus norvegicus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Rattus norvegicus [Accession]=MF4210001 [Entry] [Entry number]=10 [Entry name]=CBP nuclear coactivator binding domain in complex with p53 TAD [PDB ID]=2l14 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00348 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP00086 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=P45481 [UniProt boundaries chain A]=2059-2117 [UniProt coverage chain A]=2% [Name chain A]=Histone lysine acetyltransferase CREBBP [UniProt sequence chain A]=MAENLLDGPPNPKRAKLSSPGFSANDNTDFGSLFDLENDLPDELIPNGELSLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSTNMASLGAMGKSPLNQGDSSTPNLPKQAASTSGPTPPASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPYPAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTGTTSPFGQPFSQTGGQQMGATGVNPQLASKQSMVNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGAGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPMSIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPEVKVEAKEEEENSSNDTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQNTALIAPHQIQGRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETPEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVNMSPAGFPNVARTQPPTIVSAGKPTNQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRANINNGMPPGRAGMGTPGSQMTPVGLNVPRPNQVSGPVMSSMPPGQWQQAPIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPGHNPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNSASLAGGMAGHSQFQQPQGPGGYAPAMQQQRMQQHLPIQGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSMDQGHLGNPEQSAMLPQLNTPNRSALSSELSLVGDTTGDTLEKFVEGL [Source organism chain A]=Mus musculus [UniProt ID chain B]=P04637 [UniProt boundaries chain B]=13-61 [UniProt coverage chain B]=12% [Name chain B]=Cellular tumor antigen p53 [UniProt sequence chain B]=MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF2201002 [Entry] [Entry number]=11 [Entry name]=P160/CREB-binding protein coactivator complex [PDB ID]=2c52 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Nuclear receptor coactivator,Creb binding [Evidence level]=Direct evidence [Evidence text]=The interacting monomers have been described to undergo mutual synergistic folding upon binding (PMID:11823864). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00348 covers 100% of the sequence present in the structure [Evidence chain B]=N/A [Similar structures]=MF2201001,MF2201003 [UniProt ID chain A]=P45481 [UniProt boundaries chain A]=2059-2116 [UniProt coverage chain A]=2% [Name chain A]=Histone lysine acetyltransferase CREBBP [UniProt sequence chain A]=MAENLLDGPPNPKRAKLSSPGFSANDNTDFGSLFDLENDLPDELIPNGELSLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSTNMASLGAMGKSPLNQGDSSTPNLPKQAASTSGPTPPASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPYPAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTGTTSPFGQPFSQTGGQQMGATGVNPQLASKQSMVNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGAGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPMSIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPEVKVEAKEEEENSSNDTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQNTALIAPHQIQGRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETPEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVNMSPAGFPNVARTQPPTIVSAGKPTNQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRANINNGMPPGRAGMGTPGSQMTPVGLNVPRPNQVSGPVMSSMPPGQWQQAPIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPGHNPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNSASLAGGMAGHSQFQQPQGPGGYAPAMQQQRMQQHLPIQGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSMDQGHLGNPEQSAMLPQLNTPNRSALSSELSLVGDTTGDTLEKFVEGL [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q15788 [UniProt boundaries chain B]=920-974 [UniProt coverage chain B]=3% [Name chain B]=Nuclear receptor coactivator 1 [UniProt sequence chain B]=MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSLSVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEALDGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNGVPWPQEATRRNSHTFNCRMLIHPPDEPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQSCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDTNSGMSIPRVNPSVNPSISPAHGVARSSTLPPSNSNMVSTRINRQQSSDLHSSSHSNSSNSQGSFGCSPGSQIVANVALNQGQASSQSSNPSLNLNNSPMEGTGISLAQFMSPRRQVTSGLATRPRMPNNSFPPNISTLSSPVGMTSSACNNNNRSYSNIPVTSLQGMNEGPNNSVGFSASSPVLRQMSSQNSPSRLNIQPAKAESKDNKEIASILNEMIQSDNSSSDGKPLDSGLLHNNDRLSDGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSCTGTSNSASANSSGGSCPSSHSSLTERHKILHRLLQEGSPSDITTLSVEPDKKDSASTSVSVTGQVQGNSSIKLELDASKKKESKDHQLLRYLLDKDEKDLRSTPNLSLDDVKVKVEKKEQMDPCNTNPTPMTKPTPEEIKLEAQSQFTADLDQFDQLLPTLEKAAQLPGLCETDRMDGAVTSVTIKSEILPASLQSATARPTSRLNRLPELELEAIDNQFGQPGTGDQIPWTNNTVTAINQSKSEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKLVQGGGLDVLSERFPPQQATPPLIMEERPNLYSQPYSSPSPTANLPSPFQGMVRQKPSLGTMPVQVTPPRGAFSPGMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLIHQNRQAILNQFAATAPVGINMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQLIQQQRAMLMRQQSFGNNLPPSSGLPVQMGNPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLANRNSMVSRGMTGNIGGQFGTGINPQMQQNVFQYPGAGMVPQGEANFAPSLSPGSSMVPMPIPPPQSSLLQQTPPASGYQSPDMKAWQQGAIGNNNVFSQAVQNQPTPAQPGVYNNMSITVSMAGGNTNVQNMNPMMAQMQMSSLQMPGMNTVCPEQINDPALRHTGLYCNQLSSTDLLKTEADGTQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF2201003 [Entry] [Entry number]=12 [Entry name]=YefM antitoxin (Mycobacterium tuberculosis) [PDB ID]=3cto [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin Phd/YefM [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into unfolded monomer species (PMID:20603017). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=P9WF25 [UniProt boundaries chain A]=1-68 [UniProt coverage chain A]=74% [Name chain A]=Antitoxin RelJ [UniProt sequence chain A]=MSISASEARQRLFPLIEQVNTDHQPVRITSRAGDAVLMSADDYDAWQETVYLLRSPENARRLMEAVARDKAGHSAFTKSVDELREMAGGEE [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WF25 [UniProt boundaries chain B]=2-84 [UniProt coverage chain B]=91% [Name chain B]=Antitoxin RelJ [UniProt sequence chain B]=MSISASEARQRLFPLIEQVNTDHQPVRITSRAGDAVLMSADDYDAWQETVYLLRSPENARRLMEAVARDKAGHSAFTKSVDELREMAGGEE [Source organism chain B]=Mycobacterium tuberculosis [UniProt ID chain C]=P9WF25 [UniProt boundaries chain C]=1-86 [UniProt coverage chain C]=94% [Name chain C]=Antitoxin RelJ [UniProt sequence chain C]=MSISASEARQRLFPLIEQVNTDHQPVRITSRAGDAVLMSADDYDAWQETVYLLRSPENARRLMEAVARDKAGHSAFTKSVDELREMAGGEE [Source organism chain C]=Mycobacterium tuberculosis [UniProt ID chain D]=P9WF25 [UniProt boundaries chain D]=2-66 [UniProt coverage chain D]=71% [Name chain D]=Antitoxin RelJ [UniProt sequence chain D]=MSISASEARQRLFPLIEQVNTDHQPVRITSRAGDAVLMSADDYDAWQETVYLLRSPENARRLMEAVARDKAGHSAFTKSVDELREMAGGEE [Source organism chain D]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Mycobacterium tuberculosis [Accession]=MF4120001 [Entry] [Entry number]=13 [Entry name]=Arc repressor [PDB ID]=1arq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Arc-like DNA binding domain [Evidence level]=Direct evidence [Evidence text]=The Arc repressor protein has been experimentally shown to be a molten globule in monomeric form (PMID:8446590,PMID:7696567). Adopting the proper three dimensional structure is linked to dimerization (PMID:8110744,PMID:10889040). The Mnt repressor shows a high degree of sequential and structural similarity with the Arc and MetJ repressors (PMID:7999761) that both have been shown to adopt a stable structure only via dimerization (PMID:8110744,PMID:1390748). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Similar structures]=MF7000013,MF2140011,MF2140001,MF7000011,MF7000015,MF7000012,MF7000014 [UniProt ID chain A]=P03050 [UniProt boundaries chain A]=1-53 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional repressor arc [UniProt sequence chain A]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain A]=Salmonella phage P22 [UniProt ID chain B]=P03050 [UniProt boundaries chain B]=1-53 [UniProt coverage chain B]=100% [Name chain B]=Transcriptional repressor arc [UniProt sequence chain B]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain B]=Salmonella phage P22 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella phage P22 [Accession]=MF2140001 [Entry] [Entry number]=15 [Entry name]=Transcriptional repressor CopG [PDB ID]=2cpg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Ribbon-helix-helix protein, copG family [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:9857196). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:9857196). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). Furthermore, CopG was directly shown to associate and fold cooperatively via a two state folding and binding process (PMID:9857196,PMID:15169951). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2120006,MF2120034,MF7000918 [UniProt ID chain A]=P13920 [UniProt boundaries chain A]=1-43 [UniProt coverage chain A]=95% [Name chain A]=Protein CopG [UniProt sequence chain A]=MKKRLTITLSESVLENLEKMAREMGLSKSAMISVALENYKKGQEK [Source organism chain A]=Streptococcus agalactiae [UniProt ID chain B]=P13920 [UniProt boundaries chain B]=1-45 [UniProt coverage chain B]=100% [Name chain B]=Protein CopG [UniProt sequence chain B]=MKKRLTITLSESVLENLEKMAREMGLSKSAMISVALENYKKGQEK [Source organism chain B]=Streptococcus agalactiae [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Streptococcus agalactiae [Accession]=MF2120006 [Entry] [Entry number]=16 [Entry name]=UmuD' protein filament [PDB ID]=1ay9 [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=According to the most probable oligomerization state stored in PDBe A-2,B chains were not considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00626 covers 100% of the sequence present in the structure [Evidence chain B-2]=The region(s) described in DP00626 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=P0AG11 [UniProt boundaries chain A]=32-139 [UniProt coverage chain A]=77% [Name chain A]=Protein UmuD [UniProt sequence chain A]=MLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR [Source organism chain A]=Escherichia coli [UniProt ID chain B-2]=P0AG11 [UniProt boundaries chain B-2]=32-139 [UniProt coverage chain B-2]=77% [Name chain B-2]=Protein UmuD [UniProt sequence chain B-2]=MLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR [Source organism chain B-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Escherichia coli [Accession]=MF2120007 [Entry] [Entry number]=17 [Entry name]=Transthyretin (human) [PDB ID]=3a4d [Chains]=A,B-2,B,A-2 [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Transthyretin-like folds [Subclass]=Transthyretin [Sequence domain]=HIUase/Transthyretin family [Evidence level]=Direct evidence [Evidence text]=Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain B-2]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF4110001,MF4110002,MF4120005,MF4120002,MF4110003,MF4100001,MF4120004 [UniProt ID chain A]=P02766 [UniProt boundaries chain A]=30-145 [UniProt coverage chain A]=78% [Name chain A]=Transthyretin [UniProt sequence chain A]=MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P02766 [UniProt boundaries chain B]=30-144 [UniProt coverage chain B]=78% [Name chain B]=Transthyretin [UniProt sequence chain B]=MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE [Source organism chain B]=Homo sapiens [UniProt ID chain B-2]=P02766 [UniProt boundaries chain B-2]=30-144 [UniProt coverage chain B-2]=78% [Name chain B-2]=Transthyretin [UniProt sequence chain B-2]=MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE [Source organism chain B-2]=Homo sapiens [UniProt ID chain A-2]=P02766 [UniProt boundaries chain A-2]=30-144 [UniProt coverage chain A-2]=78% [Name chain A-2]=Transthyretin [UniProt sequence chain A-2]=MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF4100001 [Entry] [Entry number]=18 [Entry name]=Transthyretin (rat) [PDB ID]=1gke [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Transthyretin-like folds [Subclass]=Transthyretin [Sequence domain]=HIUase/Transthyretin family [Evidence level]=Direct evidence [Evidence text]=Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF4110001,MF4110002,MF4120005,MF4120002,MF4110003,MF4100001,MF4120004 [UniProt ID chain A]=P02767 [UniProt boundaries chain A]=28-147 [UniProt coverage chain A]=81% [Name chain A]=Transthyretin [UniProt sequence chain A]=MASLRLFLLCLAGLIFASEAGPGGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTADGSWEPFASGKTAESGELHGLTTDEKFTEGVYRVELDTKSYWKALGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P02767 [UniProt boundaries chain B]=28-147 [UniProt coverage chain B]=81% [Name chain B]=Transthyretin [UniProt sequence chain B]=MASLRLFLLCLAGLIFASEAGPGGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTADGSWEPFASGKTAESGELHGLTTDEKFTEGVYRVELDTKSYWKALGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN [Source organism chain B]=Rattus norvegicus [UniProt ID chain C]=P02767 [UniProt boundaries chain C]=28-147 [UniProt coverage chain C]=81% [Name chain C]=Transthyretin [UniProt sequence chain C]=MASLRLFLLCLAGLIFASEAGPGGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTADGSWEPFASGKTAESGELHGLTTDEKFTEGVYRVELDTKSYWKALGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN [Source organism chain C]=Rattus norvegicus [UniProt ID chain D]=P02767 [UniProt boundaries chain D]=28-147 [UniProt coverage chain D]=81% [Name chain D]=Transthyretin [UniProt sequence chain D]=MASLRLFLLCLAGLIFASEAGPGGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTADGSWEPFASGKTAESGELHGLTTDEKFTEGVYRVELDTKSYWKALGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN [Source organism chain D]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Rattus norvegicus [Accession]=MF4110001 [Entry] [Entry number]=19 [Entry name]=Transthyretin (Sparus aurata) [PDB ID]=1oo2 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Transthyretin-like folds [Subclass]=Transthyretin [Sequence domain]=HIUase/Transthyretin family [Evidence level]=Direct evidence [Evidence text]=Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF4110001,MF4110002,MF4120005,MF4120002,MF4110003,MF4100001,MF4120004 [UniProt ID chain A]=Q9PTT3 [UniProt boundaries chain A]=33-148 [UniProt coverage chain A]=76% [Name chain A]=Transthyretin [UniProt sequence chain A]=MLQPLHCLLLASAVLLCNTAPTPTDKHGGSDTRCPLMVKILDAVKGTPAGSVALKVSQKTADGGWTQIATGVTDATGEIHNLITEQQFPAGVYRVEFDTKAYWTNQGSTPFHEVAEVVFDAHPEGHRHYTLALLLSPFSYTTTAVVSSVRE [Source organism chain A]=Sparus aurata [UniProt ID chain B]=Q9PTT3 [UniProt boundaries chain B]=33-148 [UniProt coverage chain B]=76% [Name chain B]=Transthyretin [UniProt sequence chain B]=MLQPLHCLLLASAVLLCNTAPTPTDKHGGSDTRCPLMVKILDAVKGTPAGSVALKVSQKTADGGWTQIATGVTDATGEIHNLITEQQFPAGVYRVEFDTKAYWTNQGSTPFHEVAEVVFDAHPEGHRHYTLALLLSPFSYTTTAVVSSVRE [Source organism chain B]=Sparus aurata [UniProt ID chain C]=Q9PTT3 [UniProt boundaries chain C]=33-148 [UniProt coverage chain C]=76% [Name chain C]=Transthyretin [UniProt sequence chain C]=MLQPLHCLLLASAVLLCNTAPTPTDKHGGSDTRCPLMVKILDAVKGTPAGSVALKVSQKTADGGWTQIATGVTDATGEIHNLITEQQFPAGVYRVEFDTKAYWTNQGSTPFHEVAEVVFDAHPEGHRHYTLALLLSPFSYTTTAVVSSVRE [Source organism chain C]=Sparus aurata [UniProt ID chain D]=Q9PTT3 [UniProt boundaries chain D]=33-148 [UniProt coverage chain D]=76% [Name chain D]=Transthyretin [UniProt sequence chain D]=MLQPLHCLLLASAVLLCNTAPTPTDKHGGSDTRCPLMVKILDAVKGTPAGSVALKVSQKTADGGWTQIATGVTDATGEIHNLITEQQFPAGVYRVEFDTKAYWTNQGSTPFHEVAEVVFDAHPEGHRHYTLALLLSPFSYTTTAVVSSVRE [Source organism chain D]=Sparus aurata [ExpTech]=X-ray [Resolution]=1.56 [Source organism]=Sparus aurata [Accession]=MF4110002 [Entry] [Entry number]=20 [Entry name]=Patj/Pals1 L27 domain complex (human/rat) [PDB ID]=1y76 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=L27 domains [Subclass]=L27_2/N type [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a heterotetrameric L27 complex (PMID:15863617). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=O55164 [UniProt boundaries chain A]=6-63 [UniProt coverage chain A]=2% [Name chain A]=Multiple PDZ domain protein [UniProt sequence chain A]=MLETIDKNRALQAAERLQSKLKERGDVANEDKLSLLKSVLQSPLFSQILSLQTSLQQLKDQVNVATLATANADHAHTPQFSSAIISNLQSESLLLSPSNGNLEAISGPGAPPAMDGKPACEELDQLIKSMAQGRHVEIFELLKPPCGGLGFSVVGLRSENRGELGIFVQEIQEGSVAHRDGRLKETDQILAINGQVLDQTITHQQAISILQKAKDTIQLVIARGSLPHISSPRISRSPSAASTVSAHSNPTHWQHVETIELVNDGSGLGFGIIGGKATGVIVKTILPGGVADQHGRLCSGDHILKIGDTDLAGMSSEQVAQVLRQCGNRVKLMIARGAVEETPAPSSLGITLSSSTSTSEMRVDASTQKNEESETFDVELTKNVQGLGITIAGYIGDKKLEPSGIFVKSITKSSAVELDGRIQIGDQIVAVDGTNLQGFTNQQAVEVLRHTGQTVRLTLMRKGASQEAEITSREDTAKDVDLPAENYEKDEESLSLKRSTSILPIEEEGYPLLSTELEETEDVQQEAALLTKWQRIMGINYEIVVAHVSKFSENSGLGISLEATVGHHFIRSVLPEGPVGHSGKLFSGDELLEVNGINLLGENHQDVVNILKELPIDVTMVCCRRTVPPTALSEVDSLDIHDLELTEKPHIDLGEFIGSSETEDPMLAMSDVDQNAEEIQTPLAMWEAGIQAIELEKGSRGLGFSILDYQDPIDPANTVIVIRSLVPGGIAEKDGRLFPGDRLMFVNDINLENSTLEEAVEALKGAPSGMVRIGVAKPLPLSPEEGYVSAKEDTFLCSPHTCKEMGLSDKALFRADLALIDTPDAESVAESRFESQFSPDNDSVYSTQASVLSLHDGACSDGMNYGPSLPSSPPKDVTNSSDLVLGLHLSLEELYTQNLLQRQHAGSPPTDMSPAATSGFTVSDYTPANAVEQKYECANTVAWTPSQLPSGLSTTELAPALPAVAPKYLTEQSSLVSDAESVTLQSMSQEAFERTVTIAKGSSSLGMTVSANKDGLGVIVRSIIHGGAISRDGRIAVGDCILSINEESTISLTNAQARAMLRRHSLIGPDIKITYVPAEHLEEFRVSFGQQAGGIMALDIFSSYTGRDIPELPEREEGEGEESELQNAAYSSWSQPRRVELWREPSKSLGISIVGGRGMGSRLSNGEVMRGIFIKHVLEDSPAGKNGTLKPGDRIVEVDGMDLRDASHEQAVEAIRKAGSPVVFMVQSIVNRPRKSPLPSLPHSLYPKCSFSSTNPFAESLQLTSDKAPSQSESESEKATLCSVPSSSPSVFSEMSSDYAQPSATTVAEDEDKEDEFGYSWKNIQERYGTLTGQLHMIELEKGHSGLGLSLAGNKDRTRMSVFIVGIDPTGAAGRDGRLQIADELLEINGQILYGRSHQNASSIIKCAPSKVKIIFIRNADAVNQMAVCPGSAADPLPSTSESPQNKEVEPSITTSASAVDLSSLTNVYHLELPKDQGGLGIAICEEDTLNGVTIKSLTERGGAAKDGRLKPGDRILAVDDELVAGCPIEKFISLLKTAKTTVKLTVGAENPGCQAVPSAAVTASGERKDSSQTPAVPAPDLEPIPSTSRSSTPAIFASDPATCPIIPGCETTIEISKGQTGLGLSIVGGSDTLLGAIIIHEVYEEGAACKDGRLWAGDQILEVNGIDLRKATHDEAINVLRQTPQRVRLTLYRDEAPYKEEDVCDTFTVELQKRPGKGLGLSIVGKRNDTGVFVSDIVKGGIADADGRLMQGDQILMVNGEDVRNATQEAVAALLKCSLGTVTLEVGRIKAAPFHSERRPSQSSQVSESSLSSFSLPRSGIHTSESSESSAKKNALASEIQGLRTVEIKKGPADALGLSIAGGVGSPLGDVPIFIAMMHPNGVAAQTQKLRVGDRIVTICGTSTDGMTHTQAVNLMKNASGSIEVQVVAGGDVSVVTGHQQELANPCLAFTGLTSSTIFPDDLGPPQSKTITLDRGPDGLGFSIVGGYGSPHGDLPIYVKTVFAKGAAAEDGRLKRGDQIIAVNGQSLEGVTHEEAVAILKRTKGTVTLMVLS [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=Q8N3R9 [UniProt boundaries chain B]=118-177 [UniProt coverage chain B]=8% [Name chain B]=Protein PALS1 [UniProt sequence chain B]=MTTSHMNGHVTEESDSEVKNVDLASPEEHQKHREMAVDCPGDLGTRMMPIRRSAQLERIRQQQEDMRRRREEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPMFDTEEGIVLESPHYAVKILEIEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNKDFQNAFKIHNAITVHMNKASPPFPLISNAQDLAQEVQTVLKPVHHKEGQELTALLNTPHIQALLLAHDKVAEQEMQLEPITDERVYESIGQYGGETVKIVRIEKARDIPLGATVRNEMDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMHGTLTFVLIPSQQIKPPPAKETVIHVKAHFDYDPSDDPYVPCRELGLSFQKGDILHVISQEDPNWWQAYREGDEDNQPLAGLVPGKSFQQQREAMKQTIEEDKEPEKSGKLWCAKKNKKKRKKVLYNANKNDDYDNEEILTYEEMSLYHQPANRKRPIILIGPQNCGQNELRQRLMNKEKDRFASAVPHTTRSRRDQEVAGRDYHFVSRQAFEADIAAGKFIEHGEFEKNLYGTSIDSVRQVINSGKICLLSLRTQSLKTLRNSDLKPYIIFIAPPSQERLRALLAKEGKNPKPEELREIIEKTREMEQNNGHYFDTAIVNSDLDKAYQELLRLINKLDTEPQWVPSTWLR [Source organism chain B]=Homo sapiens [UniProt ID chain C]=O55164 [UniProt boundaries chain C]=6-63 [UniProt coverage chain C]=2% [Name chain C]=Multiple PDZ domain protein [UniProt sequence chain C]=MLETIDKNRALQAAERLQSKLKERGDVANEDKLSLLKSVLQSPLFSQILSLQTSLQQLKDQVNVATLATANADHAHTPQFSSAIISNLQSESLLLSPSNGNLEAISGPGAPPAMDGKPACEELDQLIKSMAQGRHVEIFELLKPPCGGLGFSVVGLRSENRGELGIFVQEIQEGSVAHRDGRLKETDQILAINGQVLDQTITHQQAISILQKAKDTIQLVIARGSLPHISSPRISRSPSAASTVSAHSNPTHWQHVETIELVNDGSGLGFGIIGGKATGVIVKTILPGGVADQHGRLCSGDHILKIGDTDLAGMSSEQVAQVLRQCGNRVKLMIARGAVEETPAPSSLGITLSSSTSTSEMRVDASTQKNEESETFDVELTKNVQGLGITIAGYIGDKKLEPSGIFVKSITKSSAVELDGRIQIGDQIVAVDGTNLQGFTNQQAVEVLRHTGQTVRLTLMRKGASQEAEITSREDTAKDVDLPAENYEKDEESLSLKRSTSILPIEEEGYPLLSTELEETEDVQQEAALLTKWQRIMGINYEIVVAHVSKFSENSGLGISLEATVGHHFIRSVLPEGPVGHSGKLFSGDELLEVNGINLLGENHQDVVNILKELPIDVTMVCCRRTVPPTALSEVDSLDIHDLELTEKPHIDLGEFIGSSETEDPMLAMSDVDQNAEEIQTPLAMWEAGIQAIELEKGSRGLGFSILDYQDPIDPANTVIVIRSLVPGGIAEKDGRLFPGDRLMFVNDINLENSTLEEAVEALKGAPSGMVRIGVAKPLPLSPEEGYVSAKEDTFLCSPHTCKEMGLSDKALFRADLALIDTPDAESVAESRFESQFSPDNDSVYSTQASVLSLHDGACSDGMNYGPSLPSSPPKDVTNSSDLVLGLHLSLEELYTQNLLQRQHAGSPPTDMSPAATSGFTVSDYTPANAVEQKYECANTVAWTPSQLPSGLSTTELAPALPAVAPKYLTEQSSLVSDAESVTLQSMSQEAFERTVTIAKGSSSLGMTVSANKDGLGVIVRSIIHGGAISRDGRIAVGDCILSINEESTISLTNAQARAMLRRHSLIGPDIKITYVPAEHLEEFRVSFGQQAGGIMALDIFSSYTGRDIPELPEREEGEGEESELQNAAYSSWSQPRRVELWREPSKSLGISIVGGRGMGSRLSNGEVMRGIFIKHVLEDSPAGKNGTLKPGDRIVEVDGMDLRDASHEQAVEAIRKAGSPVVFMVQSIVNRPRKSPLPSLPHSLYPKCSFSSTNPFAESLQLTSDKAPSQSESESEKATLCSVPSSSPSVFSEMSSDYAQPSATTVAEDEDKEDEFGYSWKNIQERYGTLTGQLHMIELEKGHSGLGLSLAGNKDRTRMSVFIVGIDPTGAAGRDGRLQIADELLEINGQILYGRSHQNASSIIKCAPSKVKIIFIRNADAVNQMAVCPGSAADPLPSTSESPQNKEVEPSITTSASAVDLSSLTNVYHLELPKDQGGLGIAICEEDTLNGVTIKSLTERGGAAKDGRLKPGDRILAVDDELVAGCPIEKFISLLKTAKTTVKLTVGAENPGCQAVPSAAVTASGERKDSSQTPAVPAPDLEPIPSTSRSSTPAIFASDPATCPIIPGCETTIEISKGQTGLGLSIVGGSDTLLGAIIIHEVYEEGAACKDGRLWAGDQILEVNGIDLRKATHDEAINVLRQTPQRVRLTLYRDEAPYKEEDVCDTFTVELQKRPGKGLGLSIVGKRNDTGVFVSDIVKGGIADADGRLMQGDQILMVNGEDVRNATQEAVAALLKCSLGTVTLEVGRIKAAPFHSERRPSQSSQVSESSLSSFSLPRSGIHTSESSESSAKKNALASEIQGLRTVEIKKGPADALGLSIAGGVGSPLGDVPIFIAMMHPNGVAAQTQKLRVGDRIVTICGTSTDGMTHTQAVNLMKNASGSIEVQVVAGGDVSVVTGHQQELANPCLAFTGLTSSTIFPDDLGPPQSKTITLDRGPDGLGFSIVGGYGSPHGDLPIYVKTVFAKGAAAEDGRLKRGDQIIAVNGQSLEGVTHEEAVAILKRTKGTVTLMVLS [Source organism chain C]=Rattus norvegicus [UniProt ID chain D]=Q8N3R9 [UniProt boundaries chain D]=118-177 [UniProt coverage chain D]=8% [Name chain D]=Protein PALS1 [UniProt sequence chain D]=MTTSHMNGHVTEESDSEVKNVDLASPEEHQKHREMAVDCPGDLGTRMMPIRRSAQLERIRQQQEDMRRRREEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPMFDTEEGIVLESPHYAVKILEIEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNKDFQNAFKIHNAITVHMNKASPPFPLISNAQDLAQEVQTVLKPVHHKEGQELTALLNTPHIQALLLAHDKVAEQEMQLEPITDERVYESIGQYGGETVKIVRIEKARDIPLGATVRNEMDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMHGTLTFVLIPSQQIKPPPAKETVIHVKAHFDYDPSDDPYVPCRELGLSFQKGDILHVISQEDPNWWQAYREGDEDNQPLAGLVPGKSFQQQREAMKQTIEEDKEPEKSGKLWCAKKNKKKRKKVLYNANKNDDYDNEEILTYEEMSLYHQPANRKRPIILIGPQNCGQNELRQRLMNKEKDRFASAVPHTTRSRRDQEVAGRDYHFVSRQAFEADIAAGKFIEHGEFEKNLYGTSIDSVRQVINSGKICLLSLRTQSLKTLRNSDLKPYIIFIAPPSQERLRALLAKEGKNPKPEELREIIEKTREMEQNNGHYFDTAIVNSDLDKAYQELLRLINKLDTEPQWVPSTWLR [Source organism chain D]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Rattus norvegicus ;Homo sapiens [Accession]=MF4201001 [Entry] [Entry number]=21 [Entry name]=Patj/Pals1 L27 domain complex (human/mouse) [PDB ID]=1vf6 [Chains]=A,C [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=L27 domains [Subclass]=L27_2/N type [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a heterotetrameric L27 complex (PMID:15241471). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain C]=N/A [Similar structures]=None [UniProt ID chain A]=Q8NI35 [UniProt boundaries chain A]=12-67 [UniProt coverage chain A]=3% [Name chain A]=InaD-like protein [UniProt sequence chain A]=MPENPATDKLQVLQVLDRLKMKLQEKGDTSQNEKLSMFYETLKSPLFNQILTLQQSIKQLKGQLNHIPSDCSANFDFSRKGLLVFTDGSITNGNVHRPSNNSTVSGLFPWTPKLGNEDFNSVIQQMAQGRQIEYIDIERPSTGGLGFSVVALRSQNLGKVDIFVKDVQPGSVADRDQRLKENDQILAINHTPLDQNISHQQAIALLQQTTGSLRLIVAREPVHTKSSTSSSLNDTTLPETVCWGHVEEVELINDGSGLGFGIVGGKTSGVVVRTIVPGGLADRDGRLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSVRMLVARDPAGDISVTPPAPAALPVALPTVASKGPGSDSSLFETYNVELVRKDGQSLGIRIVGYVGTSHTGEASGIYVKSIIPGSAAYHNGHIQVNDKIVAVDGVNIQGFANHDVVEVLRNAGQVVHLTLVRRKTSSSTSPLEPPSDRGTVVEPLKPPALFLTGAVETETNVDGEDEEIKERIDTLKNDNIQALEKLEKVPDSPENELKSRWENLLGPDYEVMVATLDTQIADDAELQKYSKLLPIHTLRLGVEVDSFDGHHYISSIVSGGPVDTLGLLQPEDELLEVNGMQLYGKSRREAVSFLKEVPPPFTLVCCRRLFDDEASVDEPRRTETSLPETEVDHNMDVNTEEDDDGELALWSPEVKIVELVKDCKGLGFSILDYQDPLDPTRSVIVIRSLVADGVAERSGGLLPGDRLVSVNEYCLDNTSLAEAVEILKAVPPGLVHLGICKPLVEDNEEESCYILHSSSNEDKTEFSGTIHDINSSLILEAPKGFRDEPYFKEELVDEPFLDLGKSFHSQQKEIEQSKEAWEMHEFLTPRLQEMDEEREILVDEEYELYQDPSPSMELYPLSHIQEATPVPSVNELHFGTQWLHDNEPSESQEARTGRTVYSQEAQPYGYCPENVMKENFVMESLPSVPSTEGNSQQGRFDDLENLNSLAKTSLDLGMIPNDVQGPSLLIDLPVVAQRREQEDLPLYQHQATRVISKASAYTGMLSSRYATDTCELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAGKTNALKTGDKILEVSGVDLQNASHSEAVEAIKNAGNPVVFIVQSLSSTPRVIPNVHNKANKITGNQNQDTQEKKEKRQGTAPPPMKLPPPYKALTDDSDENEEEDAFTDQKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPEGPAAADGRMRIGDELLEINNQILYGRSHQNASAIIKTAPSKVKLVFIRNEDAVNQMAVTPFPVPSSSPSSIEDQSGTEPISSEEDGSVEVGIKQLPESESFKLAVSQMKQQKYPTKVSFSSQEIPLAPASSYHSTDADFTGYGGFQAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGKDTPLNAIVIHEVYEEGAAARDGRLWAGDQILEVNGVDLRNSSHEEAITALRQTPQKVRLVVYRDEAHYRDEENLEIFPVDLQKKAGRGLGLSIVGKRNGSGVFISDIVKGGAADLDGRLIQGDQILSVNGEDMRNASQETVATILKCAQGLVQLEIGRLRAGSWTSARTTSQNSQGSQQSAHSSCHPSFAPVITGLQNLVGTKRVSDPSQKNSGTDMEPRTVEINRELSDALGISIAGGRGSPLGDIPVFIAMIQASGVAARTQKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGRIILQVVADTNISAIAAQLENMSTGYHLGSPTAEHHPEDTEEQLQMTAD [Source organism chain A]=Homo sapiens [UniProt ID chain C]=Q9JLB2 [UniProt boundaries chain C]=123-170 [UniProt coverage chain C]=7% [Name chain C]=Protein PALS1 [UniProt sequence chain C]=MTTSYMNGHVTEESDSGIKNLDLASPEEYPKHREMAVDCPGDLGTRMMPVRRSAQLERIRQQQEDMRRRREEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPIFDTEEGIVLESPHYAVNILDVEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNRDFQNAFKIHNAVTVHMSKASPPFPLIANVQDLVQEVQTVLKPVHQKEGQELTALLNAPHIQALLLAHDKVAEQEMQLEPITDERVYESIGHYGGETVKIVRIEKARDIPLGATVRNEMDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMHGTLTFVLIPSQQIKPPPAKETVIHVKAHFDYDPSDDPYVPCRELGLSFQKGDILHVISQEDPNWWQAYREGDEDNQPLAGLVPGKSFQQQREAMKQTIEEDKEPEKSGKLWCAKKNKKKRKKVLYNANKNDDYDNEEILTYEEMSLYHQPANRKRPIILIGPQNCGQNELRQRLMNKEKDRFASAVPHTTRNRRDHEVAGRDYHFVSRQAFEADIAAGKFIEHGEFEKNLYGTSIDSVRQVINSGKICLLSLRTQSLKTLRNSDLKPYIIFIAPPSQERLRALLAKEGKNPKPEELREIIEKTREMEQNNGHYFDTAIVNSDLDKAYQELLRLINKLDTEPQWVPSTWLR [Source organism chain C]=Mus musculus [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF4201002 [Entry] [Entry number]=22 [Entry name]=L27 (Lin-2, Lin-7) domain complex (mouse) [PDB ID]=1y74 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=L27 domains [Subclass]=L27_1 type [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a heterotetrameric L27 complex (PMID:15863617). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=O88951 [UniProt boundaries chain A]=8-64 [UniProt coverage chain A]=27% [Name chain A]=Protein lin-7 homolog B [UniProt sequence chain A]=MAALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRVLQSRFCSAIREVYEQLYDTLDITGSAEVRAHATAKATVAAFTASEGHAHPRVVELPKTDEGLGFNIMGGKEQNSPIYISRVIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVRYTPRVLEEMEARFEKMRSARRRQQHHSYTSLESRG [Source organism chain A]=Mus musculus [UniProt ID chain B]=O70589 [UniProt boundaries chain B]=405-454 [UniProt coverage chain B]=5% [Name chain B]=Peripheral plasma membrane protein CASK [UniProt sequence chain B]=MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDVLQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY [Source organism chain B]=Mus musculus [UniProt ID chain C]=O88951 [UniProt boundaries chain C]=8-64 [UniProt coverage chain C]=27% [Name chain C]=Protein lin-7 homolog B [UniProt sequence chain C]=MAALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRVLQSRFCSAIREVYEQLYDTLDITGSAEVRAHATAKATVAAFTASEGHAHPRVVELPKTDEGLGFNIMGGKEQNSPIYISRVIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVRYTPRVLEEMEARFEKMRSARRRQQHHSYTSLESRG [Source organism chain C]=Mus musculus [UniProt ID chain D]=O70589 [UniProt boundaries chain D]=405-454 [UniProt coverage chain D]=5% [Name chain D]=Peripheral plasma membrane protein CASK [UniProt sequence chain D]=MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDVLQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY [Source organism chain D]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus [Accession]=MF4210002 [Entry] [Entry number]=23 [Entry name]=L27 (Lin-2, Lin-7) domain complex (human/C. elegans) [PDB ID]=1zl8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=L27 domains [Subclass]=L27_1 type [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form half of a heterotetrameric L27 complex (a dimer of dimers) (PMID:16147993). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01437 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01438 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=P90976 [UniProt boundaries chain A]=116-165 [UniProt coverage chain A]=16% [Name chain A]=LIN-7 [UniProt sequence chain A]=MGLKGFTGSFQQIRGLLRPPKNLPFRGIFRKDGEVVRKDDLLVNQFKMNYHPGLNVYYENDRGERLLRAHCDGIVRISQEKCDPDYEIEEMKGYEYRKDVDLYKMTFNMDNPDGPNLERDVQRILELMEHVQKTGEVNNAKLASLQQVLQSEFFGAVREVYETVYESIDADTTPEIKAAATAKATVAAFAAAEGHAHPRIVELPKTDQGLGFNVMGGKEQNSPIYISRIIPGGVADRHGGLKRGDQLIAVNGNVEAECHEKAVDLLKSAVGSVKLVIRYMPKLLDEMERRFERQRIP [Source organism chain A]=Caenorhabditis elegans [UniProt ID chain B]=O14936 [UniProt boundaries chain B]=403-456 [UniProt coverage chain B]=5% [Name chain B]=Peripheral plasma membrane protein CASK [UniProt sequence chain B]=MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDILQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Caenorhabditis elegans;Homo sapiens [Accession]=MF2201004 [Entry] [Entry number]=24 [Entry name]=HPV E7 oncoprotein CR3 domain [PDB ID]=2b9d [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Evidence suggests that the E7-CR3 domain would not be able to maintain this tertiary structure in monomeric form or in the absence of zinc coordination and is, therefore, likely to be an obligate and zinc-dependent dimer (PMID:16249186). This is consistent with solution studies showing that HPV-E7 undergoes a monomer-dimer equilibrium with a dissociation constant of about 1 μm (PMID:11123931). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P06465 [UniProt boundaries chain A]=44-93 [UniProt coverage chain A]=53% [Name chain A]=Protein E7 [UniProt sequence chain A]=MVGEMPALKDLVLQLEPSVLDLDLYCYEEVPPDDIEEELVSPQQPYAVVASCAYCEKLVRLTVLADHSAIRQLEELLLRSLNIVCPLCTLQRQ [Source organism chain A]=Human papillomavirus type 1 [UniProt ID chain A-2]=P06465 [UniProt boundaries chain A-2]=44-93 [UniProt coverage chain A-2]=53% [Name chain A-2]=Protein E7 [UniProt sequence chain A-2]=MVGEMPALKDLVLQLEPSVLDLDLYCYEEVPPDDIEEELVSPQQPYAVVASCAYCEKLVRLTVLADHSAIRQLEELLLRSLNIVCPLCTLQRQ [Source organism chain A-2]=Human papillomavirus type 1 [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Human papillomavirus type 1 [Accession]=MF2140002 [Entry] [Entry number]=25 [Entry name]=RhoA-binding domain in Rho-kinase [PDB ID]=1uix [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:12954645). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q28021 [UniProt boundaries chain A]=979-1045 [UniProt coverage chain A]=4% [Name chain A]=Rho-associated protein kinase 2 [UniProt sequence chain A]=MSRPPPTGKMPGAPEAVSGDGAGASRQRKLEALIRDPRSPINVESLLDGLNPLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFKNDQWNWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCKENDSIQSRKNEESQEIQKKLYTLEEHLSTEIQAKEELEQKCKSVNTRLEKVAKELEEEITLRKNVESTLRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSVLESERRDRTHGSEIINDLQGRISGLEEDVKNGKILLAKVELEKRQLQERFTDLEKEKNNMEIDMTYQLKVIQQSLEQEETEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLSEERTLKQKVENLLLEAEKRCSILDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLLEMKMSLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLCKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKEAQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDTEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS [Source organism chain A]=Bos taurus [UniProt ID chain B]=Q28021 [UniProt boundaries chain B]=979-1044 [UniProt coverage chain B]=4% [Name chain B]=Rho-associated protein kinase 2 [UniProt sequence chain B]=MSRPPPTGKMPGAPEAVSGDGAGASRQRKLEALIRDPRSPINVESLLDGLNPLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFKNDQWNWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCKENDSIQSRKNEESQEIQKKLYTLEEHLSTEIQAKEELEQKCKSVNTRLEKVAKELEEEITLRKNVESTLRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSVLESERRDRTHGSEIINDLQGRISGLEEDVKNGKILLAKVELEKRQLQERFTDLEKEKNNMEIDMTYQLKVIQQSLEQEETEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLSEERTLKQKVENLLLEAEKRCSILDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLLEMKMSLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLCKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKEAQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDTEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS [Source organism chain B]=Bos taurus [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Bos taurus [Accession]=MF2110001 [Entry] [Entry number]=26 [Entry name]=Trp repressor protein (Escherichia coli) [PDB ID]=3wrp [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Trp repressor-like [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The folding and dimerization of the Trp repressor were shown to be linked by both experimental (PMID:10329154,PMID:2223756,PMID:7578063) and computational studies (PMID:10465773). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P0A881 [UniProt boundaries chain A]=8-108 [UniProt coverage chain A]=93% [Name chain A]=Trp operon repressor [UniProt sequence chain A]=MAQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEELLRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLKSD [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P0A881 [UniProt boundaries chain A-2]=8-108 [UniProt coverage chain A-2]=93% [Name chain A-2]=Trp operon repressor [UniProt sequence chain A-2]=MAQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEELLRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLKSD [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Escherichia coli [Accession]=MF2120008 [Entry] [Entry number]=27 [Entry name]=Dimerization motif of Geminin [PDB ID]=1uii [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Geminin [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:15260975). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100003,MF2200002 [UniProt ID chain A]=O75496 [UniProt boundaries chain A]=92-152 [UniProt coverage chain A]=29% [Name chain A]=Geminin [UniProt sequence chain A]=MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O75496 [UniProt boundaries chain B]=92-152 [UniProt coverage chain B]=29% [Name chain B]=Geminin [UniProt sequence chain B]=MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF2100003 [Entry] [Entry number]=28 [Entry name]=GAL4 dimerization domain [PDB ID]=1hbw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:11316794). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P04386 [UniProt boundaries chain A]=50-106 [UniProt coverage chain A]=6% [Name chain A]=Regulatory protein GAL4 [UniProt sequence chain A]=MKLLSSIEQACDICRLKKLKCSKEKPKCAKCLKNNWECRYSPKTKRSPLTRAHLTEVESRLERLEQLFLLIFPREDLDMILKMDSLQDIKALLTGLFVQDNVNKDAVTDRLASVETDMPLTLRQHRISATSSSEESSNKGQRQLTVSIDSAAHHDNSTIPLDFMPRDALHGFDWSEEDDMSDGLPFLKTDPNNNGFFGDGSLLCILRSIGFKPENYTNSNVNRLPTMITDRYTLASRSTTSRLLQSYLNNFHPYCPIVHSPTLMMLYNNQIEIASKDQWQILFNCILAIGAWCIEGESTDIDVFYYQNAKSHLTSKVFESGSIILVTALHLLSRYTQWRQKTNTSYNFHSFSIRMAISLGLNRDLPSSFSDSSILEQRRRIWWSVYSWEIQLSLLYGRSIQLSQNTISFPSSVDDVQRTTTGPTIYHGIIETARLLQVFTKIYELDKTVTAEKSPICAKKCLMICNEIEEVSRQAPKFLQMDISTTALTNLLKEHPWLSFTRFELKWKQLSLIIYVLRDFFTNFTQKKSQLEQDQNDHQSYEVKRCSIMLSDAAQRTVMSVSSYMDNHNVTPYFAWNCSYYLFNAVLVPIKTLLSNSKSNAENNETAQLLQQINTVLMLLKKLATFKIQTCEKYIQVLEEVCAPFLLSQCAIPLPHISYNNSNGSAIKNIVGSATIAQYPTLPEENVNNISVKYVSPGSVGPSPVPLKSGASFSDLVKLLSNRPPSRNSPVTIPRSTPSHRSVTPFLGQQQQLQSLVPLTPSALFGGANFNQSGNIADSSLSFTFTNSSNGPNLITTQTNSQALSQPIASSNVHDNFMNNEITASKIDDGNNSKPLSPGWTDQTAYNAFGITTGMFNTTTMDDVYNYLFDDEDTPPNPKKE [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P04386 [UniProt boundaries chain B]=50-106 [UniProt coverage chain B]=6% [Name chain B]=Regulatory protein GAL4 [UniProt sequence chain B]=MKLLSSIEQACDICRLKKLKCSKEKPKCAKCLKNNWECRYSPKTKRSPLTRAHLTEVESRLERLEQLFLLIFPREDLDMILKMDSLQDIKALLTGLFVQDNVNKDAVTDRLASVETDMPLTLRQHRISATSSSEESSNKGQRQLTVSIDSAAHHDNSTIPLDFMPRDALHGFDWSEEDDMSDGLPFLKTDPNNNGFFGDGSLLCILRSIGFKPENYTNSNVNRLPTMITDRYTLASRSTTSRLLQSYLNNFHPYCPIVHSPTLMMLYNNQIEIASKDQWQILFNCILAIGAWCIEGESTDIDVFYYQNAKSHLTSKVFESGSIILVTALHLLSRYTQWRQKTNTSYNFHSFSIRMAISLGLNRDLPSSFSDSSILEQRRRIWWSVYSWEIQLSLLYGRSIQLSQNTISFPSSVDDVQRTTTGPTIYHGIIETARLLQVFTKIYELDKTVTAEKSPICAKKCLMICNEIEEVSRQAPKFLQMDISTTALTNLLKEHPWLSFTRFELKWKQLSLIIYVLRDFFTNFTQKKSQLEQDQNDHQSYEVKRCSIMLSDAAQRTVMSVSSYMDNHNVTPYFAWNCSYYLFNAVLVPIKTLLSNSKSNAENNETAQLLQQINTVLMLLKKLATFKIQTCEKYIQVLEEVCAPFLLSQCAIPLPHISYNNSNGSAIKNIVGSATIAQYPTLPEENVNNISVKYVSPGSVGPSPVPLKSGASFSDLVKLLSNRPPSRNSPVTIPRSTPSHRSVTPFLGQQQQLQSLVPLTPSALFGGANFNQSGNIADSSLSFTFTNSSNGPNLITTQTNSQALSQPIASSNVHDNFMNNEITASKIDDGNNSKPLSPGWTDQTAYNAFGITTGMFNTTTMDDVYNYLFDDEDTPPNPKKE [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharomyces cerevisiae [Accession]=MF2110002 [Entry] [Entry number]=29 [Entry name]=Spindle pole body component SPC42 [PDB ID]=2q6q [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:18850724). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P36094 [UniProt boundaries chain A]=67-128 [UniProt coverage chain A]=17% [Name chain A]=Spindle pole body component SPC42 [UniProt sequence chain A]=MNGSPTPKRYSSKSSRLYDDYYNIPYQYSNPTPMNRDYNDVGSRINADKLVPEEYKRNTEFINKAVQQNKELNFKLREKQNEIFELKKIAETLRSKLEKYVDITKKLEDQNLNLQIKISDLEKKLSDANSTFKEMRFPKVKDPMVDDDPVSENYDQINVPKHRAPDATGNPRTTNKVSNTSDQDSRLKAIERTLSVLTNYVMRSEDGNNDRMSPLPSPLNTILPINNRLNFQEPKRYNPTVKVNPSDDDIMMYESAELKRVEEEIEELKRKILVRKKHDLRKLSLNNQLQELQSMMDGDDNIKLDNVSKHNHATHRHSSQSSRDYSPSSDACLECSNDLYEKNRVKPENNMSETFATPTPNNR [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P36094 [UniProt boundaries chain B]=67-131 [UniProt coverage chain B]=17% [Name chain B]=Spindle pole body component SPC42 [UniProt sequence chain B]=MNGSPTPKRYSSKSSRLYDDYYNIPYQYSNPTPMNRDYNDVGSRINADKLVPEEYKRNTEFINKAVQQNKELNFKLREKQNEIFELKKIAETLRSKLEKYVDITKKLEDQNLNLQIKISDLEKKLSDANSTFKEMRFPKVKDPMVDDDPVSENYDQINVPKHRAPDATGNPRTTNKVSNTSDQDSRLKAIERTLSVLTNYVMRSEDGNNDRMSPLPSPLNTILPINNRLNFQEPKRYNPTVKVNPSDDDIMMYESAELKRVEEEIEELKRKILVRKKHDLRKLSLNNQLQELQSMMDGDDNIKLDNVSKHNHATHRHSSQSSRDYSPSSDACLECSNDLYEKNRVKPENNMSETFATPTPNNR [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=1.97 [Source organism]=Saccharomyces cerevisiae [Accession]=MF2110003 [Entry] [Entry number]=31 [Entry name]=Geminin:Idas coiled coil dimer [PDB ID]=4bry [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Geminin [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:24064211). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100003,MF2200002 [UniProt ID chain A]=O75496 [UniProt boundaries chain A]=92-160 [UniProt coverage chain A]=33% [Name chain A]=Geminin [UniProt sequence chain A]=MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI [Source organism chain A]=Homo sapiens [UniProt ID chain B]=D6RGH6 [UniProt boundaries chain B]=176-244 [UniProt coverage chain B]=17% [Name chain B]=Multicilin [UniProt sequence chain B]=MQACGGGAAGRRAFDSICPNRMLALPGRALLCKPGKPERKFAPPRKFFPGCTGGSPVSVYEDPPDAEPTALPALTTIDLQDLADCSSLLGSDAPPGGDLAASQNHSHQTEADFNLQDFRDTVDDLISDSSSMMSPTLASGDFPFSPCDISPFGPCLSPPLDPRALQSPPLRPPDVPPPEQYWKEVADQNQRALGDALVENNQLHVTLTQKQEEIASLKERNVQLKELASRTRHLASVLDKLMITQSRDCGAAAEPFLLKAKAKRSLEELVSAAGQDCAEVDAILREISERCDEALQSRDPKRPRLLPEPANTDTRPGNLHGAFRGLRTDCSRSALNLSHSELEEGGSFSTRIRSHSTIRTLAFPQGNAFTIRTANGGYKFRWVPS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.89 [Source organism]=Homo sapiens [Accession]=MF2200002 [Entry] [Entry number]=32 [Entry name]=Coiled-coil trigger site of the rod domain of cortexillin I [PDB ID]=1d7m [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:10745004). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q54HG2 [UniProt boundaries chain A]=243-343 [UniProt coverage chain A]=22% [Name chain A]=Cortexillin-1 [UniProt sequence chain A]=MAGKDWEIVQEKAFTAWVNSVLDKRGEKISDVGKDLSDGVKLIFFLELISSKKFNKKYDFEPKARINMIQNVALALKFLDEELKIKVQGIGSEDFVDNNKKMILGFLWTLYRKYRIAVISEGDKSSEEGLLLWCKNTTTGYDGVNITSFTKSFRDGLAFLALSHKFEPESFKFQEFEAMDPIARLNAAFDFAEKGLGVPKLLEAEEVMRGTTDERSLVLYTSLFFHAYRAKEEKARLESSKNEMANRLAGLENSLESEKVSREQLIKQKDQLNSLLASLESEGAEREKRLRELEAKLDETLKNLELEKLARMELEARLAKTEKDRAILELKLAEAIDEKSKLEQQIEATRIRGAAEAQGLGLLRKNLDTHVHDLLKWQKLTMENSSSSSIDDQIIVEVSGLPFGEQVKHLATKLEAENLAIMKLLNQKEDDLKAQKLKSSKSKK [Source organism chain A]=Dictyostelium discoideum [UniProt ID chain B]=Q54HG2 [UniProt boundaries chain B]=243-343 [UniProt coverage chain B]=22% [Name chain B]=Cortexillin-1 [UniProt sequence chain B]=MAGKDWEIVQEKAFTAWVNSVLDKRGEKISDVGKDLSDGVKLIFFLELISSKKFNKKYDFEPKARINMIQNVALALKFLDEELKIKVQGIGSEDFVDNNKKMILGFLWTLYRKYRIAVISEGDKSSEEGLLLWCKNTTTGYDGVNITSFTKSFRDGLAFLALSHKFEPESFKFQEFEAMDPIARLNAAFDFAEKGLGVPKLLEAEEVMRGTTDERSLVLYTSLFFHAYRAKEEKARLESSKNEMANRLAGLENSLESEKVSREQLIKQKDQLNSLLASLESEGAEREKRLRELEAKLDETLKNLELEKLARMELEARLAKTEKDRAILELKLAEAIDEKSKLEQQIEATRIRGAAEAQGLGLLRKNLDTHVHDLLKWQKLTMENSSSSSIDDQIIVEVSGLPFGEQVKHLATKLEAENLAIMKLLNQKEDDLKAQKLKSSKSKK [Source organism chain B]=Dictyostelium discoideum [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Dictyostelium discoideum [Accession]=MF2110004 [Entry] [Entry number]=33 [Entry name]=Cell division factor ZapA [PDB ID]=4p1m [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=According to the most probable oligomerization state stored in PDBe A-2,B chains were not considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Cell division protein ZapA [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:25002581). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=MF2120010,MF2120012 [UniProt ID chain A]=P0ADS2 [UniProt boundaries chain A]=4-109 [UniProt coverage chain A]=97% [Name chain A]=Cell division protein ZapA [UniProt sequence chain A]=MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLEQGRITEKTNQNFE [Source organism chain A]=Escherichia coli [UniProt ID chain B-2]=P0ADS2 [UniProt boundaries chain B-2]=2-109 [UniProt coverage chain B-2]=99% [Name chain B-2]=Cell division protein ZapA [UniProt sequence chain B-2]=MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLEQGRITEKTNQNFE [Source organism chain B-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Escherichia coli [Accession]=MF2120010 [Entry] [Entry number]=34 [Entry name]=Cell division factor ZapB [PDB ID]=2jee [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:18394147). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P0AF36 [UniProt boundaries chain A]=3-81 [UniProt coverage chain A]=97% [Name chain A]=Cell division protein ZapB [UniProt sequence chain A]=MTMSLEVFEKLEAKVQQAIDTITLLQMEIEELKEKNNSLSQEVQNAQHQREELERENNHLKEQQNGWQERLQALLGRMEEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AF36 [UniProt boundaries chain B]=3-81 [UniProt coverage chain B]=97% [Name chain B]=Cell division protein ZapB [UniProt sequence chain B]=MTMSLEVFEKLEAKVQQAIDTITLLQMEIEELKEKNNSLSQEVQNAQHQREELERENNHLKEQQNGWQERLQALLGRMEEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Escherichia coli [Accession]=MF2120011 [Entry] [Entry number]=35 [Entry name]=Autophagy protein 16 [PDB ID]=3a7o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Autophagy protein 16 (ATG16) [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:19889643). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110005,MF7000153 [UniProt ID chain A]=Q03818 [UniProt boundaries chain A]=60-118 [UniProt coverage chain A]=39% [Name chain A]=Autophagy protein 16 [UniProt sequence chain A]=MGNFIITERKKAKEERSNPQTDSMDDLLIRRLTDRNDKEAHLNELFQDNSGAIGGNIVSHDDALLNTLAILQKELKSKEQEIRRLKEVIALKNKNTERLNDELISGTIENNVLQQKLSDLKKEHSQLVARWLKKTEKETEAMNSEIDGTK [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=Q03818 [UniProt boundaries chain B]=61-114 [UniProt coverage chain B]=36% [Name chain B]=Autophagy protein 16 [UniProt sequence chain B]=MGNFIITERKKAKEERSNPQTDSMDDLLIRRLTDRNDKEAHLNELFQDNSGAIGGNIVSHDDALLNTLAILQKELKSKEQEIRRLKEVIALKNKNTERLNDELISGTIENNVLQQKLSDLKKEHSQLVARWLKKTEKETEAMNSEIDGTK [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Saccharomyces cerevisiae [Accession]=MF2110005 [Entry] [Entry number]=36 [Entry name]=Assembly domain of cartilage oligomeric matrix protein (chicken) [PDB ID]=1aq5 [Chains]=A,B,C [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (trimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:9699631). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Similar structures]=None [UniProt ID chain A]=P05099 [UniProt boundaries chain A]=450-493 [UniProt coverage chain A]=8% [Name chain A]=Cartilage matrix protein [UniProt sequence chain A]=MDGIFCALPLSLLLLLQSCGVWGAPPQPRGTLCRTKPTDLVFIIDSSRSVRPQEFEKVKVFLSRVIEGLDVGPNSTRVGVINYASAVKNEFSLKTHQTKAELLQAVQRIEPLSTGTMTGLAIQFAISRAFSDTEGARLRSPNINKVAIVVTDGRPQDGVQDVSARARQAGIEIFAIGVGRVDMHTLRQIASEPLDDHVDYVESYSVIEKLTHKFQEAFCVVSDLCATGDHDCEQICISTPGSYKCACKEGFTLNNDGKTCSACSGGSGSALDLVFLIDGSKSVRPENFELVKKFINQIVESLEVSEKQAQVGLVQYSSSVRQEFPLGQFKNKKDIKAAVKKMAYMEKGTMTGQALKYLVDSSFSIANGARPGVPKVGIVFTDGRSQDYITDAAKKAKDLGFRMFAVGVGNAVEDELREIASEPVAEHYFYTADFRTISNIGKKLQMKICVEEDPCECKSIVKFQTKVEELINTLQQKLEAVAKRIEALENKII [Source organism chain A]=Gallus gallus [UniProt ID chain B]=P05099 [UniProt boundaries chain B]=450-493 [UniProt coverage chain B]=8% [Name chain B]=Cartilage matrix protein [UniProt sequence chain B]=MDGIFCALPLSLLLLLQSCGVWGAPPQPRGTLCRTKPTDLVFIIDSSRSVRPQEFEKVKVFLSRVIEGLDVGPNSTRVGVINYASAVKNEFSLKTHQTKAELLQAVQRIEPLSTGTMTGLAIQFAISRAFSDTEGARLRSPNINKVAIVVTDGRPQDGVQDVSARARQAGIEIFAIGVGRVDMHTLRQIASEPLDDHVDYVESYSVIEKLTHKFQEAFCVVSDLCATGDHDCEQICISTPGSYKCACKEGFTLNNDGKTCSACSGGSGSALDLVFLIDGSKSVRPENFELVKKFINQIVESLEVSEKQAQVGLVQYSSSVRQEFPLGQFKNKKDIKAAVKKMAYMEKGTMTGQALKYLVDSSFSIANGARPGVPKVGIVFTDGRSQDYITDAAKKAKDLGFRMFAVGVGNAVEDELREIASEPVAEHYFYTADFRTISNIGKKLQMKICVEEDPCECKSIVKFQTKVEELINTLQQKLEAVAKRIEALENKII [Source organism chain B]=Gallus gallus [UniProt ID chain C]=P05099 [UniProt boundaries chain C]=450-493 [UniProt coverage chain C]=8% [Name chain C]=Cartilage matrix protein [UniProt sequence chain C]=MDGIFCALPLSLLLLLQSCGVWGAPPQPRGTLCRTKPTDLVFIIDSSRSVRPQEFEKVKVFLSRVIEGLDVGPNSTRVGVINYASAVKNEFSLKTHQTKAELLQAVQRIEPLSTGTMTGLAIQFAISRAFSDTEGARLRSPNINKVAIVVTDGRPQDGVQDVSARARQAGIEIFAIGVGRVDMHTLRQIASEPLDDHVDYVESYSVIEKLTHKFQEAFCVVSDLCATGDHDCEQICISTPGSYKCACKEGFTLNNDGKTCSACSGGSGSALDLVFLIDGSKSVRPENFELVKKFINQIVESLEVSEKQAQVGLVQYSSSVRQEFPLGQFKNKKDIKAAVKKMAYMEKGTMTGQALKYLVDSSFSIANGARPGVPKVGIVFTDGRSQDYITDAAKKAKDLGFRMFAVGVGNAVEDELREIASEPVAEHYFYTADFRTISNIGKKLQMKICVEEDPCECKSIVKFQTKVEELINTLQQKLEAVAKRIEALENKII [Source organism chain C]=Gallus gallus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Gallus gallus [Accession]=MF3110001 [Entry] [Entry number]=37 [Entry name]=Bacteriophage T4 fibritin [PDB ID]=1aa0 [Chains]=A-3,A,A-2 [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Coiled coil/foldon domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The foldon domain folds into a trimeric beta-propeller structure and undergoes a two-state unfolding transition from folded trimer to unfolded monomers (PMID:15033360). The other subunits in the structure are bound via coiled coil interactions (PMID:9261070). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-3]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P10104 [UniProt boundaries chain A]=372-484 [UniProt coverage chain A]=23% [Name chain A]=Fibritin [UniProt sequence chain A]=MTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA [Source organism chain A]=Enterobacteria phage T4 [UniProt ID chain A-3]=P10104 [UniProt boundaries chain A-3]=372-484 [UniProt coverage chain A-3]=23% [Name chain A-3]=Fibritin [UniProt sequence chain A-3]=MTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA [Source organism chain A-3]=Enterobacteria phage T4 [UniProt ID chain A-2]=P10104 [UniProt boundaries chain A-2]=372-484 [UniProt coverage chain A-2]=23% [Name chain A-2]=Fibritin [UniProt sequence chain A-2]=MTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA [Source organism chain A-2]=Enterobacteria phage T4 [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Enterobacteria phage T4 [Accession]=MF3140001 [Entry] [Entry number]=38 [Entry name]=Trimerization domain from lung surfactant protein D [PDB ID]=1m7l [Chains]=A,B,C [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (trimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:12495025). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Similar structures]=None [UniProt ID chain A]=P35247 [UniProt boundaries chain A]=220-257 [UniProt coverage chain A]=10% [Name chain A]=Pulmonary surfactant-associated protein D [UniProt sequence chain A]=MLLFLLSALVLLTQPLGYLEAEMKTYSHRTMPSACTLVMCSSVESGLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEF [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P35247 [UniProt boundaries chain B]=220-257 [UniProt coverage chain B]=10% [Name chain B]=Pulmonary surfactant-associated protein D [UniProt sequence chain B]=MLLFLLSALVLLTQPLGYLEAEMKTYSHRTMPSACTLVMCSSVESGLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEF [Source organism chain B]=Homo sapiens [UniProt ID chain C]=P35247 [UniProt boundaries chain C]=220-257 [UniProt coverage chain C]=10% [Name chain C]=Pulmonary surfactant-associated protein D [UniProt sequence chain C]=MLLFLLSALVLLTQPLGYLEAEMKTYSHRTMPSACTLVMCSSVESGLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEF [Source organism chain C]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF3100001 [Entry] [Entry number]=39 [Entry name]=Major outer membrane lipoprotein [PDB ID]=1jcc [Chains]=A,B,C [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Alanine zipper (trimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:12741822). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Similar structures]=None [UniProt ID chain A]=P69776 [UniProt boundaries chain A]=22-72 [UniProt coverage chain A]=65% [Name chain A]=Major outer membrane lipoprotein Lpp [UniProt sequence chain A]=MKATKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P69776 [UniProt boundaries chain B]=22-73 [UniProt coverage chain B]=66% [Name chain B]=Major outer membrane lipoprotein Lpp [UniProt sequence chain B]=MKATKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK [Source organism chain B]=Escherichia coli [UniProt ID chain C]=P69776 [UniProt boundaries chain C]=22-74 [UniProt coverage chain C]=67% [Name chain C]=Major outer membrane lipoprotein Lpp [UniProt sequence chain C]=MKATKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK [Source organism chain C]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Escherichia coli [Accession]=MF3120001 [Entry] [Entry number]=40 [Entry name]=DUF16 domain of MPN010 (Mycoplasma pneumoniae) [PDB ID]=2ba2 [Chains]=A,B,C [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (trimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:16522803). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Similar structures]=None [UniProt ID chain A]=P75103 [UniProt boundaries chain A]=50-130 [UniProt coverage chain A]=61% [Name chain A]=UPF0134 protein MPN_010 [UniProt sequence chain A]=MAYSPSLNDIKSILNKYTSKDYELKCENRYDGKLELWLKGVFEEIVKTPGTRYVTHKQLDEKLKNFVTKTEFKEFQTVVMESFAVQNQNIDAQGEQIKELQVEQKAQGKTLQLILEALQGINKRLDNLESK [Source organism chain A]= [UniProt ID chain B]=P75103 [UniProt boundaries chain B]=51-130 [UniProt coverage chain B]=61% [Name chain B]=UPF0134 protein MPN_010 [UniProt sequence chain B]=MAYSPSLNDIKSILNKYTSKDYELKCENRYDGKLELWLKGVFEEIVKTPGTRYVTHKQLDEKLKNFVTKTEFKEFQTVVMESFAVQNQNIDAQGEQIKELQVEQKAQGKTLQLILEALQGINKRLDNLESK [Source organism chain B]= [UniProt ID chain C]=P75103 [UniProt boundaries chain C]=50-130 [UniProt coverage chain C]=61% [Name chain C]=UPF0134 protein MPN_010 [UniProt sequence chain C]=MAYSPSLNDIKSILNKYTSKDYELKCENRYDGKLELWLKGVFEEIVKTPGTRYVTHKQLDEKLKNFVTKTEFKEFQTVVMESFAVQNQNIDAQGEQIKELQVEQKAQGKTLQLILEALQGINKRLDNLESK [Source organism chain C]= [ExpTech]=X-ray [Resolution]=1.80 [Source organism]= [Accession]=MF3120002 [Entry] [Entry number]=41 [Entry name]=Dystrophia myotonin-protein kinase coiled-coil domain [PDB ID]=1wt6 [Chains]=A,B,D [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (trimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:16770013). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=Q09013 [UniProt boundaries chain A]=465-529 [UniProt coverage chain A]=10% [Name chain A]=Myotonin-protein kinase [UniProt sequence chain A]=MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q09013 [UniProt boundaries chain B]=461-527 [UniProt coverage chain B]=10% [Name chain B]=Myotonin-protein kinase [UniProt sequence chain B]=MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP [Source organism chain B]=Homo sapiens [UniProt ID chain D]=Q09013 [UniProt boundaries chain D]=465-527 [UniProt coverage chain D]=10% [Name chain D]=Myotonin-protein kinase [UniProt sequence chain D]=MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Homo sapiens [Accession]=MF3100002 [Entry] [Entry number]=42 [Entry name]=Gene V protein [PDB ID]=1gvp [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Reversible denaturation experiments have shown that the dimeric gene V protein unfolds in a single cooperative transition from a folded dimer into two unfolded monomers (PMID:2007116). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P69543 [UniProt boundaries chain A]=1-87 [UniProt coverage chain A]=100% [Name chain A]=DNA-Binding protein G5P [UniProt sequence chain A]=MIKVEIKPSQAQFTTRSGVSRQGKPYSLNEQLCYVDLGNEYPVLVKITLDEGQPAYAPGLYTVHLSSFKVGQFGSLMIDRLRLVPAK [Source organism chain A]=Enterobacteria phage f1 [UniProt ID chain A-2]=P69543 [UniProt boundaries chain A-2]=1-87 [UniProt coverage chain A-2]=100% [Name chain A-2]=DNA-Binding protein G5P [UniProt sequence chain A-2]=MIKVEIKPSQAQFTTRSGVSRQGKPYSLNEQLCYVDLGNEYPVLVKITLDEGQPAYAPGLYTVHLSSFKVGQFGSLMIDRLRLVPAK [Source organism chain A-2]=Enterobacteria phage f1 [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Enterobacteria phage f1 [Accession]=MF2140003 [Entry] [Entry number]=43 [Entry name]=Bacteriophage f29 scaffolding protein gp7 [PDB ID]=1no4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:12778115). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P13848 [UniProt boundaries chain A]=2-78 [UniProt coverage chain A]=78% [Name chain A]=Capsid assembly scaffolding protein [UniProt sequence chain A]=MPLKPEEHEDILNKLLDPELAQSERTEALQQLRVNYGSFVSEYNDLTKSHEKLAAEKDDLIVSNSKLFRQIGLTDKQEEDHKKADISETITIEDLEAK [Source organism chain A]=Bacillus phage phi29 [UniProt ID chain B]=P13848 [UniProt boundaries chain B]=2-76 [UniProt coverage chain B]=76% [Name chain B]=Capsid assembly scaffolding protein [UniProt sequence chain B]=MPLKPEEHEDILNKLLDPELAQSERTEALQQLRVNYGSFVSEYNDLTKSHEKLAAEKDDLIVSNSKLFRQIGLTDKQEEDHKKADISETITIEDLEAK [Source organism chain B]=Bacillus phage phi29 [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Bacillus phage phi29 [Accession]=MF2140004 [Entry] [Entry number]=44 [Entry name]=Tetrabrachion tetramerization region [PDB ID]=1fe6 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:10966648). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=Q54436 [UniProt boundaries chain A]=1238-1286 [UniProt coverage chain A]=3% [Name chain A]=Tetrabrachion [UniProt sequence chain A]=MNRVLAYSLLAIMTLSLLIIPAPGIAQRITVGVSVKAGTYNFYNITPTTQTVEVTDNGMLRVIINRTEATELGTTIRLAFILDTDKYDPNVGGYFLNVSNIGVYAPSDPTQSPYGGVIDITQNSTLTDGTQVVGNVTVVNGGNNVIILIDLSKLPDLQNVVYITNVYTETSTTANLTNTLLRVKAFDAASWDAVISGNQFKILYIPSLCKYVKINVIHSPAIVGTNVDVIVSFHKYFSLVQSIAGVSLDITVDNKTQLNMTNYYNATENYVLATFINGNLTVGGSEVFSSPTVTVINASTFKYSGQVKDYAPTVADTATPWVRTLNKFEVEFRHEIVNXTHDLIFYIHCDSDTVSYDTWPFLIVNASLDITTTEVAFNSTTINPGDIVNFTAHNVPLQYLTATNYGVLRFQLINPALVVYVPVSNMTLSANTTTGIINGSFVLPDAPYGGLDYLTYLVFNDGKFIANGYITVSPCIETYVLTNTSAYAEDAGSSYIGRFVPGYTSVPGDYIVIKGYGFALSNLTGFTVSINNTDVIILNATYNASTGKIIILAKLLDTNGTPIPVGAGFIRVGQNGTTNIAYAPFNVTRNSGLEKVLFNPRWFYNGTYYIEHDKLGDPYLYFPVDYPLVNNTFTTEMWPFNTTIEVIGWPTNTFTLKAFNKEFNLSFNLLTLSLTNGYNMTNLYNLTIPFLPYGNYTLLEGTLLSVNNRTVFTVHMGINVDLDSCGNGTLSITVVGAAPNTEYNFTFGYQVHDLNYGITRYISPQWNGTWNISLVTDIYGTGSTSVPLITLYPTSYVINATWDVITWLRLSGSGTLDLLFSVDVSYNGFTDNLTTPITYVFGPSDTTPGSFNIYVNTTYNVSVVRVAVDYLPRTNVVISVPETVLPGDTITVQIFPHHNEVWGFIEPTALFDENQLLGWYLTVRLVDPLSNTVVERVAGYYAGNLIVEDVDGDGDNEVWFVVNLTAPLVLGVDKTYRVDVELFLAVLNPSSNITGVTAVDNECYVQLDLNGTIYWNGLGSGIMLGGDGQIVTVLGVLEGKLDTIKDGIAEINATVNDINTYLKVNVTDLLKTINNSVVMIKNDTATLIIGQAEIKAKLDDLLNLTSQVNDTVTMILACCNNASKVLNRMEGTLNSTYTGVLNVKSDLSTLIDTANNVVIPKFNELYDNVTVEINASRDLIIQKISSVNDSLTTIISAGFNDVEAMISNLNTTLLNRIDELEGTLLFYMTANEQRLEGIINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILASIGNVNLTVFNKLNDLEIELGDVNATINAGIFQIQSNLGNANQLILDTLTSSKVEILNAISSNASAISSEIHNAVNQLSTLVLQVNDTLTLKITGEADNILNFLSSLEGSMNTGFNNVTSTLSAVENNILGKITDTSNLLSSKIDNTLSTLQDLITSTSNDLKNSISSAKNDIVSSLSSKVDSSTQTLSTKLDDLKSAQESNTNSINNNIMLFGAASLILLIVTIGLVGYRLIARRRVG [Source organism chain A]=Staphylothermus marinus [UniProt ID chain B]=Q54436 [UniProt boundaries chain B]=1238-1286 [UniProt coverage chain B]=3% [Name chain B]=Tetrabrachion [UniProt sequence chain B]=MNRVLAYSLLAIMTLSLLIIPAPGIAQRITVGVSVKAGTYNFYNITPTTQTVEVTDNGMLRVIINRTEATELGTTIRLAFILDTDKYDPNVGGYFLNVSNIGVYAPSDPTQSPYGGVIDITQNSTLTDGTQVVGNVTVVNGGNNVIILIDLSKLPDLQNVVYITNVYTETSTTANLTNTLLRVKAFDAASWDAVISGNQFKILYIPSLCKYVKINVIHSPAIVGTNVDVIVSFHKYFSLVQSIAGVSLDITVDNKTQLNMTNYYNATENYVLATFINGNLTVGGSEVFSSPTVTVINASTFKYSGQVKDYAPTVADTATPWVRTLNKFEVEFRHEIVNXTHDLIFYIHCDSDTVSYDTWPFLIVNASLDITTTEVAFNSTTINPGDIVNFTAHNVPLQYLTATNYGVLRFQLINPALVVYVPVSNMTLSANTTTGIINGSFVLPDAPYGGLDYLTYLVFNDGKFIANGYITVSPCIETYVLTNTSAYAEDAGSSYIGRFVPGYTSVPGDYIVIKGYGFALSNLTGFTVSINNTDVIILNATYNASTGKIIILAKLLDTNGTPIPVGAGFIRVGQNGTTNIAYAPFNVTRNSGLEKVLFNPRWFYNGTYYIEHDKLGDPYLYFPVDYPLVNNTFTTEMWPFNTTIEVIGWPTNTFTLKAFNKEFNLSFNLLTLSLTNGYNMTNLYNLTIPFLPYGNYTLLEGTLLSVNNRTVFTVHMGINVDLDSCGNGTLSITVVGAAPNTEYNFTFGYQVHDLNYGITRYISPQWNGTWNISLVTDIYGTGSTSVPLITLYPTSYVINATWDVITWLRLSGSGTLDLLFSVDVSYNGFTDNLTTPITYVFGPSDTTPGSFNIYVNTTYNVSVVRVAVDYLPRTNVVISVPETVLPGDTITVQIFPHHNEVWGFIEPTALFDENQLLGWYLTVRLVDPLSNTVVERVAGYYAGNLIVEDVDGDGDNEVWFVVNLTAPLVLGVDKTYRVDVELFLAVLNPSSNITGVTAVDNECYVQLDLNGTIYWNGLGSGIMLGGDGQIVTVLGVLEGKLDTIKDGIAEINATVNDINTYLKVNVTDLLKTINNSVVMIKNDTATLIIGQAEIKAKLDDLLNLTSQVNDTVTMILACCNNASKVLNRMEGTLNSTYTGVLNVKSDLSTLIDTANNVVIPKFNELYDNVTVEINASRDLIIQKISSVNDSLTTIISAGFNDVEAMISNLNTTLLNRIDELEGTLLFYMTANEQRLEGIINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILASIGNVNLTVFNKLNDLEIELGDVNATINAGIFQIQSNLGNANQLILDTLTSSKVEILNAISSNASAISSEIHNAVNQLSTLVLQVNDTLTLKITGEADNILNFLSSLEGSMNTGFNNVTSTLSAVENNILGKITDTSNLLSSKIDNTLSTLQDLITSTSNDLKNSISSAKNDIVSSLSSKVDSSTQTLSTKLDDLKSAQESNTNSINNNIMLFGAASLILLIVTIGLVGYRLIARRRVG [Source organism chain B]=Staphylothermus marinus [UniProt ID chain C]=Q54436 [UniProt boundaries chain C]=1239-1286 [UniProt coverage chain C]=3% [Name chain C]=Tetrabrachion [UniProt sequence chain C]=MNRVLAYSLLAIMTLSLLIIPAPGIAQRITVGVSVKAGTYNFYNITPTTQTVEVTDNGMLRVIINRTEATELGTTIRLAFILDTDKYDPNVGGYFLNVSNIGVYAPSDPTQSPYGGVIDITQNSTLTDGTQVVGNVTVVNGGNNVIILIDLSKLPDLQNVVYITNVYTETSTTANLTNTLLRVKAFDAASWDAVISGNQFKILYIPSLCKYVKINVIHSPAIVGTNVDVIVSFHKYFSLVQSIAGVSLDITVDNKTQLNMTNYYNATENYVLATFINGNLTVGGSEVFSSPTVTVINASTFKYSGQVKDYAPTVADTATPWVRTLNKFEVEFRHEIVNXTHDLIFYIHCDSDTVSYDTWPFLIVNASLDITTTEVAFNSTTINPGDIVNFTAHNVPLQYLTATNYGVLRFQLINPALVVYVPVSNMTLSANTTTGIINGSFVLPDAPYGGLDYLTYLVFNDGKFIANGYITVSPCIETYVLTNTSAYAEDAGSSYIGRFVPGYTSVPGDYIVIKGYGFALSNLTGFTVSINNTDVIILNATYNASTGKIIILAKLLDTNGTPIPVGAGFIRVGQNGTTNIAYAPFNVTRNSGLEKVLFNPRWFYNGTYYIEHDKLGDPYLYFPVDYPLVNNTFTTEMWPFNTTIEVIGWPTNTFTLKAFNKEFNLSFNLLTLSLTNGYNMTNLYNLTIPFLPYGNYTLLEGTLLSVNNRTVFTVHMGINVDLDSCGNGTLSITVVGAAPNTEYNFTFGYQVHDLNYGITRYISPQWNGTWNISLVTDIYGTGSTSVPLITLYPTSYVINATWDVITWLRLSGSGTLDLLFSVDVSYNGFTDNLTTPITYVFGPSDTTPGSFNIYVNTTYNVSVVRVAVDYLPRTNVVISVPETVLPGDTITVQIFPHHNEVWGFIEPTALFDENQLLGWYLTVRLVDPLSNTVVERVAGYYAGNLIVEDVDGDGDNEVWFVVNLTAPLVLGVDKTYRVDVELFLAVLNPSSNITGVTAVDNECYVQLDLNGTIYWNGLGSGIMLGGDGQIVTVLGVLEGKLDTIKDGIAEINATVNDINTYLKVNVTDLLKTINNSVVMIKNDTATLIIGQAEIKAKLDDLLNLTSQVNDTVTMILACCNNASKVLNRMEGTLNSTYTGVLNVKSDLSTLIDTANNVVIPKFNELYDNVTVEINASRDLIIQKISSVNDSLTTIISAGFNDVEAMISNLNTTLLNRIDELEGTLLFYMTANEQRLEGIINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILASIGNVNLTVFNKLNDLEIELGDVNATINAGIFQIQSNLGNANQLILDTLTSSKVEILNAISSNASAISSEIHNAVNQLSTLVLQVNDTLTLKITGEADNILNFLSSLEGSMNTGFNNVTSTLSAVENNILGKITDTSNLLSSKIDNTLSTLQDLITSTSNDLKNSISSAKNDIVSSLSSKVDSSTQTLSTKLDDLKSAQESNTNSINNNIMLFGAASLILLIVTIGLVGYRLIARRRVG [Source organism chain C]=Staphylothermus marinus [UniProt ID chain D]=Q54436 [UniProt boundaries chain D]=1238-1286 [UniProt coverage chain D]=3% [Name chain D]=Tetrabrachion [UniProt sequence chain D]=MNRVLAYSLLAIMTLSLLIIPAPGIAQRITVGVSVKAGTYNFYNITPTTQTVEVTDNGMLRVIINRTEATELGTTIRLAFILDTDKYDPNVGGYFLNVSNIGVYAPSDPTQSPYGGVIDITQNSTLTDGTQVVGNVTVVNGGNNVIILIDLSKLPDLQNVVYITNVYTETSTTANLTNTLLRVKAFDAASWDAVISGNQFKILYIPSLCKYVKINVIHSPAIVGTNVDVIVSFHKYFSLVQSIAGVSLDITVDNKTQLNMTNYYNATENYVLATFINGNLTVGGSEVFSSPTVTVINASTFKYSGQVKDYAPTVADTATPWVRTLNKFEVEFRHEIVNXTHDLIFYIHCDSDTVSYDTWPFLIVNASLDITTTEVAFNSTTINPGDIVNFTAHNVPLQYLTATNYGVLRFQLINPALVVYVPVSNMTLSANTTTGIINGSFVLPDAPYGGLDYLTYLVFNDGKFIANGYITVSPCIETYVLTNTSAYAEDAGSSYIGRFVPGYTSVPGDYIVIKGYGFALSNLTGFTVSINNTDVIILNATYNASTGKIIILAKLLDTNGTPIPVGAGFIRVGQNGTTNIAYAPFNVTRNSGLEKVLFNPRWFYNGTYYIEHDKLGDPYLYFPVDYPLVNNTFTTEMWPFNTTIEVIGWPTNTFTLKAFNKEFNLSFNLLTLSLTNGYNMTNLYNLTIPFLPYGNYTLLEGTLLSVNNRTVFTVHMGINVDLDSCGNGTLSITVVGAAPNTEYNFTFGYQVHDLNYGITRYISPQWNGTWNISLVTDIYGTGSTSVPLITLYPTSYVINATWDVITWLRLSGSGTLDLLFSVDVSYNGFTDNLTTPITYVFGPSDTTPGSFNIYVNTTYNVSVVRVAVDYLPRTNVVISVPETVLPGDTITVQIFPHHNEVWGFIEPTALFDENQLLGWYLTVRLVDPLSNTVVERVAGYYAGNLIVEDVDGDGDNEVWFVVNLTAPLVLGVDKTYRVDVELFLAVLNPSSNITGVTAVDNECYVQLDLNGTIYWNGLGSGIMLGGDGQIVTVLGVLEGKLDTIKDGIAEINATVNDINTYLKVNVTDLLKTINNSVVMIKNDTATLIIGQAEIKAKLDDLLNLTSQVNDTVTMILACCNNASKVLNRMEGTLNSTYTGVLNVKSDLSTLIDTANNVVIPKFNELYDNVTVEINASRDLIIQKISSVNDSLTTIISAGFNDVEAMISNLNTTLLNRIDELEGTLLFYMTANEQRLEGIINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILASIGNVNLTVFNKLNDLEIELGDVNATINAGIFQIQSNLGNANQLILDTLTSSKVEILNAISSNASAISSEIHNAVNQLSTLVLQVNDTLTLKITGEADNILNFLSSLEGSMNTGFNNVTSTLSAVENNILGKITDTSNLLSSKIDNTLSTLQDLITSTSNDLKNSISSAKNDIVSSLSSKVDSSTQTLSTKLDDLKSAQESNTNSINNNIMLFGAASLILLIVTIGLVGYRLIARRRVG [Source organism chain D]=Staphylothermus marinus [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Staphylothermus marinus [Accession]=MF4130001 [Entry] [Entry number]=45 [Entry name]=Virion-associated protein P3 [PDB ID]=3f6n [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:20181714). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=P03551 [UniProt boundaries chain A]=3-72 [UniProt coverage chain A]=54% [Name chain A]=Virion-associated protein [UniProt sequence chain A]=MANLNQIQKEVSEILSDQKSMKADIKAILELLGSQNPIKESLETVAAKIVNDLTKLINDCPCNKEILEALGTQPKEQLIEQPKEKGKGLNLGKYSYPNYGVGNEELGSSGNPKALTWPFKAPAGWPNQF [Source organism chain A]=Cauliflower mosaic virus [UniProt ID chain B]=P03551 [UniProt boundaries chain B]=2-75 [UniProt coverage chain B]=57% [Name chain B]=Virion-associated protein [UniProt sequence chain B]=MANLNQIQKEVSEILSDQKSMKADIKAILELLGSQNPIKESLETVAAKIVNDLTKLINDCPCNKEILEALGTQPKEQLIEQPKEKGKGLNLGKYSYPNYGVGNEELGSSGNPKALTWPFKAPAGWPNQF [Source organism chain B]=Cauliflower mosaic virus [UniProt ID chain C]=P03551 [UniProt boundaries chain C]=2-74 [UniProt coverage chain C]=56% [Name chain C]=Virion-associated protein [UniProt sequence chain C]=MANLNQIQKEVSEILSDQKSMKADIKAILELLGSQNPIKESLETVAAKIVNDLTKLINDCPCNKEILEALGTQPKEQLIEQPKEKGKGLNLGKYSYPNYGVGNEELGSSGNPKALTWPFKAPAGWPNQF [Source organism chain C]=Cauliflower mosaic virus [UniProt ID chain D]=P03551 [UniProt boundaries chain D]=3-74 [UniProt coverage chain D]=55% [Name chain D]=Virion-associated protein [UniProt sequence chain D]=MANLNQIQKEVSEILSDQKSMKADIKAILELLGSQNPIKESLETVAAKIVNDLTKLINDCPCNKEILEALGTQPKEQLIEQPKEKGKGLNLGKYSYPNYGVGNEELGSSGNPKALTWPFKAPAGWPNQF [Source organism chain D]=Cauliflower mosaic virus [ExpTech]=X-ray [Resolution]=3.10 [Source organism]=Cauliflower mosaic virus [Accession]=MF4140001 [Entry] [Entry number]=46 [Entry name]=Assembly domain of cartilage oligomeric matrix protein (rat) [PDB ID]=1fbm [Chains]=A,B,C,D,E [Total number of chains]=5 [Assembly]=Pentamer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (pentameric) [Sequence domain]=Cartilage oligomeric matrix protein [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:9736606). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Evidence chain E]=N/A [Similar structures]=MF5110001,MF5110002 [UniProt ID chain A]=P35444 [UniProt boundaries chain A]=27-72 [UniProt coverage chain A]=6% [Name chain A]=Cartilage oligomeric matrix protein [UniProt sequence chain A]=MSPTACVLVLALAALRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRHRVKEITFLKNTVMECDACGMQPARTPGLSVRPVALCAPGSCFPGVVCTETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKTNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQRSGCQRRGQHFCPDGSPSPCHEKADCILERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDRIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDKDKWGDACDNCRSQKNDDQKDTDRDGQGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYERHRLRRA [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P35444 [UniProt boundaries chain B]=27-72 [UniProt coverage chain B]=6% [Name chain B]=Cartilage oligomeric matrix protein [UniProt sequence chain B]=MSPTACVLVLALAALRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRHRVKEITFLKNTVMECDACGMQPARTPGLSVRPVALCAPGSCFPGVVCTETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKTNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQRSGCQRRGQHFCPDGSPSPCHEKADCILERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDRIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDKDKWGDACDNCRSQKNDDQKDTDRDGQGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYERHRLRRA [Source organism chain B]=Rattus norvegicus [UniProt ID chain C]=P35444 [UniProt boundaries chain C]=27-72 [UniProt coverage chain C]=6% [Name chain C]=Cartilage oligomeric matrix protein [UniProt sequence chain C]=MSPTACVLVLALAALRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRHRVKEITFLKNTVMECDACGMQPARTPGLSVRPVALCAPGSCFPGVVCTETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKTNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQRSGCQRRGQHFCPDGSPSPCHEKADCILERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDRIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDKDKWGDACDNCRSQKNDDQKDTDRDGQGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYERHRLRRA [Source organism chain C]=Rattus norvegicus [UniProt ID chain D]=P35444 [UniProt boundaries chain D]=27-72 [UniProt coverage chain D]=6% [Name chain D]=Cartilage oligomeric matrix protein [UniProt sequence chain D]=MSPTACVLVLALAALRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRHRVKEITFLKNTVMECDACGMQPARTPGLSVRPVALCAPGSCFPGVVCTETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKTNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQRSGCQRRGQHFCPDGSPSPCHEKADCILERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDRIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDKDKWGDACDNCRSQKNDDQKDTDRDGQGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYERHRLRRA [Source organism chain D]=Rattus norvegicus [UniProt ID chain E]=P35444 [UniProt boundaries chain E]=27-72 [UniProt coverage chain E]=6% [Name chain E]=Cartilage oligomeric matrix protein [UniProt sequence chain E]=MSPTACVLVLALAALRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRHRVKEITFLKNTVMECDACGMQPARTPGLSVRPVALCAPGSCFPGVVCTETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKTNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQRSGCQRRGQHFCPDGSPSPCHEKADCILERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDRIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDKDKWGDACDNCRSQKNDDQKDTDRDGQGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYERHRLRRA [Source organism chain E]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Rattus norvegicus [Accession]=MF5110001 [Entry] [Entry number]=47 [Entry name]=Assembly domain of cartilage oligomeric matrix protein (mouse) [PDB ID]=1mz9 [Chains]=A,B,C,D,E [Total number of chains]=5 [Assembly]=Pentamer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (pentameric) [Sequence domain]=Cartilage oligomeric matrix protein [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:12426368). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Evidence chain E]=N/A [Similar structures]=MF5110001,MF5110002 [UniProt ID chain A]=Q9R0G6 [UniProt boundaries chain A]=28-71 [UniProt coverage chain A]=5% [Name chain A]=Cartilage oligomeric matrix protein [UniProt sequence chain A]=MGPTACVLVLALAILRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRQQVKEITFLKNTVMECDACGMQPARTPGLSVRPVPLCAPGSCFPGVVCSETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKSNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQTSGCQRRGQHFCPDGSPSPCHEKANCVLERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDSDKWGDACDNCRSKKNDDQKDTDLDGRGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYESHRLQRV [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9R0G6 [UniProt boundaries chain B]=28-71 [UniProt coverage chain B]=5% [Name chain B]=Cartilage oligomeric matrix protein [UniProt sequence chain B]=MGPTACVLVLALAILRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRQQVKEITFLKNTVMECDACGMQPARTPGLSVRPVPLCAPGSCFPGVVCSETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKSNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQTSGCQRRGQHFCPDGSPSPCHEKANCVLERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDSDKWGDACDNCRSKKNDDQKDTDLDGRGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYESHRLQRV [Source organism chain B]=Mus musculus [UniProt ID chain C]=Q9R0G6 [UniProt boundaries chain C]=28-71 [UniProt coverage chain C]=5% [Name chain C]=Cartilage oligomeric matrix protein [UniProt sequence chain C]=MGPTACVLVLALAILRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRQQVKEITFLKNTVMECDACGMQPARTPGLSVRPVPLCAPGSCFPGVVCSETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKSNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQTSGCQRRGQHFCPDGSPSPCHEKANCVLERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDSDKWGDACDNCRSKKNDDQKDTDLDGRGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYESHRLQRV [Source organism chain C]=Mus musculus [UniProt ID chain D]=Q9R0G6 [UniProt boundaries chain D]=28-71 [UniProt coverage chain D]=5% [Name chain D]=Cartilage oligomeric matrix protein [UniProt sequence chain D]=MGPTACVLVLALAILRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRQQVKEITFLKNTVMECDACGMQPARTPGLSVRPVPLCAPGSCFPGVVCSETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKSNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQTSGCQRRGQHFCPDGSPSPCHEKANCVLERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDSDKWGDACDNCRSKKNDDQKDTDLDGRGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYESHRLQRV [Source organism chain D]=Mus musculus [UniProt ID chain E]=Q9R0G6 [UniProt boundaries chain E]=28-71 [UniProt coverage chain E]=5% [Name chain E]=Cartilage oligomeric matrix protein [UniProt sequence chain E]=MGPTACVLVLALAILRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRQQVKEITFLKNTVMECDACGMQPARTPGLSVRPVPLCAPGSCFPGVVCSETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKSNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQTSGCQRRGQHFCPDGSPSPCHEKANCVLERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDSDKWGDACDNCRSKKNDDQKDTDLDGRGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYESHRLQRV [Source organism chain E]=Mus musculus [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Mus musculus [Accession]=MF5110002 [Entry] [Entry number]=48 [Entry name]=Leucine zipper domain of the c-Jun homodimer [PDB ID]=1jun [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=bZIP transcription factor [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:8662824). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110006,MF2110009,MF7000301,MF7000302,MF7000303 [UniProt ID chain A]=P05412 [UniProt boundaries chain A]=276-315 [UniProt coverage chain A]=12% [Name chain A]=Transcription factor Jun [UniProt sequence chain A]=MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P05412 [UniProt boundaries chain B]=276-315 [UniProt coverage chain B]=12% [Name chain B]=Transcription factor Jun [UniProt sequence chain B]=MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2110006 [Entry] [Entry number]=49 [Entry name]=Delta sleep-inducing peptide immunoreactive peptide A homolog [PDB ID]=1dip [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:9388238). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P80220 [UniProt boundaries chain A]=1-77 [UniProt coverage chain A]=100% [Name chain A]=TSC22 domain family protein 3 [UniProt sequence chain A]=MDLVKNHLMYAVREEVEILKEQIRELVEKNSQLERENTLLKTLASPEQLEKFQSRLSPEEPAPETPEAPEAPGGSAV [Source organism chain A]=Sus scrofa [UniProt ID chain B]=P80220 [UniProt boundaries chain B]=1-77 [UniProt coverage chain B]=100% [Name chain B]=TSC22 domain family protein 3 [UniProt sequence chain B]=MDLVKNHLMYAVREEVEILKEQIRELVEKNSQLERENTLLKTLASPEQLEKFQSRLSPEEPAPETPEAPEAPGGSAV [Source organism chain B]=Sus scrofa [ExpTech]=NMR [Resolution]=N/A [Source organism]=Sus scrofa [Accession]=MF2110007 [Entry] [Entry number]=50 [Entry name]=VBP leucine zipper [PDB ID]=4u5t [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:22851716). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q10587 [UniProt boundaries chain A]=258-294 [UniProt coverage chain A]=12% [Name chain A]=Thyrotroph embryonic factor [UniProt sequence chain A]=MSDAGGGKKPPVDPQAGPGPGPGRAAGERGLSGSFPLVLKKLMENPPREARLDKEKGKEKLEEDEAAAASTMAVSASLMPPIWDKTIPYDGESFHLEYMDLDEFLLENGIPASPTHLAHNLLLPVAELEGKESASSSTASPPSSSTAIFQPSETVSSTESSLEKERETPSPIDPNCVEVDVNFNPDPADLVLSSVPGGELFNPRKHKFAEEDLKPQPMIKKAKKVFVPDEQKDEKYWTRRKKNNVAAKRSRDARRLKENQITIRAAFLEKENTALRTEVAELRKEVGKCKTIVSKYETKYGPL [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q10587 [UniProt boundaries chain B]=258-294 [UniProt coverage chain B]=12% [Name chain B]=Thyrotroph embryonic factor [UniProt sequence chain B]=MSDAGGGKKPPVDPQAGPGPGPGRAAGERGLSGSFPLVLKKLMENPPREARLDKEKGKEKLEEDEAAAASTMAVSASLMPPIWDKTIPYDGESFHLEYMDLDEFLLENGIPASPTHLAHNLLLPVAELEGKESASSSTASPPSSSTAIFQPSETVSSTESSLEKERETPSPIDPNCVEVDVNFNPDPADLVLSSVPGGELFNPRKHKFAEEDLKPQPMIKKAKKVFVPDEQKDEKYWTRRKKNNVAAKRSRDARRLKENQITIRAAFLEKENTALRTEVAELRKEVGKCKTIVSKYETKYGPL [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.30 [Source organism]=Homo sapiens [Accession]=MF2110008 [Entry] [Entry number]=51 [Entry name]=SH2B adapter protein 2 dimerization domain [PDB ID]=1q2h [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Phenylalanine zipper (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:15378031). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O14492 [UniProt boundaries chain A]=21-83 [UniProt coverage chain A]=9% [Name chain A]=SH2B adapter protein 2 [UniProt sequence chain A]=MNGAGPGPAAAAPVPVPVPVPDWRQFCELHAQAAAVDFAHKFCRFLRDNPAYDTPDAGASFSRHFAANFLDVFGEEVRRVLVAGPTTRGAAVSAEAMEPELADTSALKAAPYGHSRSSEDVSTHAATKARVRKGFSLRNMSLCVVDGVRDMWHRRASPEPDAAAAPRTAEPRDKWTRRLRLSRTLAAKVELVDIQREGALRFMVADDAAAGSGGSAQWQKCRLLLRRAVAEERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTELSCTRGGCLASRVASCSCELLTDAVDLPRPPETTAVGAVVTAPHSRGRDAVRESLIHVPLETFLQTLESPGGSGSDSNNTGEQGAETDPEAEPELELSDYPWFHGTLSRVKAAQLVLAGGPRNHGLFVIRQSETRPGEYVLTFNFQGKAKHLRLSLNGHGQCHVQHLWFQSVLDMLRHFHTHPIPLESGGSADITLRSYVRAQDPPPEPGPTPPAAPASPACWSDSPGQHYFSSLAAAACPPASPSDAAGASSSSASSSSAASGPAPPRPVEGQLSARSRSNSAERLLEAVAATAAEEPPEAAPGRARAVENQYSFY [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O14492 [UniProt boundaries chain B]=21-82 [UniProt coverage chain B]=9% [Name chain B]=SH2B adapter protein 2 [UniProt sequence chain B]=MNGAGPGPAAAAPVPVPVPVPDWRQFCELHAQAAAVDFAHKFCRFLRDNPAYDTPDAGASFSRHFAANFLDVFGEEVRRVLVAGPTTRGAAVSAEAMEPELADTSALKAAPYGHSRSSEDVSTHAATKARVRKGFSLRNMSLCVVDGVRDMWHRRASPEPDAAAAPRTAEPRDKWTRRLRLSRTLAAKVELVDIQREGALRFMVADDAAAGSGGSAQWQKCRLLLRRAVAEERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTELSCTRGGCLASRVASCSCELLTDAVDLPRPPETTAVGAVVTAPHSRGRDAVRESLIHVPLETFLQTLESPGGSGSDSNNTGEQGAETDPEAEPELELSDYPWFHGTLSRVKAAQLVLAGGPRNHGLFVIRQSETRPGEYVLTFNFQGKAKHLRLSLNGHGQCHVQHLWFQSVLDMLRHFHTHPIPLESGGSADITLRSYVRAQDPPPEPGPTPPAAPASPACWSDSPGQHYFSSLAAAACPPASPSDAAGASSSSASSSSAASGPAPPRPVEGQLSARSRSNSAERLLEAVAATAAEEPPEAAPGRARAVENQYSFY [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Homo sapiens [Accession]=MF2100004 [Entry] [Entry number]=52 [Entry name]=GTPase binding domain of neural Wiskott-Aldrich syndrome protein in complex with Escherichia coli EspF(U) [PDB ID]=2lnh [Chains]=A,C [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe B chains were not considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain C]=N/A [Similar structures]=None [UniProt ID chain A]=O00401 [UniProt boundaries chain A]=207-270 [UniProt coverage chain A]=12% [Name chain A]=Actin nucleation-promoting factor WASL [UniProt sequence chain A]=MSSVQQQPPPPRRVTNVGSLLLTPQENESLFTFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDPPNGPNLPMATVDIKNPEITTNRFYGPQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHNSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPSVAVPPPPPNRMYPPPPPALPSSAPSGPPPPPPSVLGVGPVAPPPPPPPPPPPGPPPPPGLPSDGDHQVPTTAGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVADGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDEDDEEDFEDDDEWED [Source organism chain A]=Homo sapiens [UniProt ID chain C]=P0DJ89 [UniProt boundaries chain C]=268-314 [UniProt coverage chain C]=13% [Name chain C]=Secreted effector protein EspF(U) [UniProt sequence chain C]=MINNVSSLFPTVNRNITAVYKKSSFSVSPQKITLNPVKISSPFSPSSSSISATTLFRAPNAHSASFHRQSTAESSLHQQLPNVRQRLIQHLAEHGIKPARSMAEHIPPAPNWPAPPPPVQNEQSRPLPDVAQRLVQHLAEHGIQPARNMAEHIPPAPNWPAPPLPVQNEQSRPLPDVAQRLVQHLAEHGIQPARSMAEHIPPAPNWPAPPPPVQNEQSRPLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHGINTSKRS [Source organism chain C]=Escherichia coli O157:H7 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens ;Escherichia coli O157:H7 [Accession]=MF2202001 [Entry] [Entry number]=53 [Entry name]=CesA-EspA complex [PDB ID]=1xou [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:15619638). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q47184 [UniProt boundaries chain A]=31-190 [UniProt coverage chain A]=83% [Name chain A]=EspA [UniProt sequence chain A]=MDTSTTASVASANASTSTSMAYDLGSMSKDDVIDLFNKLGVFQAAILMFAYMYQAQSDLSIAKFADMNEASKESTTAQKMANLVDAKIADVQSSSDKNAKAQLPDEVISYINDPRNDITISGIDNINAQLGAGDLQTVKAAISAKANNLTTTVNNSQLEIQQMSNTLNLLTSARSDMQSLQYRTISGISLGK [Source organism chain A]=Escherichia coli [UniProt ID chain B]=O52124 [UniProt boundaries chain B]=2-85 [UniProt coverage chain B]=78% [Name chain B]=L0052 [UniProt sequence chain B]=MSIVSQTRNKELLDKKIRSEIEAIKKIIAEFDVVKESVNELSEKAKTDPQAAEKLNKLIEGYTYGEERKLYDSALSKIEKLIETLSPARSKSQSTMNQRNRNNRKIV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Escherichia coli [Accession]=MF2220001 [Entry] [Entry number]=54 [Entry name]=Cell division factor ZapA (mutant) [PDB ID]=2mmv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Cell division protein ZapA [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2120010,MF2120012 [UniProt ID chain A]=A0A078N0N2 [UniProt boundaries chain A]=1-83 [UniProt coverage chain A]=91% [Name chain A]=Cell division protein ZapA [UniProt sequence chain A]=MTEQPKTRVSVRIYGQDYTIVGAESPAHIRLVAAFVDDKMHEFSEKNPMLDVPKLAVLTAVNIASEYLKLKEEYNRLREQLKKEKDGKQDD [Source organism chain A]=Geobacillus stearothermophilus [UniProt ID chain B]=A0A078N0N2 [UniProt boundaries chain B]=1-83 [UniProt coverage chain B]=91% [Name chain B]=Cell division protein ZapA [UniProt sequence chain B]=MTEQPKTRVSVRIYGQDYTIVGAESPAHIRLVAAFVDDKMHEFSEKNPMLDVPKLAVLTAVNIASEYLKLKEEYNRLREQLKKEKDGKQDD [Source organism chain B]=Geobacillus stearothermophilus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Geobacillus stearothermophilus [Accession]=MF2120012 [Entry] [Entry number]=56 [Entry name]=5-hydroxyisourate hydrolase (Salmonella dublin) [PDB ID]=2gpz [Chains]=A,C,C-2,A-2 [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Transthyretin-like folds [Subclass]=HIUase [Sequence domain]=HIUase/Transthyretin family [Evidence level]=Direct evidence [Evidence text]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:16787778). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain C]=N/A [Evidence chain C-2]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF4110001,MF4110002,MF4120005,MF4120002,MF4110003,MF4100001,MF4120004 [UniProt ID chain A]=Q4VYA5 [UniProt boundaries chain A]=27-136 [UniProt coverage chain A]=80% [Name chain A]=5-hydroxyisourate hydrolase [UniProt sequence chain A]=MKRHILATVIASLVAAPAMALAAGNNILSVHILDQQTGKPAPGVEVVLEQKKDNGWTQLNTGHTDQDGRIKALWPEKAAAPGDYRVIFKTGQYFESKKLDTFFPEIPVEFHISKTNEHYHVPLLLSQYGYSTYRGS [Source organism chain A]=Salmonella dublin [UniProt ID chain C]=Q4VYA5 [UniProt boundaries chain C]=27-136 [UniProt coverage chain C]=80% [Name chain C]=5-hydroxyisourate hydrolase [UniProt sequence chain C]=MKRHILATVIASLVAAPAMALAAGNNILSVHILDQQTGKPAPGVEVVLEQKKDNGWTQLNTGHTDQDGRIKALWPEKAAAPGDYRVIFKTGQYFESKKLDTFFPEIPVEFHISKTNEHYHVPLLLSQYGYSTYRGS [Source organism chain C]=Salmonella dublin [UniProt ID chain C-2]=Q4VYA5 [UniProt boundaries chain C-2]=27-136 [UniProt coverage chain C-2]=80% [Name chain C-2]=5-hydroxyisourate hydrolase [UniProt sequence chain C-2]=MKRHILATVIASLVAAPAMALAAGNNILSVHILDQQTGKPAPGVEVVLEQKKDNGWTQLNTGHTDQDGRIKALWPEKAAAPGDYRVIFKTGQYFESKKLDTFFPEIPVEFHISKTNEHYHVPLLLSQYGYSTYRGS [Source organism chain C-2]=Salmonella dublin [UniProt ID chain A-2]=Q4VYA5 [UniProt boundaries chain A-2]=27-136 [UniProt coverage chain A-2]=80% [Name chain A-2]=5-hydroxyisourate hydrolase [UniProt sequence chain A-2]=MKRHILATVIASLVAAPAMALAAGNNILSVHILDQQTGKPAPGVEVVLEQKKDNGWTQLNTGHTDQDGRIKALWPEKAAAPGDYRVIFKTGQYFESKKLDTFFPEIPVEFHISKTNEHYHVPLLLSQYGYSTYRGS [Source organism chain A-2]=Salmonella dublin [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Salmonella dublin [Accession]=MF4120002 [Entry] [Entry number]=57 [Entry name]=5-hydroxyisourate hydrolase (Bacillus subtilis) [PDB ID]=2h0e [Chains]=A-3,A,A-4,A-2 [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Transthyretin-like folds [Subclass]=HIUase [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:16782815). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-3]=N/A [Evidence chain A-4]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=O32142 [UniProt boundaries chain A]=1-114 [UniProt coverage chain A]=100% [Name chain A]=5-hydroxyisourate hydrolase [UniProt sequence chain A]=MGKLTTHILDLTCGKPAANVKIGLKRLGESIMKEVYTNNDGRVDVPLLAGEELMSGEYVMEFHAGDYFASKNMNAADQPFLTIVTVRFQLADPDAHYHIPLLLSPFGYQVYRGS [Source organism chain A]=Bacillus subtilis [UniProt ID chain A-3]=O32142 [UniProt boundaries chain A-3]=1-114 [UniProt coverage chain A-3]=100% [Name chain A-3]=5-hydroxyisourate hydrolase [UniProt sequence chain A-3]=MGKLTTHILDLTCGKPAANVKIGLKRLGESIMKEVYTNNDGRVDVPLLAGEELMSGEYVMEFHAGDYFASKNMNAADQPFLTIVTVRFQLADPDAHYHIPLLLSPFGYQVYRGS [Source organism chain A-3]=Bacillus subtilis [UniProt ID chain A-4]=O32142 [UniProt boundaries chain A-4]=1-114 [UniProt coverage chain A-4]=100% [Name chain A-4]=5-hydroxyisourate hydrolase [UniProt sequence chain A-4]=MGKLTTHILDLTCGKPAANVKIGLKRLGESIMKEVYTNNDGRVDVPLLAGEELMSGEYVMEFHAGDYFASKNMNAADQPFLTIVTVRFQLADPDAHYHIPLLLSPFGYQVYRGS [Source organism chain A-4]=Bacillus subtilis [UniProt ID chain A-2]=O32142 [UniProt boundaries chain A-2]=1-114 [UniProt coverage chain A-2]=100% [Name chain A-2]=5-hydroxyisourate hydrolase [UniProt sequence chain A-2]=MGKLTTHILDLTCGKPAANVKIGLKRLGESIMKEVYTNNDGRVDVPLLAGEELMSGEYVMEFHAGDYFASKNMNAADQPFLTIVTVRFQLADPDAHYHIPLLLSPFGYQVYRGS [Source organism chain A-2]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Bacillus subtilis [Accession]=MF4120003 [Entry] [Entry number]=58 [Entry name]=5-hydroxyisourate hydrolase (Klebsiella pneumoniae) [PDB ID]=3qva [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Transthyretin-like folds [Subclass]=HIUase [Sequence domain]=HIUase/Transthyretin family [Evidence level]=Direct evidence [Evidence text]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:21795808). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF4110001,MF4110002,MF4120005,MF4120002,MF4110003,MF4100001,MF4120004 [UniProt ID chain A]=A6T926 [UniProt boundaries chain A]=1-108 [UniProt coverage chain A]=100% [Name chain A]=5-hydroxyisourate hydrolase [UniProt sequence chain A]=MSTLSTHILDISTGTPAEGVTVSLSREGETLANLVTNAQGRIATFSAAPLPAGRYCLTAETGAWFARAGRESVFTRAQIDFVIGEAAEDHFHLPFLIAPGGWSTYRGS [Source organism chain A]=Klebsiella pneumoniae subsp pneumoniae [UniProt ID chain B]=A6T926 [UniProt boundaries chain B]=1-107 [UniProt coverage chain B]=99% [Name chain B]=5-hydroxyisourate hydrolase [UniProt sequence chain B]=MSTLSTHILDISTGTPAEGVTVSLSREGETLANLVTNAQGRIATFSAAPLPAGRYCLTAETGAWFARAGRESVFTRAQIDFVIGEAAEDHFHLPFLIAPGGWSTYRGS [Source organism chain B]=Klebsiella pneumoniae subsp pneumoniae [UniProt ID chain C]=A6T926 [UniProt boundaries chain C]=1-108 [UniProt coverage chain C]=100% [Name chain C]=5-hydroxyisourate hydrolase [UniProt sequence chain C]=MSTLSTHILDISTGTPAEGVTVSLSREGETLANLVTNAQGRIATFSAAPLPAGRYCLTAETGAWFARAGRESVFTRAQIDFVIGEAAEDHFHLPFLIAPGGWSTYRGS [Source organism chain C]=Klebsiella pneumoniae subsp pneumoniae [UniProt ID chain D]=A6T926 [UniProt boundaries chain D]=2-108 [UniProt coverage chain D]=99% [Name chain D]=5-hydroxyisourate hydrolase [UniProt sequence chain D]=MSTLSTHILDISTGTPAEGVTVSLSREGETLANLVTNAQGRIATFSAAPLPAGRYCLTAETGAWFARAGRESVFTRAQIDFVIGEAAEDHFHLPFLIAPGGWSTYRGS [Source organism chain D]=Klebsiella pneumoniae subsp pneumoniae [ExpTech]=X-ray [Resolution]=1.76 [Source organism]=Klebsiella pneumoniae subsp pneumoniae [Accession]=MF4120004 [Entry] [Entry number]=59 [Entry name]=5-hydroxyisourate hydrolase (Escherichia coli) [PDB ID]=2g2n [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Transthyretin-like folds [Subclass]=HIUase [Sequence domain]=HIUase/Transthyretin family [Evidence level]=Direct evidence [Evidence text]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:16723258). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF4110001,MF4110002,MF4120005,MF4120002,MF4110003,MF4100001,MF4120004 [UniProt ID chain A]=P76341 [UniProt boundaries chain A]=27-137 [UniProt coverage chain A]=81% [Name chain A]=5-hydroxyisourate hydrolase [UniProt sequence chain A]=MLKRYLVLSVATAAFSLPSLVNAAQQNILSVHILNQQTGKPAADVTVTLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEIPVEFHINKVNEHYHVPLLLSQYGYSTYRGS [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P76341 [UniProt boundaries chain B]=27-137 [UniProt coverage chain B]=81% [Name chain B]=5-hydroxyisourate hydrolase [UniProt sequence chain B]=MLKRYLVLSVATAAFSLPSLVNAAQQNILSVHILNQQTGKPAADVTVTLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEIPVEFHINKVNEHYHVPLLLSQYGYSTYRGS [Source organism chain B]=Escherichia coli [UniProt ID chain C]=P76341 [UniProt boundaries chain C]=26-137 [UniProt coverage chain C]=81% [Name chain C]=5-hydroxyisourate hydrolase [UniProt sequence chain C]=MLKRYLVLSVATAAFSLPSLVNAAQQNILSVHILNQQTGKPAADVTVTLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEIPVEFHINKVNEHYHVPLLLSQYGYSTYRGS [Source organism chain C]=Escherichia coli [UniProt ID chain D]=P76341 [UniProt boundaries chain D]=26-137 [UniProt coverage chain D]=81% [Name chain D]=5-hydroxyisourate hydrolase [UniProt sequence chain D]=MLKRYLVLSVATAAFSLPSLVNAAQQNILSVHILNQQTGKPAADVTVTLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEIPVEFHINKVNEHYHVPLLLSQYGYSTYRGS [Source organism chain D]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Escherichia coli [Accession]=MF4120005 [Entry] [Entry number]=60 [Entry name]=5-hydroxyisourate hydrolase (Danio rerio) [PDB ID]=2h1x [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Transthyretin-like folds [Subclass]=HIUase [Sequence domain]=HIUase/Transthyretin family [Evidence level]=Direct evidence [Evidence text]=The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:16952372). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF4110001,MF4110002,MF4120005,MF4120002,MF4110003,MF4100001,MF4120004 [UniProt ID chain A]=Q06S87 [UniProt boundaries chain A]=26-138 [UniProt coverage chain A]=81% [Name chain A]=5-hydroxyisourate hydrolase [UniProt sequence chain A]=MNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS [Source organism chain A]=Danio rerio [UniProt ID chain B]=Q06S87 [UniProt boundaries chain B]=26-138 [UniProt coverage chain B]=81% [Name chain B]=5-hydroxyisourate hydrolase [UniProt sequence chain B]=MNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS [Source organism chain B]=Danio rerio [UniProt ID chain C]=Q06S87 [UniProt boundaries chain C]=26-138 [UniProt coverage chain C]=81% [Name chain C]=5-hydroxyisourate hydrolase [UniProt sequence chain C]=MNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS [Source organism chain C]=Danio rerio [UniProt ID chain D]=Q06S87 [UniProt boundaries chain D]=26-138 [UniProt coverage chain D]=81% [Name chain D]=5-hydroxyisourate hydrolase [UniProt sequence chain D]=MNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS [Source organism chain D]=Danio rerio [ExpTech]=X-ray [Resolution]=1.98 [Source organism]=Danio rerio [Accession]=MF4110003 [Entry] [Entry number]=61 [Entry name]=Oligomerization region of the general control protein GCN4 [PDB ID]=2b1f [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. In the specific case of GCN4 refolding studies have explicitly shown that structure formation and dimerization happens at the same time (PMID:7548036) [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=P03069 [UniProt boundaries chain A]=251-279 [UniProt coverage chain A]=10% [Name chain A]=General control transcription factor GCN4 [UniProt sequence chain A]=MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P03069 [UniProt boundaries chain B]=251-280 [UniProt coverage chain B]=10% [Name chain B]=General control transcription factor GCN4 [UniProt sequence chain B]=MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER [Source organism chain B]=Saccharomyces cerevisiae [UniProt ID chain C]=P03069 [UniProt boundaries chain C]=251-279 [UniProt coverage chain C]=10% [Name chain C]=General control transcription factor GCN4 [UniProt sequence chain C]=MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER [Source organism chain C]=Saccharomyces cerevisiae [UniProt ID chain D]=P03069 [UniProt boundaries chain D]=251-278 [UniProt coverage chain D]=9% [Name chain D]=General control transcription factor GCN4 [UniProt sequence chain D]=MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER [Source organism chain D]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Saccharomyces cerevisiae [Accession]=MF4110004 [Entry] [Entry number]=62 [Entry name]=Regulatory protein Rop [PDB ID]=2ijk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Detailed thermodynamic and spectroscopic studies were carried out on the ColE1-ROP protein in order to establish a quantitative basis for the contribution of noncovalent interactions to the stability of four-helix-bundle proteins. The energetics of both heat- and GdnHCl-induced denaturation were measured by differential scanning microcalorimetry (DSC) and/or by following the change in circular dichroism in the far-UV range. No intermediate species could be detected during thermal unfolding of the dimer in the absence of GdnHCl. Under these conditions ROP unfolding exhibits a strict two-state behavior (PMID:8471599). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P03051 [UniProt boundaries chain A]=2-58 [UniProt coverage chain A]=90% [Name chain A]=Regulatory protein rop [UniProt sequence chain A]=MTKQEKTALNMARFIRSQTLTLLEKLNELDADEQADICESLHDHADELYRSCLARFGDDGENL [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P03051 [UniProt boundaries chain B]=1-58 [UniProt coverage chain B]=92% [Name chain B]=Regulatory protein rop [UniProt sequence chain B]=MTKQEKTALNMARFIRSQTLTLLEKLNELDADEQADICESLHDHADELYRSCLARFGDDGENL [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.55 [Source organism]=Escherichia coli [Accession]=MF2120014 [Entry] [Entry number]=63 [Entry name]=Bcr-Abl oncoprotein oligomerization domain [PDB ID]=1k1f [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:11780146). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=P11274 [UniProt boundaries chain A]=1-67 [UniProt coverage chain A]=5% [Name chain A]=Breakpoint cluster region protein [UniProt sequence chain A]=MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEV [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P11274 [UniProt boundaries chain B]=1-67 [UniProt coverage chain B]=5% [Name chain B]=Breakpoint cluster region protein [UniProt sequence chain B]=MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEV [Source organism chain B]=Homo sapiens [UniProt ID chain C]=P11274 [UniProt boundaries chain C]=1-67 [UniProt coverage chain C]=5% [Name chain C]=Breakpoint cluster region protein [UniProt sequence chain C]=MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEV [Source organism chain C]=Homo sapiens [UniProt ID chain D]=P11274 [UniProt boundaries chain D]=1-66 [UniProt coverage chain D]=5% [Name chain D]=Breakpoint cluster region protein [UniProt sequence chain D]=MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEV [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Homo sapiens [Accession]=MF4100002 [Entry] [Entry number]=64 [Entry name]=Antitoxin phd dimer (Escherichia coli) [PDB ID]=3hry [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin Phd/YefM [Sequence domain]=Antitoxin Phd_YefM [Evidence level]=Direct evidence [Evidence text]=The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into monomer species (PMID:20603017). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00288 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP00288 covers 100% of the sequence present in the structure [Similar structures]=MF2120015,MF2140010,MF2120024 [UniProt ID chain A]=Q06253 [UniProt boundaries chain A]=1-67 [UniProt coverage chain A]=91% [Name chain A]=Antitoxin phd [UniProt sequence chain A]=MQSINFRTARGNLSEVLNNVEAGEEVEITRRGREPAVIVSKATFEAYKKAALDAEFASLFDTLDSTNKELVNR [Source organism chain A]=Escherichia phage P1 [UniProt ID chain B]=Q06253 [UniProt boundaries chain B]=1-55 [UniProt coverage chain B]=75% [Name chain B]=Antitoxin phd [UniProt sequence chain B]=MQSINFRTARGNLSEVLNNVEAGEEVEITRRGREPAVIVSKATFEAYKKAALDAEFASLFDTLDSTNKELVNR [Source organism chain B]=Escherichia phage P1 [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Escherichia phage P1 [Accession]=MF2120015 [Entry] [Entry number]=67 [Entry name]=Tetramerization domain of the Mnt repressor [PDB ID]=1qey [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:10426954). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=P03049 [UniProt boundaries chain A]=53-83 [UniProt coverage chain A]=37% [Name chain A]=Regulatory protein mnt [UniProt sequence chain A]=MARDDPHFNFRMPMEVREKLKFRAEANGRSMNSELLQIVQDALSKPSPVTGYRNDAERLADEQSELVKKMVFDTLKDLYKKTT [Source organism chain A]=Salmonella phage P22 [UniProt ID chain B]=P03049 [UniProt boundaries chain B]=53-83 [UniProt coverage chain B]=37% [Name chain B]=Regulatory protein mnt [UniProt sequence chain B]=MARDDPHFNFRMPMEVREKLKFRAEANGRSMNSELLQIVQDALSKPSPVTGYRNDAERLADEQSELVKKMVFDTLKDLYKKTT [Source organism chain B]=Salmonella phage P22 [UniProt ID chain C]=P03049 [UniProt boundaries chain C]=53-83 [UniProt coverage chain C]=37% [Name chain C]=Regulatory protein mnt [UniProt sequence chain C]=MARDDPHFNFRMPMEVREKLKFRAEANGRSMNSELLQIVQDALSKPSPVTGYRNDAERLADEQSELVKKMVFDTLKDLYKKTT [Source organism chain C]=Salmonella phage P22 [UniProt ID chain D]=P03049 [UniProt boundaries chain D]=53-83 [UniProt coverage chain D]=37% [Name chain D]=Regulatory protein mnt [UniProt sequence chain D]=MARDDPHFNFRMPMEVREKLKFRAEANGRSMNSELLQIVQDALSKPSPVTGYRNDAERLADEQSELVKKMVFDTLKDLYKKTT [Source organism chain D]=Salmonella phage P22 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella phage P22 [Accession]=MF4140002 [Entry] [Entry number]=68 [Entry name]=ING4 dimerization domain [PDB ID]=4afl [Chains]=A,C [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Inhibitor of growth proteins N-terminal histone-binding [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:22334692). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain C]=N/A [Similar structures]=MF2100005,MF7000127 [UniProt ID chain A]=Q9UNL4 [UniProt boundaries chain A]=3-104 [UniProt coverage chain A]=40% [Name chain A]=Inhibitor of growth protein 4 [UniProt sequence chain A]=MAAGMYLEHYLDSIENLPFELQRNFQLMRDLDQRTEDLKAEIDKLATEYMSSARSLSSEEKLALLKQIQEAYGKCKEFGDDKVQLAMQTYEMVDKHIRRLDTDLARFEADLKEKQIESSDYDSSSSKGKKKGRTQKEKKAARARSKGKNSDEEAPKTAQKKLKLVRTSPEYGMPSVTFGSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWFCPRCSQERKKK [Source organism chain A]=Homo sapiens [UniProt ID chain C]=Q9UNL4 [UniProt boundaries chain C]=4-105 [UniProt coverage chain C]=40% [Name chain C]=Inhibitor of growth protein 4 [UniProt sequence chain C]=MAAGMYLEHYLDSIENLPFELQRNFQLMRDLDQRTEDLKAEIDKLATEYMSSARSLSSEEKLALLKQIQEAYGKCKEFGDDKVQLAMQTYEMVDKHIRRLDTDLARFEADLKEKQIESSDYDSSSSKGKKKGRTQKEKKAARARSKGKNSDEEAPKTAQKKLKLVRTSPEYGMPSVTFGSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWFCPRCSQERKKK [Source organism chain C]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.28 [Source organism]=Homo sapiens [Accession]=MF2100005 [Entry] [Entry number]=69 [Entry name]=H2A-H2B histone dimer (human/mouse), containing histone variants macro-H2A.1 and H2B type 3-A [PDB ID]=1u35 [Chains]=C,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,B,I,J,E,A,G chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain C]=O75367 [UniProt boundaries chain C]=12-117 [UniProt coverage chain C]=28% [Name chain C]=Core histone macro-H2A.1 [UniProt sequence chain C]=MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVSKKAGGKKGARKSKKKQGEVSKAASADSTTEGTPADGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYIGGEVGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN [Source organism chain C]=Homo sapiens [UniProt ID chain D]=Q9D2U9 [UniProt boundaries chain D]=34-126 [UniProt coverage chain D]=73% [Name chain D]=H2B.U histone 2 [UniProt sequence chain D]=MPEPSRSTPAPKKGSKKAITKAQKKDGKKRKRGRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK [Source organism chain D]=Mus musculus [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF2201005 [Entry] [Entry number]=71 [Entry name]=H2A-H2B histone dimer (human/Xenopus laevis), containing histone variants H2A.Z and H2B 1.1 [PDB ID]=1f66 [Chains]=C,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,B,I,J,E,A,G chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain C]=P0C0S5 [UniProt boundaries chain C]=17-119 [UniProt coverage chain C]=80% [Name chain C]=Histone H2A.Z [UniProt sequence chain C]=MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV [Source organism chain C]=Homo sapiens [UniProt ID chain D]=P02281 [UniProt boundaries chain D]=32-126 [UniProt coverage chain D]=75% [Name chain D]=Histone H2B 1.1 [UniProt sequence chain D]=MPEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK [Source organism chain D]=Xenopus laevis [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Xenopus laevis ;Homo sapiens [Accession]=MF2211001 [Entry] [Entry number]=72 [Entry name]=H2A-H2B histone dimer (human), containing histone variants H2A.Z and H2B type 1-J [PDB ID]=3wa9 [Chains]=C,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,B,I,J,E,A,G chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain C]=P0C0S5 [UniProt boundaries chain C]=16-121 [UniProt coverage chain C]=82% [Name chain C]=Histone H2A.Z [UniProt sequence chain C]=MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV [Source organism chain C]=Homo sapiens [UniProt ID chain D]=P06899 [UniProt boundaries chain D]=33-125 [UniProt coverage chain D]=73% [Name chain D]=Histone H2B type 1-J [UniProt sequence chain D]=MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.07 [Source organism]=Homo sapiens [Accession]=MF2200003 [Entry] [Entry number]=73 [Entry name]=H2A-H2B histone dimer (Xenopus laevis), containing histone variants H2A type 1 and H2B 1.1 [PDB ID]=1aoi [Chains]=C,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,B,I,J,E,A,G chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain C]=P06897 [UniProt boundaries chain C]=5-119 [UniProt coverage chain C]=88% [Name chain C]=Histone H2A type 1 [UniProt sequence chain C]=MSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQSVLLPKKTESAKSAKSK [Source organism chain C]=Xenopus laevis [UniProt ID chain D]=P02281 [UniProt boundaries chain D]=28-126 [UniProt coverage chain D]=78% [Name chain D]=Histone H2B 1.1 [UniProt sequence chain D]=MPEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK [Source organism chain D]=Xenopus laevis [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Xenopus laevis [Accession]=MF2210001 [Entry] [Entry number]=74 [Entry name]=H2A-H2B histone dimer (Gallus gallus), containing histone variants H2A-IV and H2B 5 [PDB ID]=2aro [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,E,D,G,C chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain A]=P02263 [UniProt boundaries chain A]=14-119 [UniProt coverage chain A]=82% [Name chain A]=Histone H2A-IV [UniProt sequence chain A]=MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTDSHKAKAK [Source organism chain A]=Gallus gallus [UniProt ID chain B]=P0C1H3 [UniProt boundaries chain B]=34-125 [UniProt coverage chain B]=73% [Name chain B]=Histone H2B 1/2/3/4/6 [UniProt sequence chain B]=MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRKKSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK [Source organism chain B]=Gallus gallus [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Gallus gallus [Accession]=MF2210002 [Entry] [Entry number]=75 [Entry name]=H2A-H2B histone dimer (mouse/human), containing histone variants H2A and H2B type 1-B [PDB ID]=3x1u [Chains]=C,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,B,I,J,E,A,G chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain C]=Q8CGP4 [UniProt boundaries chain C]=15-119 [UniProt coverage chain C]=81% [Name chain C]=Histone H2A [UniProt sequence chain C]=MSGPTKRGGKARAKVKSRSSRAGLQFPVGRVHRLLRQGNYAQRIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKTRITPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHKSQTK [Source organism chain C]=Mus musculus [UniProt ID chain D]=P33778 [UniProt boundaries chain D]=33-126 [UniProt coverage chain D]=74% [Name chain D]=Histone H2B type 1-B [UniProt sequence chain D]=MPEPSKSAPAPKKGSKKAITKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.25 [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF2201007 [Entry] [Entry number]=77 [Entry name]=H2A-H2B histone dimer (human), containing histone variants H2A.V and H2B type 1-J [PDB ID]=3waa [Chains]=C,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,B,I,J,E,A,G chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain C]=Q71UI9 [UniProt boundaries chain C]=15-121 [UniProt coverage chain C]=83% [Name chain C]=Histone H2A.V [UniProt sequence chain C]=MAGGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTA [Source organism chain C]=Homo sapiens [UniProt ID chain D]=P06899 [UniProt boundaries chain D]=32-125 [UniProt coverage chain D]=74% [Name chain D]=Histone H2B type 1-J [UniProt sequence chain D]=MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.20 [Source organism]=Homo sapiens [Accession]=MF2200004 [Entry] [Entry number]=78 [Entry name]=H3-H4 histone dimer (human), containing histone variant H3.1 [PDB ID]=3afa [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,I,J,E,D,G,C chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone domain [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2210005,MF2200005,MF2200007,MF2200006,MF2200008,MF2200017 [UniProt ID chain A]=P68431 [UniProt boundaries chain A]=39-135 [UniProt coverage chain A]=71% [Name chain A]=Histone H3.1 [UniProt sequence chain A]=MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P62805 [UniProt boundaries chain B]=26-103 [UniProt coverage chain B]=75% [Name chain B]=Histone H4 [UniProt sequence chain B]=MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Homo sapiens [Accession]=MF2200005 [Entry] [Entry number]=79 [Entry name]=H3-H4 histone dimer (human), containing histone variant H3.2 [PDB ID]=3av1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,I,J,E,D,G,C chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone domain [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2210005,MF2200005,MF2200007,MF2200006,MF2200008,MF2200017 [UniProt ID chain A]=Q71DI3 [UniProt boundaries chain A]=40-135 [UniProt coverage chain A]=70% [Name chain A]=Histone H3.2 [UniProt sequence chain A]=MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P62805 [UniProt boundaries chain B]=26-103 [UniProt coverage chain B]=75% [Name chain B]=Histone H4 [UniProt sequence chain B]=MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Homo sapiens [Accession]=MF2200006 [Entry] [Entry number]=80 [Entry name]=H3-H4 histone dimer (human), containing histone variant H3.1t [PDB ID]=3a6n [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,I,J,E,D,G,C chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone domain [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2210005,MF2200005,MF2200007,MF2200006,MF2200008,MF2200017 [UniProt ID chain A]=Q16695 [UniProt boundaries chain A]=39-135 [UniProt coverage chain A]=71% [Name chain A]=Histone H3.1t [UniProt sequence chain A]=MARTKQTARKSTGGKAPRKQLATKVARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLMREIAQDFKTDLRFQSSAVMALQEACESYLVGLFEDTNLCVIHAKRVTIMPKDIQLARRIRGERA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P62805 [UniProt boundaries chain B]=23-103 [UniProt coverage chain B]=78% [Name chain B]=Histone H4 [UniProt sequence chain B]=MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Homo sapiens [Accession]=MF2200007 [Entry] [Entry number]=81 [Entry name]=H3-H4 histone dimer (human), containing histone variant H3.3 [PDB ID]=3av2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,I,J,E,D,G,C chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone domain [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2210005,MF2200005,MF2200007,MF2200006,MF2200008,MF2200017 [UniProt ID chain A]=P84243 [UniProt boundaries chain A]=39-135 [UniProt coverage chain A]=71% [Name chain A]=Histone H3.3 [UniProt sequence chain A]=MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P62805 [UniProt boundaries chain B]=26-103 [UniProt coverage chain B]=75% [Name chain B]=Histone H4 [UniProt sequence chain B]=MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Homo sapiens [Accession]=MF2200008 [Entry] [Entry number]=83 [Entry name]=H3-H4 histone dimer (Saccharomyces cerevisiae) [PDB ID]=1id3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,I,J,E,D,G,C chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone domain [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2210005,MF2200005,MF2200007,MF2200006,MF2200008,MF2200017 [UniProt ID chain A]=P61830 [UniProt boundaries chain A]=39-135 [UniProt coverage chain A]=71% [Name chain A]=Histone H3 [UniProt sequence chain A]=MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRVTIQKKDIKLARRLRGERS [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P02309 [UniProt boundaries chain B]=25-103 [UniProt coverage chain B]=76% [Name chain B]=Histone H4 [UniProt sequence chain B]=MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=3.10 [Source organism]=Saccharomyces cerevisiae [Accession]=MF2210005 [Entry] [Entry number]=84 [Entry name]=Transthyretin (Gallus gallus) [PDB ID]=1tfp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Transthyretin-like folds [Subclass]=Transthyretin [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P27731 [UniProt boundaries chain A]=33-146 [UniProt coverage chain A]=76% [Name chain A]=Transthyretin [UniProt sequence chain A]=MAFHSTLLVFLAGLVFLSEAAPLVSHGSVDSKCPLMVKVLDAVRGSPAANVAVKVFKKAADGTWQDFATGKTTEFGEIHELTTEEQFVEGVYRVEFDTSSYWKGLGLSPFHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSDPQE [Source organism chain A]=Gallus gallus [UniProt ID chain B]=P27731 [UniProt boundaries chain B]=33-146 [UniProt coverage chain B]=76% [Name chain B]=Transthyretin [UniProt sequence chain B]=MAFHSTLLVFLAGLVFLSEAAPLVSHGSVDSKCPLMVKVLDAVRGSPAANVAVKVFKKAADGTWQDFATGKTTEFGEIHELTTEEQFVEGVYRVEFDTSSYWKGLGLSPFHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSDPQE [Source organism chain B]=Gallus gallus [ExpTech]=X-ray [Resolution]=2.90 [Source organism]=Gallus gallus [Accession]=MF4110005 [Entry] [Entry number]=86 [Entry name]=HY5 leucine zipper homodimer [PDB ID]=2oqq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=bZIP transcription factor [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110006,MF2110009,MF7000301,MF7000302,MF7000303 [UniProt ID chain A]=O24646 [UniProt boundaries chain A]=111-150 [UniProt coverage chain A]=23% [Name chain A]=Transcription factor HY5 [UniProt sequence chain A]=MQEQATSSLAASSLPSSSERSSSSAPHLEIKEGIESDEEIRRVPEFGGEAVGKETSGRESGSATGQERTQATVGESQRKRGRTPAEKENKRLKRLLRNRVSAQQARERKKAYLSELENRVKDLENKNSELEERLSTLQNENQMLRHILKNTTGNKRGGGGGSNADASL [Source organism chain A]=Arabidopsis thaliana [UniProt ID chain B]=O24646 [UniProt boundaries chain B]=111-150 [UniProt coverage chain B]=23% [Name chain B]=Transcription factor HY5 [UniProt sequence chain B]=MQEQATSSLAASSLPSSSERSSSSAPHLEIKEGIESDEEIRRVPEFGGEAVGKETSGRESGSATGQERTQATVGESQRKRGRTPAEKENKRLKRLLRNRVSAQQARERKKAYLSELENRVKDLENKNSELEERLSTLQNENQMLRHILKNTTGNKRGGGGGSNADASL [Source organism chain B]=Arabidopsis thaliana [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Arabidopsis thaliana [Accession]=MF2110009 [Entry] [Entry number]=87 [Entry name]=c-Myc-Max heterodimeric leucine zipper [PDB ID]=1a93 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=Myc leucine zipper domain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:9680483). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2211002,MF7000007 [UniProt ID chain A]=P01106 [UniProt boundaries chain A]=420-449 [UniProt coverage chain A]=6% [Name chain A]=Myc proto-oncogene protein [UniProt sequence chain A]=MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P28574 [UniProt boundaries chain B]=74-102 [UniProt coverage chain B]=18% [Name chain B]=Protein max [UniProt sequence chain B]=MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGGTISAFDGGSDSSSESEPEEPQSRKKLRMEAS [Source organism chain B]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF2211002 [Entry] [Entry number]=88 [Entry name]=Heterodimer of ATF-4 and C/EBP beta [PDB ID]=1ci6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits of the dimer were shown to be disordered in their monomeric form with the structure arising as a result of the interaction (PMID:11018027). The subunits in the structure are bound via coiled coil interactions (PMID:11018027). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P18848 [UniProt boundaries chain A]=286-341 [UniProt coverage chain A]=15% [Name chain A]=Cyclic AMP-dependent transcription factor ATF-4 [UniProt sequence chain A]=MTEMSFLSSEVLVGDLMSPFDQSGLGAEESLGLLDDYLEVAKHFKPHGFSSDKAKAGSSEWLAVDGLVSPSNNSKEDAFSGTDWMLEKMDLKEFDLDALLGIDDLETMPDDLLTTLDDTCDLFAPLVQETNKQPPQTVNPIGHLPESLTKPDQVAPFTFLQPLPLSPGVLSSTPDHSFSLELGSEVDITEGDRKPDYTAYVAMIPQCIKEEDTPSDNDSGICMSPESYLGSPQHSPSTRGSPNRSLPSPGVLCGSARPKPYDPPGEKMVAAKVKGEKLDKKLKKMEQNKTAATRYRQKKRAEQEALTGECKELEKKNEALKERADSLAKEIQYLKDLIEEVRKARGKKRVP [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P28033 [UniProt boundaries chain B]=239-285 [UniProt coverage chain B]=15% [Name chain B]=CCAAT/enhancer-binding protein beta [UniProt sequence chain B]=MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAADFAAPAPAHHDFLSDLFADDYGAKPSKKPADYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKTVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF2201008 [Entry] [Entry number]=89 [Entry name]=General corepressor Tup1p [PDB ID]=3vp8 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:22707714). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=P16649 [UniProt boundaries chain A]=4-78 [UniProt coverage chain A]=10% [Name chain A]=General transcriptional corepressor TUP1 [UniProt sequence chain A]=MTASVSNTQNKLNELLDAIRQEFLQVSQEANTYRLQNQKDYDFKMNQQLAEMQQIRNTVYELELTHRKMKDAYEEEIKHLKLGLEQRDHQIASLTVQQQRQQQQQQQVQQHLQQQQQQLAAASASVPVAQQPPATTSATATPAANTTTGSPSAFPVQASRPNLVGSQLPTTTLPVVSSNAQQQLPQQQLQQQQLQQQQPPPQVSVAPLSNTAINGSPTSKETTTLPSVKAPESTLKETEPENNNTSKINDTGSATTATTTTATETEIKPKEEDATPASLHQDHYLVPYNQRANHSKPIPPFLLDLDSQSVPDALKKQTNDYYILYNPALPREIDVELHKSLDHTSVVCCVKFSNDGEYLATGCNKTTQVYRVSDGSLVARLSDDSAANNHRNSITENNTTTSTDNNTMTTTTTTTITTTAMTSAAELAKDVENLNTSSSPSSDLYIRSVCFSPDGKFLATGAEDRLIRIWDIENRKIVMILQGHEQDIYSLDYFPSGDKLVSGSGDRTVRIWDLRTGQCSLTLSIEDGVTTVAVSPGDGKYIAAGSLDRAVRVWDSETGFLVERLDSENESGTGHKDSVYSVVFTRDGQSVVSGSLDRSVKLWNLQNANNKSDSKTPNSGTCEVTYIGHKDFVLSVATTQNDEYILSGSKDRGVLFWDKKSGNPLLMLQGHRNSVISVAVANGSPLGPEYNVFATGSGDCKARIWKYKKIAPN [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P16649 [UniProt boundaries chain B]=2-81 [UniProt coverage chain B]=11% [Name chain B]=General transcriptional corepressor TUP1 [UniProt sequence chain B]=MTASVSNTQNKLNELLDAIRQEFLQVSQEANTYRLQNQKDYDFKMNQQLAEMQQIRNTVYELELTHRKMKDAYEEEIKHLKLGLEQRDHQIASLTVQQQRQQQQQQQVQQHLQQQQQQLAAASASVPVAQQPPATTSATATPAANTTTGSPSAFPVQASRPNLVGSQLPTTTLPVVSSNAQQQLPQQQLQQQQLQQQQPPPQVSVAPLSNTAINGSPTSKETTTLPSVKAPESTLKETEPENNNTSKINDTGSATTATTTTATETEIKPKEEDATPASLHQDHYLVPYNQRANHSKPIPPFLLDLDSQSVPDALKKQTNDYYILYNPALPREIDVELHKSLDHTSVVCCVKFSNDGEYLATGCNKTTQVYRVSDGSLVARLSDDSAANNHRNSITENNTTTSTDNNTMTTTTTTTITTTAMTSAAELAKDVENLNTSSSPSSDLYIRSVCFSPDGKFLATGAEDRLIRIWDIENRKIVMILQGHEQDIYSLDYFPSGDKLVSGSGDRTVRIWDLRTGQCSLTLSIEDGVTTVAVSPGDGKYIAAGSLDRAVRVWDSETGFLVERLDSENESGTGHKDSVYSVVFTRDGQSVVSGSLDRSVKLWNLQNANNKSDSKTPNSGTCEVTYIGHKDFVLSVATTQNDEYILSGSKDRGVLFWDKKSGNPLLMLQGHRNSVISVAVANGSPLGPEYNVFATGSGDCKARIWKYKKIAPN [Source organism chain B]=Saccharomyces cerevisiae [UniProt ID chain C]=P16649 [UniProt boundaries chain C]=4-80 [UniProt coverage chain C]=10% [Name chain C]=General transcriptional corepressor TUP1 [UniProt sequence chain C]=MTASVSNTQNKLNELLDAIRQEFLQVSQEANTYRLQNQKDYDFKMNQQLAEMQQIRNTVYELELTHRKMKDAYEEEIKHLKLGLEQRDHQIASLTVQQQRQQQQQQQVQQHLQQQQQQLAAASASVPVAQQPPATTSATATPAANTTTGSPSAFPVQASRPNLVGSQLPTTTLPVVSSNAQQQLPQQQLQQQQLQQQQPPPQVSVAPLSNTAINGSPTSKETTTLPSVKAPESTLKETEPENNNTSKINDTGSATTATTTTATETEIKPKEEDATPASLHQDHYLVPYNQRANHSKPIPPFLLDLDSQSVPDALKKQTNDYYILYNPALPREIDVELHKSLDHTSVVCCVKFSNDGEYLATGCNKTTQVYRVSDGSLVARLSDDSAANNHRNSITENNTTTSTDNNTMTTTTTTTITTTAMTSAAELAKDVENLNTSSSPSSDLYIRSVCFSPDGKFLATGAEDRLIRIWDIENRKIVMILQGHEQDIYSLDYFPSGDKLVSGSGDRTVRIWDLRTGQCSLTLSIEDGVTTVAVSPGDGKYIAAGSLDRAVRVWDSETGFLVERLDSENESGTGHKDSVYSVVFTRDGQSVVSGSLDRSVKLWNLQNANNKSDSKTPNSGTCEVTYIGHKDFVLSVATTQNDEYILSGSKDRGVLFWDKKSGNPLLMLQGHRNSVISVAVANGSPLGPEYNVFATGSGDCKARIWKYKKIAPN [Source organism chain C]=Saccharomyces cerevisiae [UniProt ID chain D]=P16649 [UniProt boundaries chain D]=2-79 [UniProt coverage chain D]=10% [Name chain D]=General transcriptional corepressor TUP1 [UniProt sequence chain D]=MTASVSNTQNKLNELLDAIRQEFLQVSQEANTYRLQNQKDYDFKMNQQLAEMQQIRNTVYELELTHRKMKDAYEEEIKHLKLGLEQRDHQIASLTVQQQRQQQQQQQVQQHLQQQQQQLAAASASVPVAQQPPATTSATATPAANTTTGSPSAFPVQASRPNLVGSQLPTTTLPVVSSNAQQQLPQQQLQQQQLQQQQPPPQVSVAPLSNTAINGSPTSKETTTLPSVKAPESTLKETEPENNNTSKINDTGSATTATTTTATETEIKPKEEDATPASLHQDHYLVPYNQRANHSKPIPPFLLDLDSQSVPDALKKQTNDYYILYNPALPREIDVELHKSLDHTSVVCCVKFSNDGEYLATGCNKTTQVYRVSDGSLVARLSDDSAANNHRNSITENNTTTSTDNNTMTTTTTTTITTTAMTSAAELAKDVENLNTSSSPSSDLYIRSVCFSPDGKFLATGAEDRLIRIWDIENRKIVMILQGHEQDIYSLDYFPSGDKLVSGSGDRTVRIWDLRTGQCSLTLSIEDGVTTVAVSPGDGKYIAAGSLDRAVRVWDSETGFLVERLDSENESGTGHKDSVYSVVFTRDGQSVVSGSLDRSVKLWNLQNANNKSDSKTPNSGTCEVTYIGHKDFVLSVATTQNDEYILSGSKDRGVLFWDKKSGNPLLMLQGHRNSVISVAVANGSPLGPEYNVFATGSGDCKARIWKYKKIAPN [Source organism chain D]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=1.91 [Source organism]=Saccharomyces cerevisiae [Accession]=MF4110006 [Entry] [Entry number]=92 [Entry name]=Rb C-terminal domain bound to an E2F1-DP1 heterodimer [PDB ID]=2aze [Chains]=A,B,C [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=3 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting partners have been shown to adopt a stable structure as a result of the interaction (PMID:16360038). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=The region(s) described in DP01427 covers 100% of the sequence present in the structure [Evidence chain C]=The region(s) described in DP01426 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=Q14186 [UniProt boundaries chain A]=199-346 [UniProt coverage chain A]=36% [Name chain A]=Transcription factor Dp-1 [UniProt sequence chain A]=MAKDAGLIEANGELKVFIDQNLSPGKGVVSLVAVHPSTVNPLGKQLLPKTFGQSNVNIAQQVVIGTPQRPAASNTLVVGSPHTPSTHFASQNQPSDSSPWSAGKRNRKGEKNGKGLRHFSMKVCEKVQRKGTTSYNEVADELVAEFSAADNHILPNESAYDQKNIRRRVYDALNVLMAMNIISKEKKEIKWIGLPTNSAQECQNLEVERQRRLERIKQKQSQLQELILQQIAFKNLVQRNRHAEQQASRPPPPNSVIHLPFIIVNTSKKTVIDCSISNDKFEYLFNFDNTFEIHDDIEVLKRMGMACGLESGSCSAEDLKMARSLVPKALEPYVTEMAQGTVGGVFITTAGSTSNGTRFSASDLTNGADGMLATSSNGSQYSGSRVETPVSYVGEDDEEDDDFNENDEDD [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q01094 [UniProt boundaries chain B]=201-301 [UniProt coverage chain B]=23% [Name chain B]=Transcription factor E2F1 [UniProt sequence chain B]=MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF [Source organism chain B]=Homo sapiens [UniProt ID chain C]=P06400 [UniProt boundaries chain C]=829-872 [UniProt coverage chain C]=4% [Name chain C]=Retinoblastoma-associated protein [UniProt sequence chain C]=MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK [Source organism chain C]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.55 [Source organism]=Homo sapiens [Accession]=MF3300001 [Entry] [Entry number]=93 [Entry name]=Rab11-binding domain of Rab11 family interacting protein 2 [PDB ID]=2k6s [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:19119858). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q7L804 [UniProt boundaries chain A]=450-489 [UniProt coverage chain A]=7% [Name chain A]=Rab11 family-interacting protein 2 [UniProt sequence chain A]=MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLIQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKNDGTFSDTSSAIIPSTHMPDANSEFSSGEIQMKSKPKKPFLLGPQRLSSAHSMSDLSGSHMSSEKLKAGTIGQTHLLGHQLDSFGTVPESGSLKSPHRRTLSFDTSKMNQPDSIVDEGELCFGRQNDPFTNVTASLPQKFATLPRKKNPFEESSETWDSSMNLFSKPIEIRKENKREKREKVSLFERVTGKKDSRRSDKLNNGGSDSPCDLKSPNAFSENRQDYFDYESTNPFTAKFRASNIMPSSSFHMSPTSNEDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFSNS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q7L804 [UniProt boundaries chain B]=450-489 [UniProt coverage chain B]=7% [Name chain B]=Rab11 family-interacting protein 2 [UniProt sequence chain B]=MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLIQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKNDGTFSDTSSAIIPSTHMPDANSEFSSGEIQMKSKPKKPFLLGPQRLSSAHSMSDLSGSHMSSEKLKAGTIGQTHLLGHQLDSFGTVPESGSLKSPHRRTLSFDTSKMNQPDSIVDEGELCFGRQNDPFTNVTASLPQKFATLPRKKNPFEESSETWDSSMNLFSKPIEIRKENKREKREKVSLFERVTGKKDSRRSDKLNNGGSDSPCDLKSPNAFSENRQDYFDYESTNPFTAKFRASNIMPSSSFHMSPTSNEDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFSNS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2100006 [Entry] [Entry number]=94 [Entry name]=p53 tetramerization domain (human) [PDB ID]=2j0z [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=p53 tetramerization [Sequence domain]=P53 tetramerisation domain [Evidence level]=Direct evidence [Evidence text]=p53, p63, p73 and their homologues are all members of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF4100003,MF4100005,MF4110007,MF4110009,MF4200002 [UniProt ID chain A]=P04637 [UniProt boundaries chain A]=326-356 [UniProt coverage chain A]=7% [Name chain A]=Cellular tumor antigen p53 [UniProt sequence chain A]=MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P04637 [UniProt boundaries chain B]=326-356 [UniProt coverage chain B]=7% [Name chain B]=Cellular tumor antigen p53 [UniProt sequence chain B]=MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD [Source organism chain B]=Homo sapiens [UniProt ID chain C]=P04637 [UniProt boundaries chain C]=326-356 [UniProt coverage chain C]=7% [Name chain C]=Cellular tumor antigen p53 [UniProt sequence chain C]=MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD [Source organism chain C]=Homo sapiens [UniProt ID chain D]=P04637 [UniProt boundaries chain D]=326-356 [UniProt coverage chain D]=7% [Name chain D]=Cellular tumor antigen p53 [UniProt sequence chain D]=MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD [Source organism chain D]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF4100003 [Entry] [Entry number]=95 [Entry name]=p53 tetramerization domain (Danio rerio) [PDB ID]=4d1l [Chains]=C,D,E,F [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=p53 tetramerization [Sequence domain]=P53 tetramerisation domain [Evidence level]=Direct evidence [Evidence text]=p53, p63, p73 and their homologues are all members of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Evidence chain E]=N/A [Evidence chain F]=N/A [Similar structures]=MF4100003,MF4100005,MF4110007,MF4110009,MF4200002 [UniProt ID chain C]=G1K2L5 [UniProt boundaries chain C]=302-341 [UniProt coverage chain C]=10% [Name chain C]=Cellular tumor antigen p53 [UniProt sequence chain C]=MAQNDSQEFAELWEKNLISIQPPGGGSCWDIINDEEYLPGSFDPNFFENVLEEQPQPSTLPPTSTVPETSDYPGDHGFRLRFPQSGTAKSVTCTYSPDLNKLFCQLAKTCPVQMVVDVAPPQGSVVRATAIYKKSEHVAEVVRRCPHHERTPDGDNLAPAGHLIRVEGNQRANYREDNITLRHSVFVPYEAPQLGAEWTTVLLNYMCNSSCMGGMNRRPILTIITLETQEGQLLGRRSFEVRVCACPGRDRKTEESNFKKDQETKTMAKTTTGTKRSLVKESSSATLRPEGSKKAKGSSSDEEIFTLQVRGRERYEILKKLNDSLELSDVVPASDAEKYRQKFMTKNKKENRESSEPKQGKKLMVKDEGRSDSD [Source organism chain C]=Danio rerio [UniProt ID chain D]=G1K2L5 [UniProt boundaries chain D]=302-342 [UniProt coverage chain D]=10% [Name chain D]=Cellular tumor antigen p53 [UniProt sequence chain D]=MAQNDSQEFAELWEKNLISIQPPGGGSCWDIINDEEYLPGSFDPNFFENVLEEQPQPSTLPPTSTVPETSDYPGDHGFRLRFPQSGTAKSVTCTYSPDLNKLFCQLAKTCPVQMVVDVAPPQGSVVRATAIYKKSEHVAEVVRRCPHHERTPDGDNLAPAGHLIRVEGNQRANYREDNITLRHSVFVPYEAPQLGAEWTTVLLNYMCNSSCMGGMNRRPILTIITLETQEGQLLGRRSFEVRVCACPGRDRKTEESNFKKDQETKTMAKTTTGTKRSLVKESSSATLRPEGSKKAKGSSSDEEIFTLQVRGRERYEILKKLNDSLELSDVVPASDAEKYRQKFMTKNKKENRESSEPKQGKKLMVKDEGRSDSD [Source organism chain D]=Danio rerio [UniProt ID chain E]=G1K2L5 [UniProt boundaries chain E]=303-343 [UniProt coverage chain E]=10% [Name chain E]=Cellular tumor antigen p53 [UniProt sequence chain E]=MAQNDSQEFAELWEKNLISIQPPGGGSCWDIINDEEYLPGSFDPNFFENVLEEQPQPSTLPPTSTVPETSDYPGDHGFRLRFPQSGTAKSVTCTYSPDLNKLFCQLAKTCPVQMVVDVAPPQGSVVRATAIYKKSEHVAEVVRRCPHHERTPDGDNLAPAGHLIRVEGNQRANYREDNITLRHSVFVPYEAPQLGAEWTTVLLNYMCNSSCMGGMNRRPILTIITLETQEGQLLGRRSFEVRVCACPGRDRKTEESNFKKDQETKTMAKTTTGTKRSLVKESSSATLRPEGSKKAKGSSSDEEIFTLQVRGRERYEILKKLNDSLELSDVVPASDAEKYRQKFMTKNKKENRESSEPKQGKKLMVKDEGRSDSD [Source organism chain E]=Danio rerio [UniProt ID chain F]=G1K2L5 [UniProt boundaries chain F]=302-340 [UniProt coverage chain F]=10% [Name chain F]=Cellular tumor antigen p53 [UniProt sequence chain F]=MAQNDSQEFAELWEKNLISIQPPGGGSCWDIINDEEYLPGSFDPNFFENVLEEQPQPSTLPPTSTVPETSDYPGDHGFRLRFPQSGTAKSVTCTYSPDLNKLFCQLAKTCPVQMVVDVAPPQGSVVRATAIYKKSEHVAEVVRRCPHHERTPDGDNLAPAGHLIRVEGNQRANYREDNITLRHSVFVPYEAPQLGAEWTTVLLNYMCNSSCMGGMNRRPILTIITLETQEGQLLGRRSFEVRVCACPGRDRKTEESNFKKDQETKTMAKTTTGTKRSLVKESSSATLRPEGSKKAKGSSSDEEIFTLQVRGRERYEILKKLNDSLELSDVVPASDAEKYRQKFMTKNKKENRESSEPKQGKKLMVKDEGRSDSD [Source organism chain F]=Danio rerio [ExpTech]=X-ray [Resolution]=1.97 [Source organism]=Danio rerio [Accession]=MF4110007 [Entry] [Entry number]=96 [Entry name]=p63 tetramerization domain (human) [PDB ID]=3zy1 [Chains]=A-3,A,A-4,A-2 [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=p53 tetramerization [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=p63 is a member of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-3]=N/A [Evidence chain A-4]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q9H3D4 [UniProt boundaries chain A]=398-437 [UniProt coverage chain A]=5% [Name chain A]=Tumor protein 63 [UniProt sequence chain A]=MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSTKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEEGE [Source organism chain A]=Homo sapiens [UniProt ID chain A-3]=Q9H3D4 [UniProt boundaries chain A-3]=398-437 [UniProt coverage chain A-3]=5% [Name chain A-3]=Tumor protein 63 [UniProt sequence chain A-3]=MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSTKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEEGE [Source organism chain A-3]=Homo sapiens [UniProt ID chain A-4]=Q9H3D4 [UniProt boundaries chain A-4]=398-437 [UniProt coverage chain A-4]=5% [Name chain A-4]=Tumor protein 63 [UniProt sequence chain A-4]=MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSTKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEEGE [Source organism chain A-4]=Homo sapiens [UniProt ID chain A-2]=Q9H3D4 [UniProt boundaries chain A-2]=398-437 [UniProt coverage chain A-2]=5% [Name chain A-2]=Tumor protein 63 [UniProt sequence chain A-2]=MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSTKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEEGE [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.15 [Source organism]=Homo sapiens [Accession]=MF4100004 [Entry] [Entry number]=97 [Entry name]=p73 tetramerization domain (human) [PDB ID]=2kby [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=p53 tetramerization [Sequence domain]=P53 tetramerisation domain [Evidence level]=Direct evidence [Evidence text]=p53, p63, p73 and their homologues are all members of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF4100003,MF4100005,MF4110007,MF4110009,MF4200002 [UniProt ID chain A]=O15350 [UniProt boundaries chain A]=351-398 [UniProt coverage chain A]=7% [Name chain A]=Tumor protein p73 [UniProt sequence chain A]=MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O15350 [UniProt boundaries chain B]=351-398 [UniProt coverage chain B]=7% [Name chain B]=Tumor protein p73 [UniProt sequence chain B]=MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH [Source organism chain B]=Homo sapiens [UniProt ID chain C]=O15350 [UniProt boundaries chain C]=351-398 [UniProt coverage chain C]=7% [Name chain C]=Tumor protein p73 [UniProt sequence chain C]=MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH [Source organism chain C]=Homo sapiens [UniProt ID chain D]=O15350 [UniProt boundaries chain D]=351-398 [UniProt coverage chain D]=7% [Name chain D]=Tumor protein p73 [UniProt sequence chain D]=MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH [Source organism chain D]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF4100005 [Entry] [Entry number]=98 [Entry name]=DNA-binding domain of the E2 protein (Human papillomavirus type 16) [PDB ID]=1r8p [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=E2 (early) protein, C terminal [Evidence level]=Direct evidence [Evidence text]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2140007,MF2140009,MF2140006,MF2140005,MF2140008 [UniProt ID chain A]=P03120 [UniProt boundaries chain A]=286-365 [UniProt coverage chain A]=21% [Name chain A]=Regulatory protein E2 [UniProt sequence chain A]=METLCQRLNVCQDKILTHYENDSTDLRDHIDYWKHMRLECAIYYKAREMGFKHINHQVVPTLAVSKNKALQAIELQLTLETIYNSQYSNEKWTLQDVSLEVYLTAPTGCIKKHGYTVEVQFDGDICNTMHYTNWTHIYICEEASVTVVEGQVDYYGLYYVHEGIRTYFVQFKDDAEKYSKNKVWEVHAGGQVILCPTSVFSSNEVSSPEIIRQHLANHPAATHTKAVALGTEETQTTIQRPRSEPDTGNPCHTTKLLHRDSVDSAPILTAFNSSHKGRINCNSNTTPIVHLKGDANTLKCLRYRFKKHCTLYTAVSSTWHWTGHNVKHKSAIVTLTYDSEWQRDQFLSQVKIPKTITVSTGFMSI [Source organism chain A]=Human papillomavirus type 16 [UniProt ID chain B]=P03120 [UniProt boundaries chain B]=286-365 [UniProt coverage chain B]=21% [Name chain B]=Regulatory protein E2 [UniProt sequence chain B]=METLCQRLNVCQDKILTHYENDSTDLRDHIDYWKHMRLECAIYYKAREMGFKHINHQVVPTLAVSKNKALQAIELQLTLETIYNSQYSNEKWTLQDVSLEVYLTAPTGCIKKHGYTVEVQFDGDICNTMHYTNWTHIYICEEASVTVVEGQVDYYGLYYVHEGIRTYFVQFKDDAEKYSKNKVWEVHAGGQVILCPTSVFSSNEVSSPEIIRQHLANHPAATHTKAVALGTEETQTTIQRPRSEPDTGNPCHTTKLLHRDSVDSAPILTAFNSSHKGRINCNSNTTPIVHLKGDANTLKCLRYRFKKHCTLYTAVSSTWHWTGHNVKHKSAIVTLTYDSEWQRDQFLSQVKIPKTITVSTGFMSI [Source organism chain B]=Human papillomavirus type 16 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Human papillomavirus type 16 [Accession]=MF2140005 [Entry] [Entry number]=99 [Entry name]=DNA-binding domain of the E2 protein (Human papillomavirus type 18) [PDB ID]=1f9f [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=E2 (early) protein, C terminal [Evidence level]=Direct evidence [Evidence text]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2140007,MF2140009,MF2140006,MF2140005,MF2140008 [UniProt ID chain A]=P06790 [UniProt boundaries chain A]=287-365 [UniProt coverage chain A]=21% [Name chain A]=Regulatory protein E2 [UniProt sequence chain A]=MQTPKETLSERLSCVQDKIIDHYENDSKDIDSQIQYWQLIRWENAIFFAAREHGIQTLNHQVVPAYNISKSKAHKAIELQMALQGLAQSAYKTEDWTLQDTCEELWNTEPTHCFKKGGQTVQVYFDGNKDNCMTYVAWDSVYYMTDAGTWDKTATCVSHRGLYYVKEGYNTFYIEFKSECEKYGNTGTWEVHFGNNVIDCNDSMCSTSDDTVSATQLVKQLQHTPSPYSSTVSVGTAKTYGQTSAATRPGHCGLAEKQHCGPVNPLLGAATPTGNNKRRKLCSGNTTPIIHLKGDRNSLKCLRYRLRKHSDHYRDISSTWHWTGAGNEKTGILTVTYHSETQRTKFLNTVAIPDSVQILVGYMTM [Source organism chain A]=Human papillomavirus type 18 [UniProt ID chain B]=P06790 [UniProt boundaries chain B]=287-365 [UniProt coverage chain B]=21% [Name chain B]=Regulatory protein E2 [UniProt sequence chain B]=MQTPKETLSERLSCVQDKIIDHYENDSKDIDSQIQYWQLIRWENAIFFAAREHGIQTLNHQVVPAYNISKSKAHKAIELQMALQGLAQSAYKTEDWTLQDTCEELWNTEPTHCFKKGGQTVQVYFDGNKDNCMTYVAWDSVYYMTDAGTWDKTATCVSHRGLYYVKEGYNTFYIEFKSECEKYGNTGTWEVHFGNNVIDCNDSMCSTSDDTVSATQLVKQLQHTPSPYSSTVSVGTAKTYGQTSAATRPGHCGLAEKQHCGPVNPLLGAATPTGNNKRRKLCSGNTTPIIHLKGDRNSLKCLRYRLRKHSDHYRDISSTWHWTGAGNEKTGILTVTYHSETQRTKFLNTVAIPDSVQILVGYMTM [Source organism chain B]=Human papillomavirus type 18 [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Human papillomavirus type 18 [Accession]=MF2140006 [Entry] [Entry number]=100 [Entry name]=DNA-binding domain of the E2 protein (Human papillomavirus type 31) [PDB ID]=1dhm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=E2 (early) protein, C terminal [Evidence level]=Direct evidence [Evidence text]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2140007,MF2140009,MF2140006,MF2140005,MF2140008 [UniProt ID chain A]=P17383 [UniProt boundaries chain A]=291-372 [UniProt coverage chain A]=22% [Name chain A]=Regulatory protein E2 [UniProt sequence chain A]=METLSQRLNVCQDKILEHYENDSKRLCDHIDYWKHIRLECVLMYKAREMGIHSINHQVVPALSVSKAKALQAIELQMMLETLNNTEYKNEDWTMQQTSLELYLTAPTGCLKKHGYTVEVQFDGDVHNTMHYTNWKFIYLCIDGQCTVVEGQVNCKGIYYVHEGHITYFVNFTEEAKKYGTGKKWEVHAGGQVIVFPESVFSSDEISFAGIVTKLPTANNTTTSNSKTCALGTSEGVRRATTSTKRPRTEPEHRNTHHPNKLLRGDSVDSVNCGVISAAACTNQTRAVSCPATTPIIHLKGDANILKCLRYRLSKYKQLYEQVSSTWHWTCTDGKHKNAIVTLTYISTSQRDDFLNTVKIPNTVSVSTGYMTI [Source organism chain A]=Human papillomavirus 31 [UniProt ID chain B]=P17383 [UniProt boundaries chain B]=291-372 [UniProt coverage chain B]=22% [Name chain B]=Regulatory protein E2 [UniProt sequence chain B]=METLSQRLNVCQDKILEHYENDSKRLCDHIDYWKHIRLECVLMYKAREMGIHSINHQVVPALSVSKAKALQAIELQMMLETLNNTEYKNEDWTMQQTSLELYLTAPTGCLKKHGYTVEVQFDGDVHNTMHYTNWKFIYLCIDGQCTVVEGQVNCKGIYYVHEGHITYFVNFTEEAKKYGTGKKWEVHAGGQVIVFPESVFSSDEISFAGIVTKLPTANNTTTSNSKTCALGTSEGVRRATTSTKRPRTEPEHRNTHHPNKLLRGDSVDSVNCGVISAAACTNQTRAVSCPATTPIIHLKGDANILKCLRYRLSKYKQLYEQVSSTWHWTCTDGKHKNAIVTLTYISTSQRDDFLNTVKIPNTVSVSTGYMTI [Source organism chain B]=Human papillomavirus 31 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Human papillomavirus 31 [Accession]=MF2140007 [Entry] [Entry number]=101 [Entry name]=DNA-binding domain of the E2 protein (Human papillomavirus type 6a) [PDB ID]=2aye [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=E2 (early) protein, C terminal [Evidence level]=Direct evidence [Evidence text]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2140007,MF2140009,MF2140006,MF2140005,MF2140008 [UniProt ID chain A]=Q84294 [UniProt boundaries chain A]=283-368 [UniProt coverage chain A]=23% [Name chain A]=Regulatory protein E2 [UniProt sequence chain A]=MEAIAKRLDACQEQLLELYEENSTDLNKHVLHWKCMRHESVLLYKAKQMGLSHIGMQVVPPLKVSEAKGHNAIEMQMHLESLLKTEYSMEPWTLQETSYEMWQTPPKRCFKKRGKTVEVKFDGCANNTMDYVVWTDVYVQDTDSWVKVHSMVDAKGIYYTCGQFKTYYVNFVKEAEKYGSTKQWEVCYGSTVICSPASVSSTTQEVSIPESTTYTPAQTSTPVSSSTQEDAVQTPPRKRARGVQQSPCNALCVAHIGPVDSGNHNLITNNHDQHQRRNNSNSSATPIVQFQGESNCLKCFRYRLNDKHRHLFDLISSTWHWASPKAPHKHAIVTVTYHSEEQRQQFLNVVKIPPTIRHKLGFMSLHLL [Source organism chain A]=Human papillomavirus type 6a [UniProt ID chain B]=Q84294 [UniProt boundaries chain B]=282-368 [UniProt coverage chain B]=23% [Name chain B]=Regulatory protein E2 [UniProt sequence chain B]=MEAIAKRLDACQEQLLELYEENSTDLNKHVLHWKCMRHESVLLYKAKQMGLSHIGMQVVPPLKVSEAKGHNAIEMQMHLESLLKTEYSMEPWTLQETSYEMWQTPPKRCFKKRGKTVEVKFDGCANNTMDYVVWTDVYVQDTDSWVKVHSMVDAKGIYYTCGQFKTYYVNFVKEAEKYGSTKQWEVCYGSTVICSPASVSSTTQEVSIPESTTYTPAQTSTPVSSSTQEDAVQTPPRKRARGVQQSPCNALCVAHIGPVDSGNHNLITNNHDQHQRRNNSNSSATPIVQFQGESNCLKCFRYRLNDKHRHLFDLISSTWHWASPKAPHKHAIVTVTYHSEEQRQQFLNVVKIPPTIRHKLGFMSLHLL [Source organism chain B]=Human papillomavirus type 6a [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Human papillomavirus type 6a [Accession]=MF2140008 [Entry] [Entry number]=102 [Entry name]=DNA-binding domain of the E2 protein (Bovine papillomavirus type 1) [PDB ID]=1dbd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=E2 (early) protein, C terminal [Evidence level]=Direct evidence [Evidence text]=The DNA binding domain of E2 was shown to exhibit a two-state concerted unfolding and dissociation in denaturation/renaturation experiments (PMID:8745409,PMID:8756330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2140007,MF2140009,MF2140006,MF2140005,MF2140008 [UniProt ID chain A]=P03122 [UniProt boundaries chain A]=311-410 [UniProt coverage chain A]=24% [Name chain A]=Regulatory protein E2 [UniProt sequence chain A]=METACERLHVAQETQMQLIEKSSDKLQDHILYWTAVRTENTLLYAARKKGVTVLGHCRVPHSVVCQERAKQAIEMQLSLQELSKTEFGDEPWSLLDTSWDRYMSEPKRCFKKGARVVEVEFDGNASNTNWYTVYSNLYMRTEDGWQLAKAGADGTGLYYCTMAGAGRIYYSRFGDEAARFSTTGHYSVRDQDRVYAGVSSTSSDFRDRPDGVWVASEGPEGDPAGKEAEPAQPVSSLLGSPACGPIRAGLGWVRDGPRSHPYNFPAGSGGSILRSSSTPVQGTVPVDLASRQEEEEQSPDSTEEEPVTLPRRTTNDGFHLLKAGGSCFALISGTANQVKCYRFRVKKNHRHRYENCTTTWFTVADNGAERQGQAQILITFGSPSQRQDFLKHVPLPPGMNISGFTASLDF [Source organism chain A]=Bovine papillomavirus type 1 [UniProt ID chain B]=P03122 [UniProt boundaries chain B]=311-410 [UniProt coverage chain B]=24% [Name chain B]=Regulatory protein E2 [UniProt sequence chain B]=METACERLHVAQETQMQLIEKSSDKLQDHILYWTAVRTENTLLYAARKKGVTVLGHCRVPHSVVCQERAKQAIEMQLSLQELSKTEFGDEPWSLLDTSWDRYMSEPKRCFKKGARVVEVEFDGNASNTNWYTVYSNLYMRTEDGWQLAKAGADGTGLYYCTMAGAGRIYYSRFGDEAARFSTTGHYSVRDQDRVYAGVSSTSSDFRDRPDGVWVASEGPEGDPAGKEAEPAQPVSSLLGSPACGPIRAGLGWVRDGPRSHPYNFPAGSGGSILRSSSTPVQGTVPVDLASRQEEEEQSPDSTEEEPVTLPRRTTNDGFHLLKAGGSCFALISGTANQVKCYRFRVKKNHRHRYENCTTTWFTVADNGAERQGQAQILITFGSPSQRQDFLKHVPLPPGMNISGFTASLDF [Source organism chain B]=Bovine papillomavirus type 1 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bovine papillomavirus type 1 [Accession]=MF2140009 [Entry] [Entry number]=103 [Entry name]=Heat shock factor binding protein 1 (HSBP1) [PDB ID]=3ci9 [Chains]=A,B-3,A-2,A-3,B,B-2 [Total number of chains]=6 [Assembly]=Hexamer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (hexameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:18767159). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain B-3]=N/A [Evidence chain A-2]=N/A [Evidence chain A-3]=N/A [Evidence chain B-2]=N/A [Similar structures]=None [UniProt ID chain A]=O75506 [UniProt boundaries chain A]=6-49 [UniProt coverage chain A]=57% [Name chain A]=Heat shock factor-binding protein 1 [UniProt sequence chain A]=MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O75506 [UniProt boundaries chain B]=9-53 [UniProt coverage chain B]=59% [Name chain B]=Heat shock factor-binding protein 1 [UniProt sequence chain B]=MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS [Source organism chain B]=Homo sapiens [UniProt ID chain B-3]=O75506 [UniProt boundaries chain B-3]=9-53 [UniProt coverage chain B-3]=59% [Name chain B-3]=Heat shock factor-binding protein 1 [UniProt sequence chain B-3]=MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS [Source organism chain B-3]=Homo sapiens [UniProt ID chain A-2]=O75506 [UniProt boundaries chain A-2]=9-53 [UniProt coverage chain A-2]=59% [Name chain A-2]=Heat shock factor-binding protein 1 [UniProt sequence chain A-2]=MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS [Source organism chain A-2]=Homo sapiens [UniProt ID chain A-3]=O75506 [UniProt boundaries chain A-3]=9-53 [UniProt coverage chain A-3]=59% [Name chain A-3]=Heat shock factor-binding protein 1 [UniProt sequence chain A-3]=MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS [Source organism chain A-3]=Homo sapiens [UniProt ID chain B-2]=O75506 [UniProt boundaries chain B-2]=9-53 [UniProt coverage chain B-2]=59% [Name chain B-2]=Heat shock factor-binding protein 1 [UniProt sequence chain B-2]=MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS [Source organism chain B-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF6100001 [Entry] [Entry number]=104 [Entry name]=4-oxalocrotonate tautomerase [PDB ID]=4x19 [Chains]=A,B,C,D,E,F [Total number of chains]=6 [Assembly]=Hexamer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homohexameric enzymes [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=4-oxalocrotonate tautomerase hexamer from Pseudomonas putida was shown by DSC to follow a two-state folding with the hexameric, dimeric and secondary structure all melting at the same temperature (PMID:20465238). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Evidence chain E]=N/A [Evidence chain F]=N/A [Similar structures]=None [UniProt ID chain A]=Q01468 [UniProt boundaries chain A]=2-58 [UniProt coverage chain A]=90% [Name chain A]=2-hydroxymuconate tautomerase [UniProt sequence chain A]=MPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR [Source organism chain A]=Pseudomonas putida [UniProt ID chain B]=Q01468 [UniProt boundaries chain B]=2-57 [UniProt coverage chain B]=88% [Name chain B]=2-hydroxymuconate tautomerase [UniProt sequence chain B]=MPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR [Source organism chain B]=Pseudomonas putida [UniProt ID chain C]=Q01468 [UniProt boundaries chain C]=2-58 [UniProt coverage chain C]=90% [Name chain C]=2-hydroxymuconate tautomerase [UniProt sequence chain C]=MPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR [Source organism chain C]=Pseudomonas putida [UniProt ID chain D]=Q01468 [UniProt boundaries chain D]=2-58 [UniProt coverage chain D]=90% [Name chain D]=2-hydroxymuconate tautomerase [UniProt sequence chain D]=MPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR [Source organism chain D]=Pseudomonas putida [UniProt ID chain E]=Q01468 [UniProt boundaries chain E]=2-58 [UniProt coverage chain E]=90% [Name chain E]=2-hydroxymuconate tautomerase [UniProt sequence chain E]=MPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR [Source organism chain E]=Pseudomonas putida [UniProt ID chain F]=Q01468 [UniProt boundaries chain F]=2-58 [UniProt coverage chain F]=90% [Name chain F]=2-hydroxymuconate tautomerase [UniProt sequence chain F]=MPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR [Source organism chain F]=Pseudomonas putida [ExpTech]=X-ray [Resolution]=1.94 [Source organism]=Pseudomonas putida [Accession]=MF6120001 [Entry] [Entry number]=105 [Entry name]=Escherichia coli met repressor (MetJ) [PDB ID]=1cmb [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=MetJ was shown by differential scanning calorimetry to follow a two-state folding and dimerization (PMID:1390748). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P0A8U6 [UniProt boundaries chain A]=2-105 [UniProt coverage chain A]=99% [Name chain A]=Met repressor [UniProt sequence chain A]=MAEWSGEYISPYAEHGKKSEQVKKITVSIPLKVLKILTDERTRRQVNNLRHATNSELLCEAFLHAFTGQPLPDDADLRKERSDEIPEAAKEIMREMGINPETWEY [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0A8U6 [UniProt boundaries chain B]=2-105 [UniProt coverage chain B]=99% [Name chain B]=Met repressor [UniProt sequence chain B]=MAEWSGEYISPYAEHGKKSEQVKKITVSIPLKVLKILTDERTRRQVNNLRHATNSELLCEAFLHAFTGQPLPDDADLRKERSDEIPEAAKEIMREMGINPETWEY [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Escherichia coli [Accession]=MF2120019 [Entry] [Entry number]=106 [Entry name]=Nerve growth factor (NGF) [PDB ID]=1bet [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=NGF-like [Sequence domain]=Cystine-knot cytokine/NGF-like [Evidence level]=Direct evidence [Evidence text]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF2110010,MF2200009,MF2100007,MF2100008,MF2201009,MF2110022,MF2110011,MF7000016,MF7000017 [UniProt ID chain A]=P01139 [UniProt boundaries chain A]=131-237 [UniProt coverage chain A]=44% [Name chain A]=Beta-nerve growth factor [UniProt sequence chain A]=MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=P01139 [UniProt boundaries chain A-2]=131-237 [UniProt coverage chain A-2]=44% [Name chain A-2]=Beta-nerve growth factor [UniProt sequence chain A-2]=MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Mus musculus [Accession]=MF2110010 [Entry] [Entry number]=107 [Entry name]=Neurotrophin 3 homodimer [PDB ID]=1b8k [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=NGF-like [Sequence domain]=Cystine-knot cytokine/NGF-like [Evidence level]=Direct evidence [Evidence text]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF2110010,MF2200009,MF2100007,MF2100008,MF2201009,MF2110022,MF2110011,MF7000016,MF7000017 [UniProt ID chain A]=P20783 [UniProt boundaries chain A]=149-250 [UniProt coverage chain A]=39% [Name chain A]=Neurotrophin-3 [UniProt sequence chain A]=MSILFYVIFLAYLRGIQGNNMDQRSLPEDSLNSLIIKLIQADILKNKLSKQMVDVKENYQSTLPKAEAPREPERGGPAKSAFQPVIAMDTELLRQQRRYNSPRVLLSDSTPLEPPPLYLMEDYVGSPVVANRTSRRKRYAEHKSHRGEYSVCDSESLWVTDKSSAIDIRGHQVTVLGEIKTGNSPVKQYFYETRCKEARPVKNGCRGIDDKHWNSQCKTSQTYVRALTSENNKLVGWRWIRIDTSCVCALSRKIGRT [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P20783 [UniProt boundaries chain A-2]=149-250 [UniProt coverage chain A-2]=39% [Name chain A-2]=Neurotrophin-3 [UniProt sequence chain A-2]=MSILFYVIFLAYLRGIQGNNMDQRSLPEDSLNSLIIKLIQADILKNKLSKQMVDVKENYQSTLPKAEAPREPERGGPAKSAFQPVIAMDTELLRQQRRYNSPRVLLSDSTPLEPPPLYLMEDYVGSPVVANRTSRRKRYAEHKSHRGEYSVCDSESLWVTDKSSAIDIRGHQVTVLGEIKTGNSPVKQYFYETRCKEARPVKNGCRGIDDKHWNSQCKTSQTYVRALTSENNKLVGWRWIRIDTSCVCALSRKIGRT [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.15 [Source organism]=Homo sapiens [Accession]=MF2100007 [Entry] [Entry number]=108 [Entry name]=Neurotrophin 4 homodimer [PDB ID]=1b98 [Chains]=A,M [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=NGF-like [Sequence domain]=Cystine-knot cytokine/NGF-like [Evidence level]=Direct evidence [Evidence text]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain M]=N/A [Similar structures]=MF2110010,MF2200009,MF2100007,MF2100008,MF2201009,MF2110022,MF2110011,MF7000016,MF7000017 [UniProt ID chain A]=P34130 [UniProt boundaries chain A]=93-207 [UniProt coverage chain A]=54% [Name chain A]=Neurotrophin-4 [UniProt sequence chain A]=MLPLPSCSLPILLLFLLPSVPIESQPPPSTLPPFLAPEWDLLSPRVVLSRGAPAGPPLLFLLEAGAFRESAGAPANRSRRGVSETAPASRRGELAVCDAVSGWVTDRRTAVDLRGREVEVLGEVPAAGGSPLRQYFFETRCKADNAEEGGPGAGGGGCRGVDRRHWVSECKAKQSYVRALTADAQGRVGWRWIRIDTACVCTLLSRTGRA [Source organism chain A]=Homo sapiens [UniProt ID chain M]=P34130 [UniProt boundaries chain M]=91-206 [UniProt coverage chain M]=55% [Name chain M]=Neurotrophin-4 [UniProt sequence chain M]=MLPLPSCSLPILLLFLLPSVPIESQPPPSTLPPFLAPEWDLLSPRVVLSRGAPAGPPLLFLLEAGAFRESAGAPANRSRRGVSETAPASRRGELAVCDAVSGWVTDRRTAVDLRGREVEVLGEVPAAGGSPLRQYFFETRCKADNAEEGGPGAGGGGCRGVDRRHWVSECKAKQSYVRALTADAQGRVGWRWIRIDTACVCTLLSRTGRA [Source organism chain M]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.75 [Source organism]=Homo sapiens [Accession]=MF2100008 [Entry] [Entry number]=109 [Entry name]=Brain-derived neurotrophic factor/neurotrophin 3 heterodimer [PDB ID]=1bnd [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe A-2,B chains were not considered. [Class]=Cystine-knot cytokines [Subclass]=NGF-like [Sequence domain]=Cystine-knot cytokine/NGF-like [Evidence level]=Direct evidence [Evidence text]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=MF2110010,MF2200009,MF2100007,MF2100008,MF2201009,MF2110022,MF2110011,MF7000016,MF7000017 [UniProt ID chain A]=P23560 [UniProt boundaries chain A]=136-244 [UniProt coverage chain A]=44% [Name chain A]=Brain-derived neurotrophic factor [UniProt sequence chain A]=MTILFLTMVISYFGCMKAAPMKEANIRGQGGLAYPGVRTHGTLESVNGPKAGSRGLTSLADTFEHVIEELLDEDQKVRPNEENNKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR [Source organism chain A]=Homo sapiens [UniProt ID chain B-2]=P20783 [UniProt boundaries chain B-2]=146-253 [UniProt coverage chain B-2]=42% [Name chain B-2]=Neurotrophin-3 [UniProt sequence chain B-2]=MSILFYVIFLAYLRGIQGNNMDQRSLPEDSLNSLIIKLIQADILKNKLSKQMVDVKENYQSTLPKAEAPREPERGGPAKSAFQPVIAMDTELLRQQRRYNSPRVLLSDSTPLEPPPLYLMEDYVGSPVVANRTSRRKRYAEHKSHRGEYSVCDSESLWVTDKSSAIDIRGHQVTVLGEIKTGNSPVKQYFYETRCKEARPVKNGCRGIDDKHWNSQCKTSQTYVRALTSENNKLVGWRWIRIDTSCVCALSRKIGRT [Source organism chain B-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Homo sapiens [Accession]=MF2200009 [Entry] [Entry number]=110 [Entry name]=Brain-derived neurotrophic factor/neurotrophin 4 heterodimer [PDB ID]=1b8m [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=NGF-like [Sequence domain]=Cystine-knot cytokine/NGF-like [Evidence level]=Direct evidence [Evidence text]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110010,MF2200009,MF2100007,MF2100008,MF2201009,MF2110022,MF2110011,MF7000016,MF7000017 [UniProt ID chain A]=P23560 [UniProt boundaries chain A]=136-244 [UniProt coverage chain A]=44% [Name chain A]=Brain-derived neurotrophic factor [UniProt sequence chain A]=MTILFLTMVISYFGCMKAAPMKEANIRGQGGLAYPGVRTHGTLESVNGPKAGSRGLTSLADTFEHVIEELLDEDQKVRPNEENNKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P34130 [UniProt boundaries chain B]=92-210 [UniProt coverage chain B]=56% [Name chain B]=Neurotrophin-4 [UniProt sequence chain B]=MLPLPSCSLPILLLFLLPSVPIESQPPPSTLPPFLAPEWDLLSPRVVLSRGAPAGPPLLFLLEAGAFRESAGAPANRSRRGVSETAPASRRGELAVCDAVSGWVTDRRTAVDLRGREVEVLGEVPAAGGSPLRQYFFETRCKADNAEEGGPGAGGGGCRGVDRRHWVSECKAKQSYVRALTADAQGRVGWRWIRIDTACVCTLLSRTGRA [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.75 [Source organism]=Homo sapiens [Accession]=MF2201009 [Entry] [Entry number]=111 [Entry name]=Ovulation-inducing factor (OIF) from llama seminal plasma [PDB ID]=4efv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=NGF-like [Sequence domain]=Cystine-knot cytokine/NGF-like [Evidence level]=Direct evidence [Evidence text]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110010,MF2200009,MF2100007,MF2100008,MF2201009,MF2110022,MF2110011,MF7000016,MF7000017 [UniProt ID chain A]=J9PBR9 [UniProt boundaries chain A]=9-116 [UniProt coverage chain A]=92% [Name chain A]=Ovulation-inducing factor (OIF) [UniProt sequence chain A]=APSHPIFHRGEFSVCDSVSVWVADKTTATDIKGKEVMVLGEVNINNSVFKQYFFETKCRDPNPVASGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTACVCVLSKKAS [Source organism chain A]=Lama glama [UniProt ID chain B]=J9PBR9 [UniProt boundaries chain B]=10-117 [UniProt coverage chain B]=92% [Name chain B]=Ovulation-inducing factor (OIF) [UniProt sequence chain B]=APSHPIFHRGEFSVCDSVSVWVADKTTATDIKGKEVMVLGEVNINNSVFKQYFFETKCRDPNPVASGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTACVCVLSKKAS [Source organism chain B]=Lama glama [ExpTech]=X-ray [Resolution]=2.32 [Source organism]=Lama glama [Accession]=MF2110011 [Entry] [Entry number]=112 [Entry name]=Dimerization domain of HNF-1alpha [PDB ID]=1jb6 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=HNF dimer The thermal and chemical equilibrium unfolding of a 32-residue α-helical peptide comprising the dimerization domain of HNF-1 was monitored by circular dichroism spectroscopy. The conformational stability of this peptide was shown to be concentration dependent, and the unfolding reaction is described as a two-state transition between folded dimers and unfolded monomers (PMID:1988015). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P22361 [UniProt boundaries chain A]=1-33 [UniProt coverage chain A]=5% [Name chain A]=Hepatocyte nuclear factor 1-alpha [UniProt sequence chain A]=MVSKLSQLQTELLAALLESGLSKEALIQALGEPGPYLMVGEGPLDKGESCGGSRGDLTELPNGLGETRGSEDDTDDDGEDFAPPILKELENLSPEEAAHQKAVVESLLQEDPWRVAKMVKSYLQQHNIPQREVVDTTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREVAQQFTHAGQGGLIEEPTGDELPTKKGRRNRFKWGPASQQILFQAYERQKNPSKEERETLVEECNRAECIQRGVSPSQAQGLGSNLVTEVRVYNWFANRRKEEAFRHKLAMDTYNGPPPGPGPGPALPAHSSPGLPTTTLSPSKVHGVRYGQSATSEAAEVPSSSGGPLVTVSAALHQVSPTGLEPSSLLSTEAKLVSATGGPLPPVSTLTALHSLEQTSPGLNQQPQNLIMASLPGVMTIGPGEPASLGPTFTNTGASTLVIGLASTQAQSVPVINSMGSSLTTLQPVQFSQPLHPSYQQPLMPPVQSHVAQSPFMATMAQLQSPHALYSHKPEVAQYTHTSLLPQTMLITDTNLSTLASLTPTKQVFTSDTEASSEPGLHEPPSPATTIHIPSQDPSNIQHLQPAHRLSTSPTVSSSSLVLYQSSDSNGHSHLLPSNHSVIETFISTQMASSSQ [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=P22361 [UniProt boundaries chain A-2]=3-30 [UniProt coverage chain A-2]=4% [Name chain A-2]=Hepatocyte nuclear factor 1-alpha [UniProt sequence chain A-2]=MVSKLSQLQTELLAALLESGLSKEALIQALGEPGPYLMVGEGPLDKGESCGGSRGDLTELPNGLGETRGSEDDTDDDGEDFAPPILKELENLSPEEAAHQKAVVESLLQEDPWRVAKMVKSYLQQHNIPQREVVDTTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREVAQQFTHAGQGGLIEEPTGDELPTKKGRRNRFKWGPASQQILFQAYERQKNPSKEERETLVEECNRAECIQRGVSPSQAQGLGSNLVTEVRVYNWFANRRKEEAFRHKLAMDTYNGPPPGPGPGPALPAHSSPGLPTTTLSPSKVHGVRYGQSATSEAAEVPSSSGGPLVTVSAALHQVSPTGLEPSSLLSTEAKLVSATGGPLPPVSTLTALHSLEQTSPGLNQQPQNLIMASLPGVMTIGPGEPASLGPTFTNTGASTLVIGLASTQAQSVPVINSMGSSLTTLQPVQFSQPLHPSYQQPLMPPVQSHVAQSPFMATMAQLQSPHALYSHKPEVAQYTHTSLLPQTMLITDTNLSTLASLTPTKQVFTSDTEASSEPGLHEPPSPATTIHIPSQDPSNIQHLQPAHRLSTSPTVSSSSLVLYQSSDSNGHSHLLPSNHSVIETFISTQMASSSQ [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Mus musculus [Accession]=MF2110012 [Entry] [Entry number]=113 [Entry name]=Factor for inversion stimulation (FIS) [PDB ID]=1ety [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=DNA-binding HTH domain and helical dimerization domain [Sequence domain]=Fis-type HTH domain transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=FIS forms an intertwined homodimer. Helices A and B join of the two monomer to form an antiparallel four-helix bundle. Equilibrium and kinetic methods have shown that FIS follows a two-step folding reaction where the two unfolded monomers associate to a dimeric intermediate during a fast phase, which is followed by a slower, subsequent folding of the dimeric intermediate to the native dimer (PMID:14698300). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000982,MF2120020 [UniProt ID chain A]=P0A6R3 [UniProt boundaries chain A]=10-98 [UniProt coverage chain A]=90% [Name chain A]=DNA-binding protein Fis [UniProt sequence chain A]=MFEQRVNSDVLTVSTVNSQDQVTQKPLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEQPLLDMVMQYTRGNQTRAALMMGINRGTLRKKLKKYGMN [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0A6R3 [UniProt boundaries chain B]=6-98 [UniProt coverage chain B]=94% [Name chain B]=DNA-binding protein Fis [UniProt sequence chain B]=MFEQRVNSDVLTVSTVNSQDQVTQKPLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEQPLLDMVMQYTRGNQTRAALMMGINRGTLRKKLKKYGMN [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Escherichia coli [Accession]=MF2120020 [Entry] [Entry number]=114 [Entry name]=Neuronal SNARE core complex (Vamp2 / Syntaxin-1A / SNAP25) [PDB ID]=1n7s [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=3 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric, 4-helix bundle) [Sequence domain]=Synaptobrevin,SNARE domain [Evidence level]=Direct evidence [Evidence text]=The structure shows the core domain of a SNARE complex (PMID:12496247). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00622 covers 98% of the sequence present in the structure [Evidence chain B]=N/A [Evidence chain C]=The region(s) described in DP00068 covers 100% of the sequence present in the structure [Evidence chain D]=The region(s) described in DP00068 covers 100% of the sequence present in the structure [Similar structures]=MF4410001,MF4410002 [UniProt ID chain A]=P63045 [UniProt boundaries chain A]=27-89 [UniProt coverage chain A]=54% [Name chain A]=Vesicle-associated membrane protein 2 [UniProt sequence chain A]=MSATAATVPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFST [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P32851 [UniProt boundaries chain B]=191-256 [UniProt coverage chain B]=22% [Name chain B]=Syntaxin-1A [UniProt sequence chain B]=MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG [Source organism chain B]=Rattus norvegicus [UniProt ID chain C]=P60881 [UniProt boundaries chain C]=7-83 [UniProt coverage chain C]=37% [Name chain C]=Synaptosomal-associated protein 25 [UniProt sequence chain C]=MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG [Source organism chain C]=Rattus norvegicus [UniProt ID chain D]=P60881 [UniProt boundaries chain D]=141-204 [UniProt coverage chain D]=31% [Name chain D]=Synaptosomal-associated protein 25 [UniProt sequence chain D]=MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG [Source organism chain D]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=1.45 [Source organism]=Rattus norvegicus [Accession]=MF4410001 [Entry] [Entry number]=115 [Entry name]=Autophagic SNARE core complex (Vamp8 / Syntaxin-17 / SNAP29) [PDB ID]=4wy4 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=3 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric, 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The structure shows the core domain of a SNARE complex (PMID:25686604). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=The region(s) described in DP03670 covers 100% of the sequence present in the structure [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=Q9BV40 [UniProt boundaries chain A]=11-74 [UniProt coverage chain A]=64% [Name chain A]=Vesicle-associated membrane protein 8 [UniProt sequence chain A]=MEEASEGGGNDRVRNLQSEVEGVKNIMTQNVERILARGENLEHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVLICVIVFIIILFIVLFATGAFS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P56962 [UniProt boundaries chain B]=170-227 [UniProt coverage chain B]=19% [Name chain B]=Syntaxin-17 [UniProt sequence chain B]=MSEDEEKVKLRRLEPAIQKFIKIVIPTDLERLRKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREIEKLCLKVRKDDLVLLKRMIDPVKEEASAATAEFLQLHLESVEELKKQFNDEETLLQPPLTRSMTVGGAFHTTEAEASSQSLTQIYALPEIPQDQNAAESWETLEADLIELSQLVTDFSLLVNSQQEKIDSIADHVNSAAVNVEEGTKNLGKAAKYKLAALPVAGALIGGMVGGPIGLLAGFKVAGIAAALGGGVLGFTGGKLIQRKKQKMMEKLTSSCPDLPSQTDKKCS [Source organism chain B]=Homo sapiens [UniProt ID chain C]=O95721 [UniProt boundaries chain C]=39-116 [UniProt coverage chain C]=30% [Name chain C]=Synaptosomal-associated protein 29 [UniProt sequence chain C]=MSAYPKSYNPFDDDGEDEGARPAPWRDARDLPDGPDAPADRQQYLRQEVLRRAEATAASTSRSLALMYESEKVGVASSEELARQRGVLERTEKMVDKMDQDLKISQKHINSIKSVFGGLVNYFKSKPVETPPEQNGTLTSQPNNRLKEAISTSKEQEAKYQASHPNLRKLDDTDPVPRGAGSAMSTDAYPKNPHLRAYHQKIDSNLDELSMGLGRLKDIALGMQTEIEEQDDILDRLTTKVDKLDVNIKSTERKVRQL [Source organism chain C]=Homo sapiens [UniProt ID chain D]=O95721 [UniProt boundaries chain D]=194-258 [UniProt coverage chain D]=25% [Name chain D]=Synaptosomal-associated protein 29 [UniProt sequence chain D]=MSAYPKSYNPFDDDGEDEGARPAPWRDARDLPDGPDAPADRQQYLRQEVLRRAEATAASTSRSLALMYESEKVGVASSEELARQRGVLERTEKMVDKMDQDLKISQKHINSIKSVFGGLVNYFKSKPVETPPEQNGTLTSQPNNRLKEAISTSKEQEAKYQASHPNLRKLDDTDPVPRGAGSAMSTDAYPKNPHLRAYHQKIDSNLDELSMGLGRLKDIALGMQTEIEEQDDILDRLTTKVDKLDVNIKSTERKVRQL [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Homo sapiens [Accession]=MF4400001 [Entry] [Entry number]=116 [Entry name]=Endosomal SNARE core complex (Vamp4 / Vti1-rp2 / Syntaxin-6 / Syntaxin-13) [PDB ID]=2nps [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=4 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric, 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The structure shows the core domain of a SNARE complex (PMID:17159904). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01498 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01501 covers 100% of the sequence present in the structure [Evidence chain C]=The region(s) described in DP01499 covers 93% of the sequence present in the structure [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=O70480 [UniProt boundaries chain A]=49-111 [UniProt coverage chain A]=44% [Name chain A]=Vesicle-associated membrane protein 4 [UniProt sequence chain A]=MPPKFKRHLNDDDVTGSVKSERRNLLEDDSDEEEDFFLRGPSGPRFGPRNDKIKHVQNQVDEVIDVMQENITKVIERGERLDELQDKSESLSDNATAFSNRSKQLRRQMWWRGCKIKAIMALAAAILLLMIIILIVVKFRT [Source organism chain A]=Mus musculus [UniProt ID chain B]=G3V7P1 [UniProt boundaries chain B]=184-248 [UniProt coverage chain B]=23% [Name chain B]=Syntaxin-12 [UniProt sequence chain B]=MSYGPLDMYRNPGPSGPQPRDFNSIIQTCSGNIQRISQATAQIKNLMSQLGTKQDSSKLQENLQQFQHSTNQLAKETNELLKELGSLPLPLSASEQRQQKLQKERLMNDFSSALNNFQVVQRKVSEKEKESIARARAGSRLSAEDRQREEQLVSFDSHEEWNQMQSQEEEAAITEQDLELIKERETAIQQLEADILDVNQIFKDLAMMIHDQGDLIDSIEANVESSEVHVERASDQLQRAAYYQKKSRKKMCILVLVLSVIVTVLVVVIWVASK [Source organism chain B]=Rattus norvegicus [UniProt ID chain C]=Q9JI51 [UniProt boundaries chain C]=122-197 [UniProt coverage chain C]=33% [Name chain C]=Vesicle transport through interaction with t-SNAREs homolog 1A [UniProt sequence chain C]=MSADFEGYEQDFAVLTAEITSKISRVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDAGNSSENQLIKLREERAHLLDNTERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTGMLRRIIQNRILLVILGIIVVITILTAITFFVRGH [Source organism chain C]=Rattus norvegicus [UniProt ID chain D]=O43752 [UniProt boundaries chain D]=170-232 [UniProt coverage chain D]=24% [Name chain D]=Syntaxin-6 [UniProt sequence chain D]=MSMEDPFFVVKGEVQKAVNTAQGLFQRWTELLQDPSTATREEIDWTTNELRNNLRSIEWDLEDLDETISIVEANPRKFNLDATELSIRKAFITSTRQVVRDMKDQMSTSSVQALAERKNRQALLGDSGSQNWSTGTTDKYGRLDRELQRANSHFIEEQQAQQQLIVEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLEDFSHELESTQSRLDNVMKKLAKVSHMTSDRRQWCAIAILFAVLLVVLILFLVL [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Rattus norvegicus ;Mus musculus ;Homo sapiens [Accession]=MF4411001 [Entry] [Entry number]=117 [Entry name]=Endosomal SNARE core complex (Vamp8 / Vti1-rp1 / Syntaxin-7 / Syntaxin-8) [PDB ID]=1gl2 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=4 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric, 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The structure shows the core domain of a SNARE complex (PMID:11786915). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=Q9WUF4 [UniProt boundaries chain A]=11-64 [UniProt coverage chain A]=54% [Name chain A]=Vesicle-associated membrane protein 8 [UniProt sequence chain A]=MEASGSAGNDRVRNLQSEVEGVKNIMTQNVERILARGENLDHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVIICVIVLIILILIILFATGTIPT [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=O70439 [UniProt boundaries chain B]=169-228 [UniProt coverage chain B]=22% [Name chain B]=Syntaxin-7 [UniProt sequence chain B]=MSYTPGIGGDSAQLAQRISSNIQKITQCSVEIQRTLNQLGTPQDSPELRQLLQQKQQYTNQLAKETDKYIKEFGSLPTTPSEQRQRKIQKDRLVAEFTTSLTNFQKAQRQAAEREKEFVARVRASSRVSGGFPEDSSKEKNLVSWESQTQPQVQVQDEEITEDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRAADYQRKSRKTLCIIIFILVVRIVIICLIVWGLKG [Source organism chain B]=Mus musculus [UniProt ID chain C]=O88384 [UniProt boundaries chain C]=139-198 [UniProt coverage chain C]=25% [Name chain C]=Vesicle transport through interaction with t-SNAREs homolog 1B [UniProt sequence chain C]=MAASAASSEHFEKLHEIFRGLLEDLQGVPERLLGTAGTEEKKKLVRDFDENQQEANETLAEMEEELRYAPLTFRNPMMSKLRNYRKDLAKLHREVRSTPLTAAPGGRGDLKYGTYTLENEHLNRLQSQRALLLQGTESLNRATQSIERSHRIATETDQIGTEIIEELGEQRDQLERTKSRLVNTNENLSKSRKILRSMSRKVITNKLLLSVIILLELAILVGLVYYKFFRHH [Source organism chain C]=Mus musculus [UniProt ID chain D]=Q9Z2Q7 [UniProt boundaries chain D]=152-206 [UniProt coverage chain D]=23% [Name chain D]=Syntaxin-8 [UniProt sequence chain D]=MAPDPWFSTYDSTCQIAQEIAEKIQERNQCERRGEKTPKLTLTIRTLLKNLKVKIDLLKDLLLRAVSTRQITQLEGDRRQNLLDDLVTRERLLLASFKNEGSEPDLIRSSLMSEEAKRGTPNPWLCEEPEETRGLGFDEIRQQQQKIIQEQDAGLDALSSIISRQKQMGQEIGNELDEQNEIIDDLANLVENTDEKLRTEARRVTLVDRKSASCGMIMVILLLLVAIVVVAVWPTN [Source organism chain D]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Rattus norvegicus ;Mus musculus [Accession]=MF4411002 [Entry] [Entry number]=118 [Entry name]=Neuronal SNARE core complex (Syntaxin-binding protein 5 / Syntaxin-1A / SNAP25) [PDB ID]=1urq [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=3 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric, 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The structure shows the core domain of a SNARE complex (PMID:15316007). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=The region(s) described in DP00068 covers 100% of the sequence present in the structure [Evidence chain D]=The region(s) described in DP00068 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=Q9WU70 [UniProt boundaries chain A]=1087-1144 [UniProt coverage chain A]=5% [Name chain A]=Syntaxin-binding protein 5 [UniProt sequence chain A]=MRKFNIRKVLDGLTAGSSSASQQQQQQQHPPGNREPEIQETLQSEHFQLCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPAVLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSGYVIMWNKAIELSSKSHPGPVVHISDNPMDEGKLLIGFESGTVVLWDLKSKKADYRYTYDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPTKPVQTITPHGKQLKDGKKPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETPYPNDFQEPYAVVVLLEKDLVLIDLAQNGYPIFENPYPLSIHESPVTCCEYFADCPVDLIPALYSVGARQKRQGYSKKEWPINGGNWGLGAQSYPEIIITGHADGSIKFWDASAITLQVLYKLKTSKVFEKSRNKDDRQNTDIVDEDPYAIQIISWCPESRMLCIAGVSAHVIIYRFSKQEVVTEVIPMLEVRLLYEINDVETPEGEQPPPLSTPVGSSTSQPIPPQSHPSTSSSSSDGLRDNVPCLKVKNSPLKQSPGYQTELVIQLVWVGGEPPQQITSLALNSSYGLVVFGNSNGIAMVDYLQKAVLLNLSTIELYGSNDPYRREPRSPRKSRQPSGAGLCDITEGTVVPEDRCKSPTSGSSSPHNSDDEQKVNNFIEKVKTQSRKFSKMVASDLAKMSRKLSLPTDLKPDLDVKDNSFSRSRSSSVTSIDKESREAISALHFCETFTRKADSSPSPCLWVGTTVGTAFVITLNLPLGPEQRLLQPVIVSPSGTILRLKGAILRMAFLDAAGCLMPPAYEPWTEHNVPEEKDEKEKLKKRRPVSVSPSSSQEISENQYAVICSEKQAKVISLPTQNCAYKQNITETSFVLRGDIVALSNSVCLACFCANGHIMTFSLPSLRPLLDVYYLPLTNMRIARTFCFANSGQALYLVSPTEIQRLTYSQETCENLQEMLGELFTPVETPEAPNRGFFKGLFGGGAQSLDREELFGESSSGKASRSLAQHIPGPGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYKDKKWYQF [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P32851 [UniProt boundaries chain B]=196-259 [UniProt coverage chain B]=22% [Name chain B]=Syntaxin-1A [UniProt sequence chain B]=MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG [Source organism chain B]=Rattus norvegicus [UniProt ID chain C]=P60881 [UniProt boundaries chain C]=16-83 [UniProt coverage chain C]=33% [Name chain C]=Synaptosomal-associated protein 25 [UniProt sequence chain C]=MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG [Source organism chain C]=Rattus norvegicus [UniProt ID chain D]=P60881 [UniProt boundaries chain D]=141-200 [UniProt coverage chain D]=29% [Name chain D]=Synaptosomal-associated protein 25 [UniProt sequence chain D]=MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG [Source organism chain D]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Rattus norvegicus [Accession]=MF4411003 [Entry] [Entry number]=119 [Entry name]=Exocytotic SNARE core complex (Synaptobrevin homolog 1 / SSO1 / Protein transport protein SEC9) [PDB ID]=3b5n [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=3 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric, 4-helix bundle) [Sequence domain]=Synaptobrevin,SNARE domain [Evidence level]=Direct evidence [Evidence text]=The structure shows the core domain of a SNARE complex (PMID:17956869). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00113 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01503 covers 95% of the sequence present in the structure [Evidence chain C]=The region(s) described in DP00128 covers 100% of the sequence present in the structure [Evidence chain D]=The region(s) described in DP00128 covers 100% of the sequence present in the structure [Similar structures]=MF4410001,MF4410002 [UniProt ID chain A]=P31109 [UniProt boundaries chain A]=27-86 [UniProt coverage chain A]=51% [Name chain A]=Synaptobrevin homolog 1 [UniProt sequence chain A]=MSSSTPFDPYALSEHDEERPQNVQSKSRTAELQAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAVSAQGFKRGANRVRKAMWYKDLKMKMCLALVIIILLVVIIVPIAVHFSR [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P32867 [UniProt boundaries chain B]=189-257 [UniProt coverage chain B]=23% [Name chain B]=Protein SSO1 [UniProt sequence chain B]=MSYNNPYQLETPFEESYELDEGSSAIGAEGHDFVGFMNKISQINRDLDKYDHTINQVDSLHKRLLTEVNEEQASHLRHSLDNFVAQATDLQFKLKNEIKSAQRDGIHDTNKQAQAENSRQRFLKLIQDYRIVDSNYKEENKEQAKRQYMIIQPEATEDEVEAAISDVGGQQIFSQALLNANRRGEAKTALAEVQARHQELLKLEKSMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQLDVEQGVGHTDKAVKSARKARKNKIRCWLIVFAIIVVVVVVVVVPAVVKTR [Source organism chain B]=Saccharomyces cerevisiae [UniProt ID chain C]=P40357 [UniProt boundaries chain C]=433-499 [UniProt coverage chain C]=10% [Name chain C]=Protein transport protein SEC9 [UniProt sequence chain C]=MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR [Source organism chain C]=Saccharomyces cerevisiae [UniProt ID chain D]=P40357 [UniProt boundaries chain D]=589-650 [UniProt coverage chain D]=9% [Name chain D]=Protein transport protein SEC9 [UniProt sequence chain D]=MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR [Source organism chain D]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Saccharomyces cerevisiae [Accession]=MF4410002 [Entry] [Entry number]=120 [Entry name]=Endosomal SNARE core complex (Syntaxin-1A / SNAP25) [PDB ID]=1jth [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric, 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The structure shows the core domain of a SNARE complex (PMID:11533035). SNARE complexes are formed by the parallel arrangement of four protein chains bound by coiled-coil interactions forming a four helix bundle (PMID:9390521). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00068 covers 100% of the sequence present in the structure [Evidence chain B]=N/A [Evidence chain C]=The region(s) described in DP00068 covers 100% of the sequence present in the structure [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=P60881 [UniProt boundaries chain A]=11-72 [UniProt coverage chain A]=30% [Name chain A]=Synaptosomal-associated protein 25 [UniProt sequence chain A]=MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P32851 [UniProt boundaries chain B]=191-257 [UniProt coverage chain B]=23% [Name chain B]=Syntaxin-1A [UniProt sequence chain B]=MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG [Source organism chain B]=Rattus norvegicus [UniProt ID chain C]=P60881 [UniProt boundaries chain C]=10-78 [UniProt coverage chain C]=33% [Name chain C]=Synaptosomal-associated protein 25 [UniProt sequence chain C]=MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG [Source organism chain C]=Rattus norvegicus [UniProt ID chain D]=P32851 [UniProt boundaries chain D]=195-245 [UniProt coverage chain D]=17% [Name chain D]=Syntaxin-1A [UniProt sequence chain D]=MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG [Source organism chain D]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Rattus norvegicus [Accession]=MF4210003 [Entry] [Entry number]=121 [Entry name]=CENP-A/histone H4 dimer (human) [PDB ID]=3nqj [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe A-2,B chains were not considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Dimer of a histone and histone-like domain [Evidence level]=Direct evidence [Evidence text]=The structure shows a dimer adopting the histone fold with Centromere protein A (CENP-A) substituting histone H3 in a classical H3/H4 dimer (PMID:20739937). While CENP-A containing dimers show slight structural differences compared to H3/H4 dimers, the overall dimer and nucleosomal structure (and based on these presumably the folding kinetics) are essentially the same (PMID:22127263). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=MF2200010,MF2210006 [UniProt ID chain A]=P49450 [UniProt boundaries chain A]=60-134 [UniProt coverage chain A]=53% [Name chain A]=Histone H3-like centromeric protein A [UniProt sequence chain A]=MGPRRRSRKPEAPRRRSPSPTPTPGPSRRGPSLGASSHQHSRRRQGWLKEIRKLQKSTHLLIRKLPFSRLAREICVKFTRGVDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTLFPKDVQLARRIRGLEEGLG [Source organism chain A]=Homo sapiens [UniProt ID chain B-2]=P62805 [UniProt boundaries chain B-2]=25-93 [UniProt coverage chain B-2]=66% [Name chain B-2]=Histone H4 [UniProt sequence chain B-2]=MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG [Source organism chain B-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Homo sapiens [Accession]=MF2200010 [Entry] [Entry number]=122 [Entry name]=CENP-A/histone H4 dimer (Kluyveromyces lactis) [PDB ID]=2yfw [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe G,H chains were not considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Dimer of a histone and histone-like domain [Evidence level]=Direct evidence [Evidence text]=The structure shows a dimer adopting the histone fold with Centromere protein A (CENP-A) substituting histone H3 in a classical H3/H4 dimer (PMID:21606327). While CENP-A containing dimers show slight structural differences compared to H3/H4 dimers, the overall dimer and nucleosomal structure (and based on these presumably the folding kinetics) are essentially the same (PMID:22127263). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2200010,MF2210006 [UniProt ID chain A]=Q6CTI2 [UniProt boundaries chain A]=105-183 [UniProt coverage chain A]=42% [Name chain A]=Histone H3-like centromeric protein CSE4 [UniProt sequence chain A]=MEQSIRSIDGSRSLSNVGASLIDRESINQRALQLLQRNRRRRLLLNRSEDKARYIQPERSASSQQIHPPEHHISAHERITKARGTRYKPTDLALAEIRKYQRSTDLLISRMPFARLVKEVTDQFTTESEPLRWQSMAIMALQEASEAYLVGLLEHTNLLALHAKRITIMRKDMQLARRIRGQFI [Source organism chain A]=NRRL Y-1140 / WM37) [UniProt ID chain B]=Q6CMU6 [UniProt boundaries chain B]=30-95 [UniProt coverage chain B]=64% [Name chain B]=Histone H4 [UniProt sequence chain B]=MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRNVLKTFLESVIRDAVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG [Source organism chain B]=NRRL Y-1140 / WM37) [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=NRRL Y-1140 / WM37) [Accession]=MF2210006 [Entry] [Entry number]=123 [Entry name]=CENP-S/CENP-X dimer (human) [PDB ID]=4ne3 [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe A-2,B chains were not considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=CENP-S protein [Evidence level]=Direct evidence [Evidence text]=Centromere proteins S and X (CENP-S and CENP-X), also called MHF1 and MHF2 form histone-like heterodimers (PMID:20347428). These dimers further associate with heterodimers formed by CENP-T and CENP-W and these tetrameric structures share a high degree of similarity with canonical histone multimers within the nucleosome (PMID:22304917). CENP-T-W-S-X tetramers - similarly to nucleosomes formed by histones - are able to bind and supercoil DNA (PMID:24234442). Apart from some structural differences leading to different functions (e.g. CENP-T-W-S-X tetramers show a preference for branched DNA as opposed to nucleosomes, PMID:24390579), both the overall and the underlying basic structures of nucleosomes and CENP-T-W-S-X tetramers are essentially the same with both CENP-S/CENP-X and CENP-T/W dimers forming structures nearly identical to that of histone dimers (PMID:20347428 and PMID:19070575). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=MF2210007,MF2200011 [UniProt ID chain A]=Q8N2Z9 [UniProt boundaries chain A]=14-105 [UniProt coverage chain A]=66% [Name chain A]=Centromere protein S [UniProt sequence chain A]=MEEEAETEEQQRFSYQQRLKAAVHYTVGCLCEEVALDKEMQFSKQTIAAISELTFRQCENFAKDLEMFARHAKRTTINTEDVKLLARRSNSLLKYITDKSEEIAQINLERKAQKKKKSEDGSKNSRQPAEAGVVESEN [Source organism chain A]=Homo sapiens [UniProt ID chain B-2]=A8MT69 [UniProt boundaries chain B-2]=8-81 [UniProt coverage chain B-2]=91% [Name chain B-2]=Centromere protein X [UniProt sequence chain B-2]=MEGAGAGSGFRKELVSRLLHLHFKDDKTKVSGDALQLMVELLKVFVVEAAVRGVRQAQAEDALRVDVDQLEKVLPQLLLDF [Source organism chain B-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF2200011 [Entry] [Entry number]=124 [Entry name]=CENP-S/CENP-X dimer (Gallus gallus) [PDB ID]=3b0b [Chains]=A,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe C,B chains were not considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=CENP-S protein [Evidence level]=Direct evidence [Evidence text]=Centromere proteins S and X (CENP-S and CENP-X), also called MHF1 and MHF2 form histone-like heterodimers (PMID:20347428). These dimers further associate with heterodimers formed by CENP-T and CENP-W and these tetrameric structures share a high degree of similarity with canonical histone multimers within the nucleosome (PMID:22304917). CENP-T-W-S-X tetramers - similarly to nucleosomes formed by histones - are able to bind and supercoil DNA (PMID:24234442). Apart from some structural differences leading to different functions (e.g. CENP-T-W-S-X tetramers show a preference for branched DNA as opposed to nucleosomes, PMID:24390579), both the overall and the underlying basic structures of nucleosomes and CENP-T-W-S-X tetramers are essentially the same with both CENP-S/CENP-X and CENP-T/W dimers forming structures nearly identical to that of histone dimers (PMID:20347428 and PMID:19070575). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210007,MF2200011 [UniProt ID chain A]=E1BSW7 [UniProt boundaries chain A]=5-102 [UniProt coverage chain A]=70% [Name chain A]=Centromere protein S [UniProt sequence chain A]=MEAAGGEQRELLIQRLRAAVHYTTGCLCQDVAEDKGVLFSKQTVAAISEITFRQCENFARDLEMFARHAKRSTITSEDVKLLARRSNSLLKYITQKSDELASSNMEQKEKKKKKSSAAKGRKTEENETPVTESEDSNMA [Source organism chain A]=Gallus gallus [UniProt ID chain D]=P0DJH7 [UniProt boundaries chain D]=6-80 [UniProt coverage chain D]=93% [Name chain D]=Centromere protein X [UniProt sequence chain D]=MEEREGGFRKETVERLLRLHFRDGRTRVNGDALLLMAELLKVFVREAAARAARQAQAEDLEKVDIEHVEKVLPQLLLDFV [Source organism chain D]=Gallus gallus [ExpTech]=X-ray [Resolution]=2.15 [Source organism]=Gallus gallus [Accession]=MF2210007 [Entry] [Entry number]=125 [Entry name]=MHF complex (Saccharomyces cerevisiae) [PDB ID]=3v9r [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe D,C chains were not considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Centromere proteins S and X (CENP-S and CENP-X), also called MHF1 and MHF2 form histone-like heterodimers (MHF complex, PMID:20347428). These dimers further associate with heterodimers formed by CENP-T and CENP-W and these tetrameric structures share a high degree of similarity with canonical histone multimers within the nucleosome (PMID:22304917). CENP-T-W-S-X tetramers - similarly to nucleosomes formed by histones - are able to bind and supercoil DNA (PMID:24234442). Apart from some structural differences leading to different functions (e.g. CENP-T-W-S-X tetramers show a preference for branched DNA as opposed to nucleosomes, PMID:24390579), both the overall and the underlying basic structures of nucleosomes and CENP-T-W-S-X tetramers are essentially the same with both CENP-S/CENP-X and CENP-T/W dimers forming structures nearly identical to that of histone dimers (PMID:20347428 and PMID:19070575). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q3E835 [UniProt boundaries chain A]=2-89 [UniProt coverage chain A]=97% [Name chain A]=Inner kinetochore subunit MHF1 [UniProt sequence chain A]=MNDDEDRAQLKARLWIRVEERLQQVLSSEDIKYTPRFINSLLELAYLQLGEMGSDLQAFARHAGRGVVNKSDLMLYLRKQPDLQERVTQE [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=Q3E829 [UniProt boundaries chain B]=1-80 [UniProt coverage chain B]=100% [Name chain B]=Inner kinetochore subunit MHF2 [UniProt sequence chain B]=MLSKEALIKILSQNEGGNDMKIADEVVPMIQKYLDIFIDEAVLRSLQSHKDINGERGDKSPLELSHQDLERIVGLLLMDM [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Saccharomyces cerevisiae [Accession]=MF2210008 [Entry] [Entry number]=126 [Entry name]=CENP-T/CENP-W dimer (Gallus gallus) [PDB ID]=3b0c [Chains]=T,W [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Centromere proteins T and W (CENP-T and CENP-W) form histone-like heterodimers (PMID:19070575). These dimers further associate with heterodimers formed by CENP-S and CENP-X and these tetrameric structures share a high degree of similarity with canonical histone multimers within the nucleosome (PMID:22304917). CENP-T-W-S-X tetramers - similarly to nucleosomes formed by histones - are able to bind and supercoil DNA (PMID:24234442). Apart from some structural differences leading to different functions (e.g. CENP-T-W-S-X tetramers show a preference for branched DNA as opposed to nucleosomes, PMID:24390579), both the overall and the underlying basic structures of nucleosomes and CENP-T-W-S-X tetramers are essentially the same with both CENP-S/CENP-X and CENP-T/W dimers forming structures nearly identical to that of histone dimers (PMID:20347428 and PMID:19070575). Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain T]=N/A [Evidence chain W]=N/A [Similar structures]=None [UniProt ID chain T]=F1NPG5 [UniProt boundaries chain T]=538-628 [UniProt coverage chain T]=14% [Name chain T]=Centromere protein T [UniProt sequence chain T]=MDGRVGLRASRRAAPTPRVAVRSSPRHRARVREQEPVVSAMSGSGLGKENKAGSSTPLRHRPNAFSELDNATPRVMLRKIIQNQPQVSPLALQTVQLEETEDARPEPPSQRTSSTVELQLPDLVPEDASVTTFRMTRKRKKLSISEFERAADKRLPQNQAHSTLDSTLVRSLRMSVGSVMAPDTVEKRGLLRRPQNHKAIDIAAFEGGVEQNMLQIKAQDYLVDLQTSSMTGTTTIRTDAEVVLNNTELFVEPQLGEQNLLAVEPQLSDSKTSAQRSNTSYPAHEKARLEGLVSRVSTDERRTLRFSEKDLITDHEHVDGITQKTPAKQGEEEQDHSQQNDPMEQFSESEEMAGTTEHHADAEYSEHSEKKLSRKAVSQLTAAQDAGVEMEMTPSEGGVAEGTEHQDSPKAELQMAGSPGGHSPASYSLEKPGAKPLKEAVEQTGEIERGTITGVLDAAEEEATDDESDKEDHESEEISMKTPMFVHAAAYRPQPVLSPPHPVKSASPELPPQPVRAKPVPKSSGAAQRKTREPEIASSLIKQIFSHYVKTPVTRDAYKIVEKCSERYFKQISSDLEAYSQHAGRKTVEMADVELLMRRQGLVTDKMPLHVLVERHLPLEYRKLLIPIAVSGNKVIPCK [Source organism chain T]=Gallus gallus [UniProt ID chain W]=P0DJH6 [UniProt boundaries chain W]=4-76 [UniProt coverage chain W]=96% [Name chain W]=Centromere protein W [UniProt sequence chain W]=MRRTVPRGTLRKIIKKHKPHLRLAANTDLLVHLSFLLFLHRLAEEARTNAFENKSKIIKPEHTIAAAKVILKKSRG [Source organism chain W]=Gallus gallus [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Gallus gallus [Accession]=MF2210009 [Entry] [Entry number]=127 [Entry name]=Oligomerization domain of Drosophila melanogaster p53 [PDB ID]=2rp4 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=p53 tetramerization [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=While the C-terminal region of p53 from humans and D. melanogaster do not share a high degree of sequential identity, they are structurally and functionally similar (PMID:10778859). The oligomerization domain (OD) of D. melanogaster p53 (Dmp53) includes the structural elements of that of human p53 exhibiting a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). Human p53 tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028). The main difference between the two p53 variants are the additional structural elements in Dmp53 OD which comprise an additional helix and a beta-strand. The deletion of these structural elements destabilize the oligomer hinting at a suboptimal binding of the core structural elements compared to the human counterpart (PMID:17581633). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=Q8IH92 [UniProt boundaries chain A]=449-519 [UniProt coverage chain A]=13% [Name chain A]=AT28346p [UniProt sequence chain A]=WSTEDSCGHKSQLLNKIYLFECTAMSLHKSASFSLTFNQNTSIVSRSNSRTIFEAFKEFLDFWDIGNEVSAESAVRVSSNGAFNLPQSFGNESNEYAHLATPVDPAYGGNNTNNMMQFTNNLEILANNNSDGNNKINACNKFVCHKGTDSEDDSTEVDIKEDIPKTVEVSGSELTTEPMAFLQGLNSGNLMQFSQQSVLREMMLQDIQIQANTLPKLENHNIGGYCFSMVLDEPPKSLWMYSIPLNKLYIRMNKAFNVDVQFKSKMPIQPLNLRVFLCFSNDVSAPVVRCQNHLSVEPLTANNAKMRESLLRSENPNSVYCGNAQGKGISERFSVVVPLNMSRSVTRSGLTRQTLAFKFVCQNSCIGRKETSLVFCLEKACGDIVGQHVIHVKICTCPKRDRIQDERQLNSKKRKSVPEAAEEDEPSKVRRCIAIKTEDTESNDSRDCDDSAAEWNVSRTPDGDYRLAITCPNKEWLLQSIEGMIKEAAAEVLRNPNQENLRRHANKLLSLKKRAYELP [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=Q8IH92 [UniProt boundaries chain B]=449-519 [UniProt coverage chain B]=13% [Name chain B]=AT28346p [UniProt sequence chain B]=WSTEDSCGHKSQLLNKIYLFECTAMSLHKSASFSLTFNQNTSIVSRSNSRTIFEAFKEFLDFWDIGNEVSAESAVRVSSNGAFNLPQSFGNESNEYAHLATPVDPAYGGNNTNNMMQFTNNLEILANNNSDGNNKINACNKFVCHKGTDSEDDSTEVDIKEDIPKTVEVSGSELTTEPMAFLQGLNSGNLMQFSQQSVLREMMLQDIQIQANTLPKLENHNIGGYCFSMVLDEPPKSLWMYSIPLNKLYIRMNKAFNVDVQFKSKMPIQPLNLRVFLCFSNDVSAPVVRCQNHLSVEPLTANNAKMRESLLRSENPNSVYCGNAQGKGISERFSVVVPLNMSRSVTRSGLTRQTLAFKFVCQNSCIGRKETSLVFCLEKACGDIVGQHVIHVKICTCPKRDRIQDERQLNSKKRKSVPEAAEEDEPSKVRRCIAIKTEDTESNDSRDCDDSAAEWNVSRTPDGDYRLAITCPNKEWLLQSIEGMIKEAAAEVLRNPNQENLRRHANKLLSLKKRAYELP [Source organism chain B]=Drosophila melanogaster [UniProt ID chain C]=Q8IH92 [UniProt boundaries chain C]=449-519 [UniProt coverage chain C]=13% [Name chain C]=AT28346p [UniProt sequence chain C]=WSTEDSCGHKSQLLNKIYLFECTAMSLHKSASFSLTFNQNTSIVSRSNSRTIFEAFKEFLDFWDIGNEVSAESAVRVSSNGAFNLPQSFGNESNEYAHLATPVDPAYGGNNTNNMMQFTNNLEILANNNSDGNNKINACNKFVCHKGTDSEDDSTEVDIKEDIPKTVEVSGSELTTEPMAFLQGLNSGNLMQFSQQSVLREMMLQDIQIQANTLPKLENHNIGGYCFSMVLDEPPKSLWMYSIPLNKLYIRMNKAFNVDVQFKSKMPIQPLNLRVFLCFSNDVSAPVVRCQNHLSVEPLTANNAKMRESLLRSENPNSVYCGNAQGKGISERFSVVVPLNMSRSVTRSGLTRQTLAFKFVCQNSCIGRKETSLVFCLEKACGDIVGQHVIHVKICTCPKRDRIQDERQLNSKKRKSVPEAAEEDEPSKVRRCIAIKTEDTESNDSRDCDDSAAEWNVSRTPDGDYRLAITCPNKEWLLQSIEGMIKEAAAEVLRNPNQENLRRHANKLLSLKKRAYELP [Source organism chain C]=Drosophila melanogaster [UniProt ID chain D]=Q8IH92 [UniProt boundaries chain D]=449-519 [UniProt coverage chain D]=13% [Name chain D]=AT28346p [UniProt sequence chain D]=WSTEDSCGHKSQLLNKIYLFECTAMSLHKSASFSLTFNQNTSIVSRSNSRTIFEAFKEFLDFWDIGNEVSAESAVRVSSNGAFNLPQSFGNESNEYAHLATPVDPAYGGNNTNNMMQFTNNLEILANNNSDGNNKINACNKFVCHKGTDSEDDSTEVDIKEDIPKTVEVSGSELTTEPMAFLQGLNSGNLMQFSQQSVLREMMLQDIQIQANTLPKLENHNIGGYCFSMVLDEPPKSLWMYSIPLNKLYIRMNKAFNVDVQFKSKMPIQPLNLRVFLCFSNDVSAPVVRCQNHLSVEPLTANNAKMRESLLRSENPNSVYCGNAQGKGISERFSVVVPLNMSRSVTRSGLTRQTLAFKFVCQNSCIGRKETSLVFCLEKACGDIVGQHVIHVKICTCPKRDRIQDERQLNSKKRKSVPEAAEEDEPSKVRRCIAIKTEDTESNDSRDCDDSAAEWNVSRTPDGDYRLAITCPNKEWLLQSIEGMIKEAAAEVLRNPNQENLRRHANKLLSLKKRAYELP [Source organism chain D]=Drosophila melanogaster [ExpTech]=NMR [Resolution]=N/A [Source organism]=Drosophila melanogaster [Accession]=MF4110008 [Entry] [Entry number]=128 [Entry name]=Bulb-type mannose-binding lectin (Allium sativum) [PDB ID]=1kj1 [Chains]=A,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bulb-type lectin domain [Subclass]=Heterodimeric lectin [Sequence domain]=Bulb-type lectin domain [Evidence level]=Direct evidence [Evidence text]=The association between the two subunits of mannose-binding lectin from garlic bulbs was shown to be highly reversible and can be defined as a two-state process in which the folded dimer is converted directly into the unfolded monomers (PMID:11401577). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain D]=N/A [Similar structures]=MF2110027,MF2210010,MF2210012,MF2110015 [UniProt ID chain A]=Q38789 [UniProt boundaries chain A]=177-285 [UniProt coverage chain A]=35% [Name chain A]=I lectin [UniProt sequence chain A]=TTSSPKLMSIATVAAILTILASTCMARNLLTNGEGLYAGQSLNVEPYHFIMQEDCNLVLYDHSTAVWATNTDIPGKKECRAVLQSDGNFVVYDADGRPLWASHSVRGNGNYVLVLQEDGNVVIYGSDIWSTGTYVKAARGPVVVAMNGTVDGGSLIRPVIVNKNHVPVIRKVGTLSRNILRNDEGLYAGQSLDVEPYHFIMQEDCNLVLYDHSTAVWASNTDIPGKKGCKAVLQSDGNFVVYDAEGRSLWASHSVRGNGNYVLVLQEDGNVVIYGSDIWSTDTYRKSARGPVIRKVGTLAGAA [Source organism chain A]=Allium sativum [UniProt ID chain D]=Q38783 [UniProt boundaries chain D]=29-137 [UniProt coverage chain D]=70% [Name chain D]=II lectin [UniProt sequence chain D]=RMTTPSPKVMSIATVAAILTIWASTCMARNILMNDEGLYAGQSLDVEPYHLIMQEDCNLVLYDHSTAVWTSNTDIPGKKGCKAVLQSDGNFVVYDAEGRSLWASHSVRGNGNYVLVLQEDGNVVIYGSDIWSTNTYKGSARGPVIRKVGTLAGAA [Source organism chain D]=Allium sativum [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Allium sativum [Accession]=MF2210010 [Entry] [Entry number]=131 [Entry name]=Mannose-binding lectin (Polygonatum cyrtonema) [PDB ID]=3a0e [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bulb-type lectin domain [Subclass]=Homodimeric lectin [Sequence domain]=Bulb-type lectin domain [Evidence level]=Direct evidence [Evidence text]=A closely homologous lectin of the same type sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF2110027,MF2210010,MF2210012,MF2110015 [UniProt ID chain A]=Q8L568 [UniProt boundaries chain A]=29-138 [UniProt coverage chain A]=68% [Name chain A]=Mannose/sialic acid-binding lectin [UniProt sequence chain A]=MAASSSPILLLMATIAIFGLMVASPCAAVNSLSSPNSLFTGHSLEVGPSYRLIMPGDCNFVLYDSGKPVWASNTGGLGSGCRLTLHNNGNLVIYDQSNRVIWQTKTNGKEDHYVLVLQQDRNVVIYGPVVWATGSGPAVGLTLIPHNATDIVHATPMLNE [Source organism chain A]=Polygonatum cyrtonema [UniProt ID chain A-2]=Q8L568 [UniProt boundaries chain A-2]=29-138 [UniProt coverage chain A-2]=68% [Name chain A-2]=Mannose/sialic acid-binding lectin [UniProt sequence chain A-2]=MAASSSPILLLMATIAIFGLMVASPCAAVNSLSSPNSLFTGHSLEVGPSYRLIMPGDCNFVLYDSGKPVWASNTGGLGSGCRLTLHNNGNLVIYDQSNRVIWQTKTNGKEDHYVLVLQQDRNVVIYGPVVWATGSGPAVGLTLIPHNATDIVHATPMLNE [Source organism chain A-2]=Polygonatum cyrtonema [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Polygonatum cyrtonema [Accession]=MF2110015 [Entry] [Entry number]=133 [Entry name]=Neoculin heterodimer (Molineria latifolia) [PDB ID]=2d04 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bulb-type lectin domain [Subclass]=Heterodimeric lectin [Sequence domain]=Bulb-type lectin domain [Evidence level]=Direct evidence [Evidence text]=A closely homologous protein (bulb-type lectin) sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110027,MF2210010,MF2210012,MF2110015 [UniProt ID chain A]=Q6F495 [UniProt boundaries chain A]=23-133 [UniProt coverage chain A]=70% [Name chain A]=Curculin-2 [UniProt sequence chain A]=MAAKFLLTILVTFAAVASLGMADSVLLSGQTLYAGHSLTSGSYTLTIQNNCNLVKYQHGRQIWASDTDGQGSQCRLTLRSDGNLIIYDDNNMVVWGSDCWGNNGTYALVLQQDGLFVIYGPVLWPLGLNGCRSLNGEITVAKDSTEPQHEDIKMVINN [Source organism chain A]=Molineria latifolia [UniProt ID chain B]=P19667 [UniProt boundaries chain B]=23-133 [UniProt coverage chain B]=70% [Name chain B]=Curculin-1 [UniProt sequence chain B]=MAAKFLLTILVTFAAVASLGMADNVLLSGQTLHADHSLQAGAYTLTIQNKCNLVKYQNGRQIWASNTDRRGSGCRLTLLSDGNLVIYDHNNNDVWGSACWGDNGKYALVLQKDGRFVIYGPVLWSLGPNGCRRVNGGITVAKDSTEPQHEDIKMVINN [Source organism chain B]=Molineria latifolia [ExpTech]=X-ray [Resolution]=2.76 [Source organism]=Molineria latifolia [Accession]=MF2210012 [Entry] [Entry number]=135 [Entry name]=Basic HLH/leucine zipper domain of Max [PDB ID]=1r05 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Basic helix-loop-helix (bHLH) [Sequence domain]=Helix-loop-helix DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294, PMID:9488706). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100009,MF2110021,MF2110023,MF2100010,MF7000192,MF7000402,MF7000403,MF7000444,MF7000371 [UniProt ID chain A]=P61244 [UniProt boundaries chain A]=22-103 [UniProt coverage chain A]=51% [Name chain A]=Protein max [UniProt sequence chain A]=MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P61244 [UniProt boundaries chain B]=22-103 [UniProt coverage chain B]=51% [Name chain B]=Protein max [UniProt sequence chain B]=MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2100009 [Entry] [Entry number]=136 [Entry name]=Transcription factor HES-1 dimer [PDB ID]=2mh3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Basic helix-loop-helix (bHLH) [Sequence domain]=Helix-loop-helix DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294, PMID:9488706). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100009,MF2110021,MF2110023,MF2100010,MF7000192,MF7000402,MF7000403,MF7000444,MF7000371 [UniProt ID chain A]=Q14469 [UniProt boundaries chain A]=27-95 [UniProt coverage chain A]=24% [Name chain A]=Transcription factor HES-1 [UniProt sequence chain A]=MPADIMEKNSSSPVAATPASVNTTPDKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQMTAALSTDPSVLGKYRAGFSECMNEVTRFLSTCEGVNTEVRTRLLGHLANCMTQINAMTYPGQPHPALQAPPPPPPGPGGPQHAPFAPPPPLVPIPGGAAPPPGGAPCKLGSQAGEAAKVFGGFQVVPAPDGQFAFLIPNGAFAHSGPVIPVYTSNSGTSVGPNAVSPSSGPSLTADSMWRPWRN [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q14469 [UniProt boundaries chain B]=27-95 [UniProt coverage chain B]=24% [Name chain B]=Transcription factor HES-1 [UniProt sequence chain B]=MPADIMEKNSSSPVAATPASVNTTPDKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQMTAALSTDPSVLGKYRAGFSECMNEVTRFLSTCEGVNTEVRTRLLGHLANCMTQINAMTYPGQPHPALQAPPPPPPGPGGPQHAPFAPPPPLVPIPGGAAPPPGGAPCKLGSQAGEAAKVFGGFQVVPAPDGQFAFLIPNGAFAHSGPVIPVYTSNSGTSVGPNAVSPSSGPSLTADSMWRPWRN [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2100010 [Entry] [Entry number]=138 [Entry name]=CesAB chaperone homodimer [PDB ID]=2lhk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=E. coli CesAB was shown to form a loosely packed four-helix bundle stabilized by coiled-coil interactions that are partially disrupted by packing irregularities. Thus native CesAB adopts a molted globule-like structure even in its dimeric state (PMID:22152477). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O52124 [UniProt boundaries chain A]=1-107 [UniProt coverage chain A]=100% [Name chain A]=L0052 [UniProt sequence chain A]=MSIVSQTRNKELLDKKIRSEIEAIKKIIAEFDVVKESVNELSEKAKTDPQAAEKLNKLIEGYTYGEERKLYDSALSKIEKLIETLSPARSKSQSTMNQRNRNNRKIV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=O52124 [UniProt boundaries chain B]=1-107 [UniProt coverage chain B]=100% [Name chain B]=L0052 [UniProt sequence chain B]=MSIVSQTRNKELLDKKIRSEIEAIKKIIAEFDVVKESVNELSEKAKTDPQAAEKLNKLIEGYTYGEERKLYDSALSKIEKLIETLSPARSKSQSTMNQRNRNNRKIV [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF2120021 [Entry] [Entry number]=139 [Entry name]=Quorum-sensing antiactivator TraM [PDB ID]=1rfy [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Other [Sequence domain]=Prokaryotic Transcriptional repressor TraM [Evidence level]=Direct evidence [Evidence text]=TraM dimers were shown to fold/refold in a single step via a two-state mechanism using thermal unfolding experiments monitored by CD (PMID:16997969). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF2120022,MF2120023 [UniProt ID chain A]=Q57471 [UniProt boundaries chain A]=10-98 [UniProt coverage chain A]=87% [Name chain A]=Transcriptional repressor TraM [UniProt sequence chain A]=MELEDANVTKKVELRPLIGLTRGLPPTDLETITIDAIRTHRRLVEKADELFQALPETYKTGQACGGPQHIRYIEASIEMHAQMSALNTLYSILGFIPKVVVN [Source organism chain A]=radiobacter) [UniProt ID chain A-2]=Q57471 [UniProt boundaries chain A-2]=12-99 [UniProt coverage chain A-2]=86% [Name chain A-2]=Transcriptional repressor TraM [UniProt sequence chain A-2]=MELEDANVTKKVELRPLIGLTRGLPPTDLETITIDAIRTHRRLVEKADELFQALPETYKTGQACGGPQHIRYIEASIEMHAQMSALNTLYSILGFIPKVVVN [Source organism chain A-2]=radiobacter) [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=radiobacter) [Accession]=MF2120022 [Entry] [Entry number]=140 [Entry name]=Quorum-sensing antiactivator TraM2 [PDB ID]=2hjd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Other [Sequence domain]=Prokaryotic Transcriptional repressor TraM [Evidence level]=Direct evidence [Evidence text]=TraM dimers were shown to fold/refold in a single step via a two-state mechanism using thermal unfolding experiments monitored by CD (PMID:16997969). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2120022,MF2120023 [UniProt ID chain A]=Q20HX4 [UniProt boundaries chain A]=12-100 [UniProt coverage chain A]=87% [Name chain A]=Quorum-sensing antiactivator [UniProt sequence chain A]=MDLKDSVVSDTFELRPVIGLTRGLSSADIETLTANAIRLHRQLLEKADQLFQVLPDDIKIGTAAGGEQHLEYIEAMIEMHAQMSAVNTLVGLLGFIPKVSVN [Source organism chain A]=radiobacter) [UniProt ID chain B]=Q20HX4 [UniProt boundaries chain B]=12-100 [UniProt coverage chain B]=87% [Name chain B]=Quorum-sensing antiactivator [UniProt sequence chain B]=MDLKDSVVSDTFELRPVIGLTRGLSSADIETLTANAIRLHRQLLEKADQLFQVLPDDIKIGTAAGGEQHLEYIEAMIEMHAQMSAVNTLVGLLGFIPKVSVN [Source organism chain B]=radiobacter) [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=radiobacter) [Accession]=MF2120023 [Entry] [Entry number]=141 [Entry name]=The synaptic acetylcholinesterase tetramer assembled around a polyproline-II helix [PDB ID]=1vzj [Chains]=A,B,C,D,I [Total number of chains]=5 [Assembly]=Pentamer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:15526038). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Evidence chain I]=N/A [Similar structures]=None [UniProt ID chain A]=P22303 [UniProt boundaries chain A]=577-602 [UniProt coverage chain A]=4% [Name chain A]=Acetylcholinesterase [UniProt sequence chain A]=MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P22303 [UniProt boundaries chain B]=575-605 [UniProt coverage chain B]=5% [Name chain B]=Acetylcholinesterase [UniProt sequence chain B]=MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL [Source organism chain B]=Homo sapiens [UniProt ID chain C]=P22303 [UniProt boundaries chain C]=575-606 [UniProt coverage chain C]=5% [Name chain C]=Acetylcholinesterase [UniProt sequence chain C]=MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL [Source organism chain C]=Homo sapiens [UniProt ID chain D]=P22303 [UniProt boundaries chain D]=575-606 [UniProt coverage chain D]=5% [Name chain D]=Acetylcholinesterase [UniProt sequence chain D]=MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL [Source organism chain D]=Homo sapiens [UniProt ID chain I]=Q9Y215 [UniProt boundaries chain I]=53-67 [UniProt coverage chain I]=3% [Name chain I]=Acetylcholinesterase collagenic tail peptide [UniProt sequence chain I]=MVVLNPMTLGIYLQLFFLSIVSQPTFINSVLPISAALPSLDQKKRGGHKACCLLTPPPPPLFPPPFFRGGRSPLLSPDMKNLMLELETSQSPCMQGSLGSPGPPGPQGPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVPGMPGPIGWPGPEGPRGEKGDLGMMGLPGSRGPMGSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVMGPPGKPGPSGQPGRPGPPGPPPAGQLIMGPKGERGFPGPPGRCLCGPTMNVNNPSYGESVYGPSSPRVPVIFVVNNQEELERLNTQNAIAFRRDQRSLYFKDSLGWLPIQLTPFYPVDYTADQHGTCGDGLLQPGEECDDGNSDVGDDCIRCHRAYCGDGHRHEGVEDCDGSDFGYLTCETYLPGSYGDLQCTQYCYIDSTPCRYFT [Source organism chain I]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Homo sapiens [Accession]=MF5200001 [Entry] [Entry number]=142 [Entry name]=Antitoxin phd dimer (Escherichia virus P1) [PDB ID]=3hs2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=According to the most probable oligomerization state stored in PDBe G chains were not considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin Phd/YefM [Sequence domain]=Antitoxin Phd_YefM [Evidence level]=Direct evidence [Evidence text]=The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into monomer species (PMID:20603017). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00288 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP00288 covers 100% of the sequence present in the structure [Similar structures]=MF2120015,MF2140010,MF2120024 [UniProt ID chain A]=Q06253 [UniProt boundaries chain A]=1-56 [UniProt coverage chain A]=76% [Name chain A]=Antitoxin phd [UniProt sequence chain A]=MQSINFRTARGNLSEVLNNVEAGEEVEITRRGREPAVIVSKATFEAYKKAALDAEFASLFDTLDSTNKELVNR [Source organism chain A]=Escherichia phage P1 [UniProt ID chain B]=Q06253 [UniProt boundaries chain B]=1-56 [UniProt coverage chain B]=76% [Name chain B]=Antitoxin phd [UniProt sequence chain B]=MQSINFRTARGNLSEVLNNVEAGEEVEITRRGREPAVIVSKATFEAYKKAALDAEFASLFDTLDSTNKELVNR [Source organism chain B]=Escherichia phage P1 [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Escherichia phage P1 [Accession]=MF2140010 [Entry] [Entry number]=143 [Entry name]=Antitoxin phd dimer (Mycobacterium tuberculosis) [PDB ID]=3g5o [Chains]=A,D [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=According to the most probable oligomerization state stored in PDBe C,B chains were not considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin Phd/YefM [Sequence domain]=Antitoxin Phd_YefM [Evidence level]=Direct evidence [Evidence text]=The dimerization of the prevents host death (phd) antitoxin from Escherichia virus P1 has been shown with differential scanning calorimetry to fit well to a two-state model consisting of a dimer unfolding into monomer species (PMID:20603017). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain D]=N/A [Similar structures]=MF2120015,MF2140010,MF2120024 [UniProt ID chain A]=O33347 [UniProt boundaries chain A]=1-91 [UniProt coverage chain A]=97% [Name chain A]=Antitoxin RelF [UniProt sequence chain A]=MRILPISTIKGKLNEFVDAVSSTQDQITITKNGAPAAVLVGADEWESLQETLYWLAQPGIRESIAEADADIASGRTYGEDEIRAEFGVPRRPH [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain D]=O33347 [UniProt boundaries chain D]=1-91 [UniProt coverage chain D]=97% [Name chain D]=Antitoxin RelF [UniProt sequence chain D]=MRILPISTIKGKLNEFVDAVSSTQDQITITKNGAPAAVLVGADEWESLQETLYWLAQPGIRESIAEADADIASGRTYGEDEIRAEFGVPRRPH [Source organism chain D]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Mycobacterium tuberculosis [Accession]=MF2120024 [Entry] [Entry number]=144 [Entry name]=Docking domain A of the erythronolide synthase [PDB ID]=1pzq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:12954331). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q03132 [UniProt boundaries chain A]=3490-3547 [UniProt coverage chain A]=1% [Name chain A]=6-deoxyerythronolide-B synthase EryA2, modules 3 and 4 [UniProt sequence chain A]=MTDSEKVAEYLRRATLDLRAARQRIRELESDPIAIVSMACRLPGGVNTPQRLWELLREGGETLSGFPTDRGWDLARLHHPDPDNPGTSYVDKGGFLDDAAGFDAEFFGVSPREAAAMDPQQRLLLETSWELVENAGIDPHSLRGTATGVFLGVAKFGYGEDTAAAEDVEGYSVTGVAPAVASGRISYTMGLEGPSISVDTACSSSLVALHLAVESLRKGESSMAVVGGAAVMATPGVFVDFSRQRALAADGRSKAFGAGADGFGFSEGVTLVLLERLSEARRNGHEVLAVVRGSALNQDGASNGLSAPSGPAQRRVIRQALESCGLEPGDVDAVEAHGTGTALGDPIEANALLDTYGRDRDADRPLWLGSVKSNIGHTQAAAGVTGLLKVVLALRNGELPATLHVEEPTPHVDWSSGGVALLAGNQPWRRGERTRRARVSAFGISGTNAHVIVEEAPEREHRETTAHDGRPVPLVVSARTTAALRAQAAQIAELLERPDADLAGVGLGLATTRARHEHRAAVVASTREEAVRGLREIAAGAATADAVVEGVTEVDGRNVVFLFPGQGSQWAGMGAELLSSSPVFAGKIRACDESMAPMQDWKVSDVLRQAPGAPGLDRVDVVQPVLFAVMVSLAELWRSYGVEPAAVVGHSQGEIAAAHVAGALTLEDAAKLVVGRSRLMRSLSGEGGMAAVALGEAAVRERLRPWQDRLSVAAVNGPRSVVVSGEPGALRAFSEDCAAEGIRVRDIDVDYASHSPQIERVREELLETTGDIAPRPARVTFHSTVESRSMDGTELDARYWYRNLRETVRFADAVTRLAESGYDAFIEVSPHPVVVQAVEEAVEEADGAEDAVVVGSLHRDGGDLSAFLRSMATAHVSGVDIRWDVALPGAAPFALPTYPFQRKRYWLQPAAPAAASDELAYRVSWTPIEKPESGNLDGDWLVVTPLISPEWTEMLCEAINANGGRALRCEVDTSASRTEMAQAVAQAGTGFRGVLSLLSSDESACRPGVPAGAVGLLTLVQALGDAGVDAPVWCLTQGAVRTPADDDLARPAQTTAHGFAQVAGLELPGRWGGVVDLPESVDDAALRLLVAVLRGGGRAEDHLAVRDGRLHGRRVVRASLPQSGSRSWTPHGTVLVTGAASPVGDQLVRWLADRGAERLVLAGACPGDDLLAAVEEAGASAVVCAQDAAALREALGDEPVTALVHAGTLTNFGSISEVAPEEFAETIAAKTALLAVLDEVLGDRAVEREVYCSSVAGIWGGAGMAAYAAGSAYLDALAEHHRARGRSCTSVAWTPWALPGGAVDDGYLRERGLRSLSADRAMRTWERVLAAGPVSVAVADVDWPVLSEGFAATRPTALFAELAGRGGQAEAEPDSGPTGEPAQRLAGLSPDEQQENLLELVANAVAEVLGHESAAEINVRRAFSELGLDSLNAMALRKRLSASTGLRLPASLVFDHPTVTALAQHLRARLVGDADQAAVRVVGAADESEPIAIVGIGCRFPGGIGSPEQLWRVLAEGANLTTGFPADRGWDIGRLYHPDPDNPGTSYVDKGGFLTDAADFDPGFFGITPREALAMDPQQRLMLETAWEAVERAGIDPDALRGTDTGVFVGMNGQSYMQLLAGEAERVDGYQGLGNSASVLSGRIAYTFGWEGPALTVDTACSSSLVGIHLAMQALRRGECSLALAGGVTVMSDPYTFVDFSTQRGLASDGRCKAFSARADGFALSEGVAALVLEPLSRARANGHQVLAVLRGSAVNQDGASNGLAAPNGPSQERVIRQALAASGVPAADVDVVEAHGTGTELGDPIEAGALIATYGQDRDRPLRLGSVKTNIGHTQAAAGAAGVIKVVLAMRHGMLPRSLHADELSPHIDWESGAVEVLREEVPWPAGERPRRAGVSSFGVSGTNAHVIVEEAPAEQEAARTERGPLPFVLSGRSEAVVAAQARALAEHLRDTPELGLTDAAWTLATGRARFDVRAAVLGDDRAGVCAELDALAEGRPSADAVAPVTSAPRKPVLVFPGQGAQWVGMARDLLESSEVFAESMSRCAEALSPHTDWKLLDVVRGDGGPDPHERVDVLQPVLFSIMVSLAELWRAHGVTPAAVVGHSQGEIAAAHVAGALSLEAAAKVVALRSQVLRELDDQGGMVSVGASRDELETVLARWDGRVAVAAVNGPGTSVVAGPTAELDEFFAEAEAREMKPRRIAVRYASHSPEVARIEDRLAAELGTITAVRGSVPLHSTVTGEVIDTSAMDASYWYRNLRRPVLFEQAVRGLVEQGFDTFVEVSPHPVLLMAVEETAEHAGAEVTCVPTLRREQSGPHEFLRNLLRAHVHGVGADLRPAVAGGRPAELPTYPFEHQRFWPRPHRPADVSALGVRGAEHPLLLAAVDVPGHGGAVFTGRLSTDEQPWLAEHVVGGRTLVPGSVLVDLALAAGEDVGLPVLEELVLQRPLVLAGAGALLRMSVGAPDESGRRTIDVHAAEDVADLADAQWSQHATGTLAQGVAAGPRDTEQWPPEDAVRIPLDDHYDGLAEQGYEYGPSFQALRAAWRKDDSVYAEVSIAADEEGYAFHPVLLDAVAQTLSLGALGEPGGGKLPFAWNTVTLHASGATSVRVVATPAGADAMALRVTDPAGHLVATVDSLVVRSTGEKWEQPEPRGGEGELHALDWGRLAEPGSTGRVVAADASDLDAVLRSGEPEPDAVLVRYEPEGDDPRAAARHGVLWAAALVRRWLEQEELPGATLVIATSGAVTVSDDDSVPEPGAAAMWGVIRCAQAESPDRFVLLDTDAEPGMLPAVPDNPQLALRGDDVFVPRLSPLAPSALTLPAGTQRLVPGDGAIDSVAFEPAPDVEQPLRAGEVRVDVRATGVNFRDVLLALGMYPQKADMGTEAAGVVTAVGPDVDAFAPGDRVLGLFQGAFAPIAVTDHRLLARVPDGWSDADAAAVPIAYTTAHYALHDLAGLRAGQSVLIHAAAGGVGMAAVALARRAGAEVLATAGPAKHGTLRALGLDDEHIASSRETGFARKFRERTGGRGVDVVLNSLTGELLDESADLLAEDGVFVEMGKTDLRDAGDFRGRYAPFDLGEAGDDRLGEILREVVGLLGAGELDRLPVSAWELGSAPAALQHMSRGRHVGKLVLTQPAPVDPDGTVLITGGTGTLGRLLARHLVTEHGVRHLLLVSRRGADAPGSDELRAEIEDLGASAEIAACDTADRDALSALLDGLPRPLTGVVHAAGVLADGLVTSIDEPAVEQVLRAKVDAAWNLHELTANTGLSFFVLFSSAASVLAGPGQGVYAAANESLNALAALRRTRGLPAKALGWGLWAQASEMTSGLGDRIARTGVAALPTERALALFDSALRRGGEVVFPLSINRSALRRAEFVPEVLRGMVRAKLRAAGQAEAAGPNVVDRLAGRSESDQVAGLAELVRSHAAAVSGYGSADQLPERKAFKDLGFDSLAAVELRNRLGTATGVRLPSTLVFDHPTPLAVAEHLRDRLFAASPAVDIGDRLDELEKALEALSAEDGHDDVGQRLESLLRRWNSRRADAPSTSAISEDASDDELFSMLDQRFGGGEDL [Source organism chain A]=Saccharopolyspora erythraea [UniProt ID chain B]=Q03132 [UniProt boundaries chain B]=3490-3547 [UniProt coverage chain B]=1% [Name chain B]=6-deoxyerythronolide-B synthase EryA2, modules 3 and 4 [UniProt sequence chain B]=MTDSEKVAEYLRRATLDLRAARQRIRELESDPIAIVSMACRLPGGVNTPQRLWELLREGGETLSGFPTDRGWDLARLHHPDPDNPGTSYVDKGGFLDDAAGFDAEFFGVSPREAAAMDPQQRLLLETSWELVENAGIDPHSLRGTATGVFLGVAKFGYGEDTAAAEDVEGYSVTGVAPAVASGRISYTMGLEGPSISVDTACSSSLVALHLAVESLRKGESSMAVVGGAAVMATPGVFVDFSRQRALAADGRSKAFGAGADGFGFSEGVTLVLLERLSEARRNGHEVLAVVRGSALNQDGASNGLSAPSGPAQRRVIRQALESCGLEPGDVDAVEAHGTGTALGDPIEANALLDTYGRDRDADRPLWLGSVKSNIGHTQAAAGVTGLLKVVLALRNGELPATLHVEEPTPHVDWSSGGVALLAGNQPWRRGERTRRARVSAFGISGTNAHVIVEEAPEREHRETTAHDGRPVPLVVSARTTAALRAQAAQIAELLERPDADLAGVGLGLATTRARHEHRAAVVASTREEAVRGLREIAAGAATADAVVEGVTEVDGRNVVFLFPGQGSQWAGMGAELLSSSPVFAGKIRACDESMAPMQDWKVSDVLRQAPGAPGLDRVDVVQPVLFAVMVSLAELWRSYGVEPAAVVGHSQGEIAAAHVAGALTLEDAAKLVVGRSRLMRSLSGEGGMAAVALGEAAVRERLRPWQDRLSVAAVNGPRSVVVSGEPGALRAFSEDCAAEGIRVRDIDVDYASHSPQIERVREELLETTGDIAPRPARVTFHSTVESRSMDGTELDARYWYRNLRETVRFADAVTRLAESGYDAFIEVSPHPVVVQAVEEAVEEADGAEDAVVVGSLHRDGGDLSAFLRSMATAHVSGVDIRWDVALPGAAPFALPTYPFQRKRYWLQPAAPAAASDELAYRVSWTPIEKPESGNLDGDWLVVTPLISPEWTEMLCEAINANGGRALRCEVDTSASRTEMAQAVAQAGTGFRGVLSLLSSDESACRPGVPAGAVGLLTLVQALGDAGVDAPVWCLTQGAVRTPADDDLARPAQTTAHGFAQVAGLELPGRWGGVVDLPESVDDAALRLLVAVLRGGGRAEDHLAVRDGRLHGRRVVRASLPQSGSRSWTPHGTVLVTGAASPVGDQLVRWLADRGAERLVLAGACPGDDLLAAVEEAGASAVVCAQDAAALREALGDEPVTALVHAGTLTNFGSISEVAPEEFAETIAAKTALLAVLDEVLGDRAVEREVYCSSVAGIWGGAGMAAYAAGSAYLDALAEHHRARGRSCTSVAWTPWALPGGAVDDGYLRERGLRSLSADRAMRTWERVLAAGPVSVAVADVDWPVLSEGFAATRPTALFAELAGRGGQAEAEPDSGPTGEPAQRLAGLSPDEQQENLLELVANAVAEVLGHESAAEINVRRAFSELGLDSLNAMALRKRLSASTGLRLPASLVFDHPTVTALAQHLRARLVGDADQAAVRVVGAADESEPIAIVGIGCRFPGGIGSPEQLWRVLAEGANLTTGFPADRGWDIGRLYHPDPDNPGTSYVDKGGFLTDAADFDPGFFGITPREALAMDPQQRLMLETAWEAVERAGIDPDALRGTDTGVFVGMNGQSYMQLLAGEAERVDGYQGLGNSASVLSGRIAYTFGWEGPALTVDTACSSSLVGIHLAMQALRRGECSLALAGGVTVMSDPYTFVDFSTQRGLASDGRCKAFSARADGFALSEGVAALVLEPLSRARANGHQVLAVLRGSAVNQDGASNGLAAPNGPSQERVIRQALAASGVPAADVDVVEAHGTGTELGDPIEAGALIATYGQDRDRPLRLGSVKTNIGHTQAAAGAAGVIKVVLAMRHGMLPRSLHADELSPHIDWESGAVEVLREEVPWPAGERPRRAGVSSFGVSGTNAHVIVEEAPAEQEAARTERGPLPFVLSGRSEAVVAAQARALAEHLRDTPELGLTDAAWTLATGRARFDVRAAVLGDDRAGVCAELDALAEGRPSADAVAPVTSAPRKPVLVFPGQGAQWVGMARDLLESSEVFAESMSRCAEALSPHTDWKLLDVVRGDGGPDPHERVDVLQPVLFSIMVSLAELWRAHGVTPAAVVGHSQGEIAAAHVAGALSLEAAAKVVALRSQVLRELDDQGGMVSVGASRDELETVLARWDGRVAVAAVNGPGTSVVAGPTAELDEFFAEAEAREMKPRRIAVRYASHSPEVARIEDRLAAELGTITAVRGSVPLHSTVTGEVIDTSAMDASYWYRNLRRPVLFEQAVRGLVEQGFDTFVEVSPHPVLLMAVEETAEHAGAEVTCVPTLRREQSGPHEFLRNLLRAHVHGVGADLRPAVAGGRPAELPTYPFEHQRFWPRPHRPADVSALGVRGAEHPLLLAAVDVPGHGGAVFTGRLSTDEQPWLAEHVVGGRTLVPGSVLVDLALAAGEDVGLPVLEELVLQRPLVLAGAGALLRMSVGAPDESGRRTIDVHAAEDVADLADAQWSQHATGTLAQGVAAGPRDTEQWPPEDAVRIPLDDHYDGLAEQGYEYGPSFQALRAAWRKDDSVYAEVSIAADEEGYAFHPVLLDAVAQTLSLGALGEPGGGKLPFAWNTVTLHASGATSVRVVATPAGADAMALRVTDPAGHLVATVDSLVVRSTGEKWEQPEPRGGEGELHALDWGRLAEPGSTGRVVAADASDLDAVLRSGEPEPDAVLVRYEPEGDDPRAAARHGVLWAAALVRRWLEQEELPGATLVIATSGAVTVSDDDSVPEPGAAAMWGVIRCAQAESPDRFVLLDTDAEPGMLPAVPDNPQLALRGDDVFVPRLSPLAPSALTLPAGTQRLVPGDGAIDSVAFEPAPDVEQPLRAGEVRVDVRATGVNFRDVLLALGMYPQKADMGTEAAGVVTAVGPDVDAFAPGDRVLGLFQGAFAPIAVTDHRLLARVPDGWSDADAAAVPIAYTTAHYALHDLAGLRAGQSVLIHAAAGGVGMAAVALARRAGAEVLATAGPAKHGTLRALGLDDEHIASSRETGFARKFRERTGGRGVDVVLNSLTGELLDESADLLAEDGVFVEMGKTDLRDAGDFRGRYAPFDLGEAGDDRLGEILREVVGLLGAGELDRLPVSAWELGSAPAALQHMSRGRHVGKLVLTQPAPVDPDGTVLITGGTGTLGRLLARHLVTEHGVRHLLLVSRRGADAPGSDELRAEIEDLGASAEIAACDTADRDALSALLDGLPRPLTGVVHAAGVLADGLVTSIDEPAVEQVLRAKVDAAWNLHELTANTGLSFFVLFSSAASVLAGPGQGVYAAANESLNALAALRRTRGLPAKALGWGLWAQASEMTSGLGDRIARTGVAALPTERALALFDSALRRGGEVVFPLSINRSALRRAEFVPEVLRGMVRAKLRAAGQAEAAGPNVVDRLAGRSESDQVAGLAELVRSHAAAVSGYGSADQLPERKAFKDLGFDSLAAVELRNRLGTATGVRLPSTLVFDHPTPLAVAEHLRDRLFAASPAVDIGDRLDELEKALEALSAEDGHDDVGQRLESLLRRWNSRRADAPSTSAISEDASDDELFSMLDQRFGGGEDL [Source organism chain B]=Saccharopolyspora erythraea [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharopolyspora erythraea [Accession]=MF2120025 [Entry] [Entry number]=145 [Entry name]=Human glutathione S-transferase A1 [PDB ID]=1k3y [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glutathione S-transferase [Evidence level]=Direct evidence [Evidence text]=The urea-induced unfolding/refolding of human glutathione S-transferase A1 dimer has been shown to be a two-state process (PMID:9548764) with the association of disordered monomers forming a structured dimer. While there may be some structuring of the monomers before dimerization, this partial structure does not fully stabilize the protein (PMID:10600132). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110017,MF2100012,MF2110018 [UniProt ID chain A]=P08263 [UniProt boundaries chain A]=2-222 [UniProt coverage chain A]=99% [Name chain A]=Glutathione S-transferase A1 [UniProt sequence chain A]=MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P08263 [UniProt boundaries chain B]=2-222 [UniProt coverage chain B]=99% [Name chain B]=Glutathione S-transferase A1 [UniProt sequence chain B]=MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.30 [Source organism]=Homo sapiens [Accession]=MF2100012 [Entry] [Entry number]=146 [Entry name]=Archaeal histone hMfB [PDB ID]=1bfm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) and archaeal histone [Evidence level]=Direct evidence [Evidence text]=Data on the GdmCl-induced unfolding and refolding transitions of the dimer (monitored by stopped-flow far UV CD) fitted to a two-state model (PMID:15313621). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2130001,MF7000001,MF7000002,MF7000004,MF7000005,MF7000384,MF7000385 [UniProt ID chain A]=P19267 [UniProt boundaries chain A]=1-69 [UniProt coverage chain A]=100% [Name chain A]=DNA-binding protein HMf-2 [UniProt sequence chain A]=MELPIAPIGRIIKDAGAERVSDDARITLAKILEEMGRDIASEAIKLARHAGRKTIKAEDIELAVRRFKK [Source organism chain A]=Methanothermus fervidus [UniProt ID chain B]=P19267 [UniProt boundaries chain B]=1-69 [UniProt coverage chain B]=100% [Name chain B]=DNA-binding protein HMf-2 [UniProt sequence chain B]=MELPIAPIGRIIKDAGAERVSDDARITLAKILEEMGRDIASEAIKLARHAGRKTIKAEDIELAVRRFKK [Source organism chain B]=Methanothermus fervidus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Methanothermus fervidus [Accession]=MF2130001 [Entry] [Entry number]=147 [Entry name]=S100B [PDB ID]=1uwo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P04271 [UniProt boundaries chain A]=2-92 [UniProt coverage chain A]=98% [Name chain A]=Protein S100-B [UniProt sequence chain A]=MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P04271 [UniProt boundaries chain B]=2-92 [UniProt coverage chain B]=98% [Name chain B]=Protein S100-B [UniProt sequence chain B]=MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2100013 [Entry] [Entry number]=148 [Entry name]=Dynein light chain TcTex-1 [PDB ID]=1ygt [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Tctex-1 family [Evidence level]=Direct evidence [Evidence text]=The equilibrium unfolding transition of the dynein light chain TcTex-1 dimer was monitored by intrinsic fluorescence intensity, fluorescence anisotropy, and circular dichroism and was modeled as a two-state mechanism where a folded dimer dissociates to two unfolded monomers without populating thermodynamically stable monomeric or dimeric intermediates (PMID:16734416). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000137,MF2110016 [UniProt ID chain A]=Q94524 [UniProt boundaries chain A]=8-111 [UniProt coverage chain A]=93% [Name chain A]=Dynein light chain Tctex-type [UniProt sequence chain A]=MDDSREESQFIVDDVSKTIKEAIETTIGGNAYQHDKVNNWTGQVVENCLTVLTKEQKPYKYIVTAMIMQKNGAGLHTASSCYWNNDTDGSCTVRWENKTMYCIVSVFGLAV [Source organism chain A]=Drosophila melanogaster [UniProt ID chain A-2]=Q94524 [UniProt boundaries chain A-2]=8-111 [UniProt coverage chain A-2]=93% [Name chain A-2]=Dynein light chain Tctex-type [UniProt sequence chain A-2]=MDDSREESQFIVDDVSKTIKEAIETTIGGNAYQHDKVNNWTGQVVENCLTVLTKEQKPYKYIVTAMIMQKNGAGLHTASSCYWNNDTDGSCTVRWENKTMYCIVSVFGLAV [Source organism chain A-2]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Drosophila melanogaster [Accession]=MF2110016 [Entry] [Entry number]=149 [Entry name]=Dihydrofolate reductase [PDB ID]=1cz3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The enzyme DHFR from the hyperthermophilic bacterium Thermotoga maritima represents an extremely stable dimer; no isolated structured monomers could be detected in equilibrium or during unfolding. The equilibrium unfolding strictly follows the two-state model for the dimer (PMID:10413491). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q60034 [UniProt boundaries chain A]=2-165 [UniProt coverage chain A]=97% [Name chain A]=Dihydrofolate reductase [UniProt sequence chain A]=MAKVIFVLAMDVSGKIASSVESWSSFEDRKNFRKITTEIGNVVMGRITFEEIGRPLPERLNVVLTRRPKTSNNPSLVFFNGSPADVVKFLEGKGYERVAVIGGKTVFTEFLREKLVDELFVTVEPYVFGKGIPFFDEFEGYFPLKLLEMRRLNERGTLFLKYSVEKSHR [Source organism chain A]=/ MSB8) [UniProt ID chain B]=Q60034 [UniProt boundaries chain B]=2-169 [UniProt coverage chain B]=99% [Name chain B]=Dihydrofolate reductase [UniProt sequence chain B]=MAKVIFVLAMDVSGKIASSVESWSSFEDRKNFRKITTEIGNVVMGRITFEEIGRPLPERLNVVLTRRPKTSNNPSLVFFNGSPADVVKFLEGKGYERVAVIGGKTVFTEFLREKLVDELFVTVEPYVFGKGIPFFDEFEGYFPLKLLEMRRLNERGTLFLKYSVEKSHR [Source organism chain B]=/ MSB8) [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=/ MSB8) [Accession]=MF2120026 [Entry] [Entry number]=150 [Entry name]=Type II dihydrofolate reductase [PDB ID]=2rh2 [Chains]=A-3,A,A-4,A-2 [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homotetrameric enzymes [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Using absorbance, fluorescence, and circular dichroism the unfolding of type II DHFR is protein concentration dependent and can be described by a two-state model involving native dimer and unfolded monomer (PMID:1932013). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-3]=N/A [Evidence chain A-4]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P00383 [UniProt boundaries chain A]=21-78 [UniProt coverage chain A]=74% [Name chain A]=Dihydrofolate reductase type 2 [UniProt sequence chain A]=MERSSNEVSNPVAGNFVFPSNATFGMGDRVRKKSGAAWQGQIVGWYCTNLTPEGYAVESEAHPGSVQIYPVAALERIN [Source organism chain A]=Escherichia coli [UniProt ID chain A-3]=P00383 [UniProt boundaries chain A-3]=21-78 [UniProt coverage chain A-3]=74% [Name chain A-3]=Dihydrofolate reductase type 2 [UniProt sequence chain A-3]=MERSSNEVSNPVAGNFVFPSNATFGMGDRVRKKSGAAWQGQIVGWYCTNLTPEGYAVESEAHPGSVQIYPVAALERIN [Source organism chain A-3]=Escherichia coli [UniProt ID chain A-4]=P00383 [UniProt boundaries chain A-4]=21-78 [UniProt coverage chain A-4]=74% [Name chain A-4]=Dihydrofolate reductase type 2 [UniProt sequence chain A-4]=MERSSNEVSNPVAGNFVFPSNATFGMGDRVRKKSGAAWQGQIVGWYCTNLTPEGYAVESEAHPGSVQIYPVAALERIN [Source organism chain A-4]=Escherichia coli [UniProt ID chain A-2]=P00383 [UniProt boundaries chain A-2]=21-78 [UniProt coverage chain A-2]=74% [Name chain A-2]=Dihydrofolate reductase type 2 [UniProt sequence chain A-2]=MERSSNEVSNPVAGNFVFPSNATFGMGDRVRKKSGAAWQGQIVGWYCTNLTPEGYAVESEAHPGSVQIYPVAALERIN [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=0.96 [Source organism]=Escherichia coli [Accession]=MF4120007 [Entry] [Entry number]=151 [Entry name]=Class pi glutathione S-transferase (Sus scrofa) [PDB ID]=2gsr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glutathione S-transferase [Evidence level]=Direct evidence [Evidence text]=Guanidine hydrochloride and urea induced denaturation of the dimer is well described by a two-state model involving significant populations of only the folded dimer and unfolded monomer. Neither a folded, active monomeric form nor stable unfolding intermediates were detected (PMID:1930226). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110017,MF2100012,MF2110018 [UniProt ID chain A]=P80031 [UniProt boundaries chain A]=1-206 [UniProt coverage chain A]=99% [Name chain A]=Glutathione S-transferase P [UniProt sequence chain A]=PPYTITYFPVRGRCEAMRMLLADQDQSWKEEVVTMETWPPLKPSCLFRQLPKFQDGDLTLYQSNAILRHLGRSFGLYGKDQKEAALVDMVNDGVEDLRCKYATLIYTNYEAGKEKYVKELPEHLKPFETLLSQNQGGQAFVVGSQISFADYNLLDLLRIHQVLNPSCLDAFPLLSAYVARLSARPKIKAFLASPEHVNRPINGNGKN [Source organism chain A]=Sus scrofa [UniProt ID chain B]=P80031 [UniProt boundaries chain B]=1-206 [UniProt coverage chain B]=99% [Name chain B]=Glutathione S-transferase P [UniProt sequence chain B]=PPYTITYFPVRGRCEAMRMLLADQDQSWKEEVVTMETWPPLKPSCLFRQLPKFQDGDLTLYQSNAILRHLGRSFGLYGKDQKEAALVDMVNDGVEDLRCKYATLIYTNYEAGKEKYVKELPEHLKPFETLLSQNQGGQAFVVGSQISFADYNLLDLLRIHQVLNPSCLDAFPLLSAYVARLSARPKIKAFLASPEHVNRPINGNGKN [Source organism chain B]=Sus scrofa [ExpTech]=X-ray [Resolution]=2.11 [Source organism]=Sus scrofa [Accession]=MF2110017 [Entry] [Entry number]=152 [Entry name]=Glutathione S-transferase (Schistosoma japonicum) [PDB ID]=4wr4 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glutathione S-transferase [Evidence level]=Direct evidence [Evidence text]=Data of the urea- and temperature-induced unfolding of the dimer indicate the absence of thermodynamically stable intermediates and that the unfolding/refolding transition is a two-state process involving folded native dimer and unfolded monomer. Thermograms obtained by differential scanning microcalorimetry also fitted a two-state unfolding transition model (PMID:9041642). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF2110017,MF2100012,MF2110018 [UniProt ID chain A]=P08515 [UniProt boundaries chain A]=2-217 [UniProt coverage chain A]=99% [Name chain A]=Glutathione S-transferase class-mu 26 kDa isozyme [UniProt sequence chain A]=MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPK [Source organism chain A]=Schistosoma japonicum [UniProt ID chain A-2]=P08515 [UniProt boundaries chain A-2]=2-217 [UniProt coverage chain A-2]=99% [Name chain A-2]=Glutathione S-transferase class-mu 26 kDa isozyme [UniProt sequence chain A-2]=MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPK [Source organism chain A-2]=Schistosoma japonicum [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Schistosoma japonicum [Accession]=MF2110018 [Entry] [Entry number]=153 [Entry name]=Monellin [PDB ID]=1krl [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The two chains of monellin have been shown to be unstructured prior to assembly of the dimer. While the native dimeric structure is reached through various competing pathways entailing different intermediates, these partially structured states can only arise after the encounter complex has been formed (PMID:22542529). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P02881 [UniProt boundaries chain A]=2-45 [UniProt coverage chain A]=97% [Name chain A]=Monellin chain A [UniProt sequence chain A]=FREIKGYEYQLYVYASDKLFRADISEDYKTRGRKLLRFNGPVPPP [Source organism chain A]=Dioscoreophyllum cumminsii [UniProt ID chain B]=P02882 [UniProt boundaries chain B]=1-48 [UniProt coverage chain B]=96% [Name chain B]=Monellin chain B [UniProt sequence chain B]=GEWEIIDIGPFTQNLGKFAVDEENKIGQYGRLTFNKVIRPCMKKTIYEEN [Source organism chain B]=Dioscoreophyllum cumminsii [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Dioscoreophyllum cumminsii [Accession]=MF2210014 [Entry] [Entry number]=154 [Entry name]=Bacterial antitoxin CcdA [PDB ID]=2adl [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:17007877). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00928 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP00928 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=P62552 [UniProt boundaries chain A]=1-72 [UniProt coverage chain A]=100% [Name chain A]=Antitoxin CcdA [UniProt sequence chain A]=MKQRITVTVDSDSYQLLKAYDVNISGLVSTTMQNEARRLRAERWKAENQEGMAEVARFIEMNGSFADENRDW [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P62552 [UniProt boundaries chain B]=1-72 [UniProt coverage chain B]=100% [Name chain B]=Antitoxin CcdA [UniProt sequence chain B]=MKQRITVTVDSDSYQLLKAYDVNISGLVSTTMQNEARRLRAERWKAENQEGMAEVARFIEMNGSFADENRDW [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF2120027 [Entry] [Entry number]=155 [Entry name]=Nucleoside diphosphate kinase (Dictyostelium discoideum) [PDB ID]=1npk [Chains]=A-2,A-3,A-5,A,A-4,A-6 [Total number of chains]=6 [Assembly]=Hexamer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homohexameric enzymes [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The hexameric NDP kinase from Dictyostelium discoideum displays one single, irreversible differential scanning calorimetry peak (Tm:62°C) over a broad protein concentration, indicating a single step denaturation. However, the P105G substitution, which affects a loop implicated in subunit contacts, yields a protein that reversibly dissociates to folded monomers at 38°C before the irreversible denaturation occurs (Tm:47°C). These data indicate a “coupling” of the quaternary structure with the tertiary structure in the wild-type, but not in the mutated protein (PMID:8663370). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Evidence chain A-3]=N/A [Evidence chain A-5]=N/A [Evidence chain A-4]=N/A [Evidence chain A-6]=N/A [Similar structures]=None [UniProt ID chain A]=P22887 [UniProt boundaries chain A]=6-155 [UniProt coverage chain A]=96% [Name chain A]=Nucleoside diphosphate kinase, cytosolic [UniProt sequence chain A]=MSTNKVNKERTFLAVKPDGVARGLVGEIIARYEKKGFVLVGLKQLVPTKDLAESHYAEHKERPFFGGLVSFITSGPVVAMVFEGKGVVASARLMIGVTNPLASAPGSIRGDFGVDVGRNIIHGSDSVESANREIALWFKPEELLTEVKPNPNLYE [Source organism chain A]=Dictyostelium discoideum [UniProt ID chain A-2]=P22887 [UniProt boundaries chain A-2]=6-155 [UniProt coverage chain A-2]=96% [Name chain A-2]=Nucleoside diphosphate kinase, cytosolic [UniProt sequence chain A-2]=MSTNKVNKERTFLAVKPDGVARGLVGEIIARYEKKGFVLVGLKQLVPTKDLAESHYAEHKERPFFGGLVSFITSGPVVAMVFEGKGVVASARLMIGVTNPLASAPGSIRGDFGVDVGRNIIHGSDSVESANREIALWFKPEELLTEVKPNPNLYE [Source organism chain A-2]=Dictyostelium discoideum [UniProt ID chain A-3]=P22887 [UniProt boundaries chain A-3]=6-155 [UniProt coverage chain A-3]=96% [Name chain A-3]=Nucleoside diphosphate kinase, cytosolic [UniProt sequence chain A-3]=MSTNKVNKERTFLAVKPDGVARGLVGEIIARYEKKGFVLVGLKQLVPTKDLAESHYAEHKERPFFGGLVSFITSGPVVAMVFEGKGVVASARLMIGVTNPLASAPGSIRGDFGVDVGRNIIHGSDSVESANREIALWFKPEELLTEVKPNPNLYE [Source organism chain A-3]=Dictyostelium discoideum [UniProt ID chain A-5]=P22887 [UniProt boundaries chain A-5]=6-155 [UniProt coverage chain A-5]=96% [Name chain A-5]=Nucleoside diphosphate kinase, cytosolic [UniProt sequence chain A-5]=MSTNKVNKERTFLAVKPDGVARGLVGEIIARYEKKGFVLVGLKQLVPTKDLAESHYAEHKERPFFGGLVSFITSGPVVAMVFEGKGVVASARLMIGVTNPLASAPGSIRGDFGVDVGRNIIHGSDSVESANREIALWFKPEELLTEVKPNPNLYE [Source organism chain A-5]=Dictyostelium discoideum [UniProt ID chain A-4]=P22887 [UniProt boundaries chain A-4]=6-155 [UniProt coverage chain A-4]=96% [Name chain A-4]=Nucleoside diphosphate kinase, cytosolic [UniProt sequence chain A-4]=MSTNKVNKERTFLAVKPDGVARGLVGEIIARYEKKGFVLVGLKQLVPTKDLAESHYAEHKERPFFGGLVSFITSGPVVAMVFEGKGVVASARLMIGVTNPLASAPGSIRGDFGVDVGRNIIHGSDSVESANREIALWFKPEELLTEVKPNPNLYE [Source organism chain A-4]=Dictyostelium discoideum [UniProt ID chain A-6]=P22887 [UniProt boundaries chain A-6]=6-155 [UniProt coverage chain A-6]=96% [Name chain A-6]=Nucleoside diphosphate kinase, cytosolic [UniProt sequence chain A-6]=MSTNKVNKERTFLAVKPDGVARGLVGEIIARYEKKGFVLVGLKQLVPTKDLAESHYAEHKERPFFGGLVSFITSGPVVAMVFEGKGVVASARLMIGVTNPLASAPGSIRGDFGVDVGRNIIHGSDSVESANREIALWFKPEELLTEVKPNPNLYE [Source organism chain A-6]=Dictyostelium discoideum [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Dictyostelium discoideum [Accession]=MF6110001 [Entry] [Entry number]=156 [Entry name]=Superoxide dismutase (SOD) [PDB ID]=2c9v [Chains]=A,F [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=CD measurements and a global analysis decomposition of the time-resolved fluorescence decay over denaturant concentration shows the presence of an intermediate in the unfolding of human SOD by guanidinium hydrochloride. Considering previous measurements of partially denatured HSOD as a function of protein concentration (PMID:1510915), these results strongly suggest that the unfolding intermediate is a monomer that displays a molten globule state (PMID:8298055). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain F]=N/A [Similar structures]=None [UniProt ID chain A]=P00441 [UniProt boundaries chain A]=2-154 [UniProt coverage chain A]=99% [Name chain A]=Superoxide dismutase [Cu-Zn] [UniProt sequence chain A]=MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ [Source organism chain A]=Homo sapiens [UniProt ID chain F]=P00441 [UniProt boundaries chain F]=2-154 [UniProt coverage chain F]=99% [Name chain F]=Superoxide dismutase [Cu-Zn] [UniProt sequence chain F]=MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ [Source organism chain F]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.07 [Source organism]=Homo sapiens [Accession]=MF2100014 [Entry] [Entry number]=158 [Entry name]=4-aminobutyrate aminotransferase [PDB ID]=1ohv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Aminotransferase class-III [Evidence level]=Direct evidence [Evidence text]=The equilibrium unfolding of pig liver 4-aminobutyrate aminotransferase by urea was found to be a cooperative process. The kinetic results indicated that the aminotransferase unfolds in a single kinetic phase (PMID:8075151). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110019,MF7000973 [UniProt ID chain A]=P80147 [UniProt boundaries chain A]=39-499 [UniProt coverage chain A]=92% [Name chain A]=4-aminobutyrate aminotransferase, mitochondrial [UniProt sequence chain A]=MASVLLTRRLACSFRHNHRLLVPGWRHISQAAAKVDVEFDYDGPLMKTEVPGPRSRELMKQLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSIPIGYSHPALVKLVQQPQNVSTFINRPALGILPPENFVEKLRESLLSVAPKGMSQLITMACGSCSNENAFKTIFMWYRSKERGQSAFSKEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDISRKHGCAFLVDEVQTGGGSTGKFWAHEHWGLDDPADVMTFSKKMMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLSNAAHAGKVLLTGLLDLQARYPQFISRVRGRGTFCSFDTPDESIRNKLISIARNKGVMLGGCGDKSIRFRPTLVFRDHHAHLFLNIFSDILADFK [Source organism chain A]=Sus scrofa [UniProt ID chain B]=P80147 [UniProt boundaries chain B]=39-499 [UniProt coverage chain B]=92% [Name chain B]=4-aminobutyrate aminotransferase, mitochondrial [UniProt sequence chain B]=MASVLLTRRLACSFRHNHRLLVPGWRHISQAAAKVDVEFDYDGPLMKTEVPGPRSRELMKQLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSIPIGYSHPALVKLVQQPQNVSTFINRPALGILPPENFVEKLRESLLSVAPKGMSQLITMACGSCSNENAFKTIFMWYRSKERGQSAFSKEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDISRKHGCAFLVDEVQTGGGSTGKFWAHEHWGLDDPADVMTFSKKMMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLSNAAHAGKVLLTGLLDLQARYPQFISRVRGRGTFCSFDTPDESIRNKLISIARNKGVMLGGCGDKSIRFRPTLVFRDHHAHLFLNIFSDILADFK [Source organism chain B]=Sus scrofa [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Sus scrofa [Accession]=MF2110019 [Entry] [Entry number]=159 [Entry name]=Dimeric Mnt repressor [PDB ID]=1mnt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Arc-like DNA binding domain [Evidence level]=Direct evidence [Evidence text]=The Arc repressor protein has been experimentally shown to be a molten globule in monomeric form (PMID:8446590,PMID:7696567). Adopting the proper three dimensional structure is linked to dimerization (PMID:8110744,PMID:10889040). The Mnt repressor shows a high degree of sequential and structural similarity with the Arc and MetJ repressors (PMID:7999761) that both have been shown to adopt a stable structure only via dimerization (PMID:8110744,PMID:1390748). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000013,MF2140011,MF2140001,MF7000011,MF7000015,MF7000012,MF7000014 [UniProt ID chain A]=P03049 [UniProt boundaries chain A]=2-67 [UniProt coverage chain A]=79% [Name chain A]=Regulatory protein mnt [UniProt sequence chain A]=MARDDPHFNFRMPMEVREKLKFRAEANGRSMNSELLQIVQDALSKPSPVTGYRNDAERLADEQSELVKKMVFDTLKDLYKKTT [Source organism chain A]=Salmonella phage P22 [UniProt ID chain B]=P03049 [UniProt boundaries chain B]=2-67 [UniProt coverage chain B]=79% [Name chain B]=Regulatory protein mnt [UniProt sequence chain B]=MARDDPHFNFRMPMEVREKLKFRAEANGRSMNSELLQIVQDALSKPSPVTGYRNDAERLADEQSELVKKMVFDTLKDLYKKTT [Source organism chain B]=Salmonella phage P22 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella phage P22 [Accession]=MF2140011 [Entry] [Entry number]=160 [Entry name]=Dimeric serine proteinase from Semliki Forest virus core protein [PDB ID]=1vcq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00999 covers 95% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP00999 covers 95% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=P03315 [UniProt boundaries chain A]=119-267 [UniProt coverage chain A]=11% [Name chain A]=Structural polyprotein [UniProt sequence chain A]=MNYIPTQTFYGRRWRPRPAARPWPLQATPVAPVVPDFQAQQMQQLISAVNALTMRQNAIAPARPPKPKKKKTTKPKPKTQPKKINGKTQQQKKKDKQADKKKKKPGKRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEWSAPLITAMCVLANATFPCFQPPCVPCCYENNAEATLRMLEDNVDRPGYYDLLQAALTCRNGTRHRRSVSQHFNVYKATRPYIAYCADCGAGHSCHSPVAIEAVRSEATDGMLKIQFSAQIGIDKSDNHDYTKIRYADGHAIENAVRSSLKVATSGDCFVHGTMGHFILAKCPPGEFLQVSIQDTRNAVRACRIQYHHDPQPVGREKFTIRPHYGKEIPCTTYQQTTAETVEEIDMHMPPDTPDRTLLSQQSGNVKITVGGKKVKYNCTCGTGNVGTTNSDMTINTCLIEQCHVSVTDHKKWQFNSPFVPRADEPARKGKVHIPFPLDNITCRVPMAREPTVIHGKREVTLHLHPDHPTLFSYRTLGEDPQYHEEWVTAAVERTIPVPVDGMEYHWGNNDPVRLWSQLTTEGKPHGWPHQIVQYYYGLYPAATVSAVVGMSLLALISIFASCYMLVAARSKCLTPYALTPGAAVPWTLGILCCAPRAHAASVAETMAYLWDQNQALFWLEFAAPVACILIITYCLRNVLCCCKSLSFLVLLSLGATARAYEHSTVMPNVVGFPYKAHIERPGYSPLTLQMQVVETSLEPTLNLEYITCEYKTVVPSPYVKCCGASECSTKEKPDYQCKVYTGVYPFMWGGAYCFCDSENTQLSEAYVDRSDVCRHDHASAYKAHTASLKAKVRVMYGNVNQTVDVYVNGDHAVTIGGTQFIFGPLSSAWTPFDNKIVVYKDEVFNQDFPPYGSGQPGRFGDIQSRTVESNDLYANTALKLARPSPGMVHVPYTQTPSGFKYWLKEKGTALNTKAPFGCQIKTNPVRAMNCAVGNIPVSMNLPDSAFTRIVEAPTIIDLTCTVATCTHSSDFGGVLTLTYKTNKNGDCSVHSHSNVATLQEATAKVKTAGKVTLHFSTASASPSFVVSLCSARATCSASCEPPKDHIVPYAASHSNVVFPDMSGTALSWVQKISGGLGAFAIGAILVLVVVTCIGLRR [Source organism chain A]=Semliki forest virus [UniProt ID chain B]=P03315 [UniProt boundaries chain B]=119-267 [UniProt coverage chain B]=11% [Name chain B]=Structural polyprotein [UniProt sequence chain B]=MNYIPTQTFYGRRWRPRPAARPWPLQATPVAPVVPDFQAQQMQQLISAVNALTMRQNAIAPARPPKPKKKKTTKPKPKTQPKKINGKTQQQKKKDKQADKKKKKPGKRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEWSAPLITAMCVLANATFPCFQPPCVPCCYENNAEATLRMLEDNVDRPGYYDLLQAALTCRNGTRHRRSVSQHFNVYKATRPYIAYCADCGAGHSCHSPVAIEAVRSEATDGMLKIQFSAQIGIDKSDNHDYTKIRYADGHAIENAVRSSLKVATSGDCFVHGTMGHFILAKCPPGEFLQVSIQDTRNAVRACRIQYHHDPQPVGREKFTIRPHYGKEIPCTTYQQTTAETVEEIDMHMPPDTPDRTLLSQQSGNVKITVGGKKVKYNCTCGTGNVGTTNSDMTINTCLIEQCHVSVTDHKKWQFNSPFVPRADEPARKGKVHIPFPLDNITCRVPMAREPTVIHGKREVTLHLHPDHPTLFSYRTLGEDPQYHEEWVTAAVERTIPVPVDGMEYHWGNNDPVRLWSQLTTEGKPHGWPHQIVQYYYGLYPAATVSAVVGMSLLALISIFASCYMLVAARSKCLTPYALTPGAAVPWTLGILCCAPRAHAASVAETMAYLWDQNQALFWLEFAAPVACILIITYCLRNVLCCCKSLSFLVLLSLGATARAYEHSTVMPNVVGFPYKAHIERPGYSPLTLQMQVVETSLEPTLNLEYITCEYKTVVPSPYVKCCGASECSTKEKPDYQCKVYTGVYPFMWGGAYCFCDSENTQLSEAYVDRSDVCRHDHASAYKAHTASLKAKVRVMYGNVNQTVDVYVNGDHAVTIGGTQFIFGPLSSAWTPFDNKIVVYKDEVFNQDFPPYGSGQPGRFGDIQSRTVESNDLYANTALKLARPSPGMVHVPYTQTPSGFKYWLKEKGTALNTKAPFGCQIKTNPVRAMNCAVGNIPVSMNLPDSAFTRIVEAPTIIDLTCTVATCTHSSDFGGVLTLTYKTNKNGDCSVHSHSNVATLQEATAKVKTAGKVTLHFSTASASPSFVVSLCSARATCSASCEPPKDHIVPYAASHSNVVFPDMSGTALSWVQKISGGLGAFAIGAILVLVVVTCIGLRR [Source organism chain B]=Semliki forest virus [ExpTech]=X-ray [Resolution]=3.10 [Source organism]=Semliki forest virus [Accession]=MF2140012 [Entry] [Entry number]=162 [Entry name]=SinR dimerization domain [PDB ID]=2yal [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P06533 [UniProt boundaries chain A]=75-109 [UniProt coverage chain A]=31% [Name chain A]=HTH-type transcriptional regulator SinR [UniProt sequence chain A]=MIGQRIKQYRKEKGYSLSELAEKAGVAKSYLSSIERNLQTNPSIQFLEKVSAVLDVSVHTLLDEKHETEYDGQLDSEWEKLVRDAMTSGVSKKQFREFLDYQKWRKSQKEE [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P06533 [UniProt boundaries chain B]=75-108 [UniProt coverage chain B]=30% [Name chain B]=HTH-type transcriptional regulator SinR [UniProt sequence chain B]=MIGQRIKQYRKEKGYSLSELAEKAGVAKSYLSSIERNLQTNPSIQFLEKVSAVLDVSVHTLLDEKHETEYDGQLDSEWEKLVRDAMTSGVSKKQFREFLDYQKWRKSQKEE [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=2.27 [Source organism]=Bacillus subtilis [Accession]=MF2120029 [Entry] [Entry number]=163 [Entry name]=The mid-region of tropomyosin [PDB ID]=2b9c [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Tropomyosin [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:16365313). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110025,MF2110020 [UniProt ID chain A]=P04692 [UniProt boundaries chain A]=98-208 [UniProt coverage chain A]=39% [Name chain A]=Tropomyosin alpha-1 chain [UniProt sequence chain A]=MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P04692 [UniProt boundaries chain B]=93-208 [UniProt coverage chain B]=40% [Name chain B]=Tropomyosin alpha-1 chain [UniProt sequence chain B]=MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI [Source organism chain B]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Rattus norvegicus [Accession]=MF2110020 [Entry] [Entry number]=164 [Entry name]=Antitoxin RelB [PDB ID]=2k29 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:18501926). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P0C079 [UniProt boundaries chain A]=1-50 [UniProt coverage chain A]=63% [Name chain A]=Antitoxin RelB [UniProt sequence chain A]=MGSINLRIDDELKARSYAALEKMGVTPSEALRLMLEYIADNERLPFKQTLLSDEDAELVEIVKERLRNPKPVRVTLDEL [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0C079 [UniProt boundaries chain B]=1-50 [UniProt coverage chain B]=63% [Name chain B]=Antitoxin RelB [UniProt sequence chain B]=MGSINLRIDDELKARSYAALEKMGVTPSEALRLMLEYIADNERLPFKQTLLSDEDAELVEIVKERLRNPKPVRVTLDEL [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF2120030 [Entry] [Entry number]=165 [Entry name]=Dimerization domain of the rabies virus phosphoprotein [PDB ID]=3l32 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q0GBY3 [UniProt boundaries chain A]=90-133 [UniProt coverage chain A]=14% [Name chain A]=Phosphoprotein [UniProt sequence chain A]=MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNQAHLQGEPIEVDDLPEDMKRLHLDDEKSSNLGEMVRVGEGKYREDFQMDEGEDPNLLFQSYLDNVGVQIVRQMRSGERFLKIWSQTVEEIVSYVTVNFPNPPRRSSENKSTQTTGRELKKETTSAFSQRESQPSKARMVAQVAPGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVKEAKNVPGVTRLAHDGSKIPLRCVLGYVALANSKKFQLLVEADKLSKIMQDDLNRYTSC [Source organism chain A]=Rabies virus [UniProt ID chain B]=Q0GBY3 [UniProt boundaries chain B]=90-133 [UniProt coverage chain B]=14% [Name chain B]=Phosphoprotein [UniProt sequence chain B]=MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNQAHLQGEPIEVDDLPEDMKRLHLDDEKSSNLGEMVRVGEGKYREDFQMDEGEDPNLLFQSYLDNVGVQIVRQMRSGERFLKIWSQTVEEIVSYVTVNFPNPPRRSSENKSTQTTGRELKKETTSAFSQRESQPSKARMVAQVAPGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVKEAKNVPGVTRLAHDGSKIPLRCVLGYVALANSKKFQLLVEADKLSKIMQDDLNRYTSC [Source organism chain B]=Rabies virus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Rabies virus [Accession]=MF2140014 [Entry] [Entry number]=166 [Entry name]=Capsid protein C fragment from dengue virus capsid protein [PDB ID]=1r6r [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Capsid proteins [Sequence domain]=Flavivirus capsid protein C [Evidence level]=Direct evidence [Evidence text]=The structure of flavivirus C protein shows a fold with a large hydrophobic dimerization surface contributed by two pairs of helices, one of which has characteristics of a coiled-coil. The large relative interaction surface area explains the high stability of the dimer and is consistent with the estimated Kd < 10 nM. The hydrophobic core of the dimer is assembled from both monomers, which strongly suggests that the monomeric form of the protein would be unstable (PMID:14993605). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2140015,MF7000391 [UniProt ID chain A]=P12823 [UniProt boundaries chain A]=21-100 [UniProt coverage chain A]=2% [Name chain A]=Genome polyprotein [UniProt sequence chain A]=MNDQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRTAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTKDGTNMCTLMAMDLGELCEDTITYKCPFLKQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETWILRHPGFTIMAAILAYTIGTTHFQRVLIFILLTAIAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTDSRCPTQGEPTLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFTCKKNMEGKIVQPENLEYTVVITPHSGEEHAVGNDTGKHGKEVKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQMKDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKTPFEIMDLEKRHVLGRLTTVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLDWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFVTDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITSELNHILSENEVKLTIMTGDIKGIMQVGKRSLRPQPTELRYSWKTWGKAKMLSTELHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLRLREKQDAFCDSKLMSAAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMVIPKNFAGPVSQHNNRPGYHTQTAGPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVSSLVTAGHGQIDNFSLGILGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDLGRVMVMVGATMTDDIGMGVTYLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSSIPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAILCVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVSILASSLLKNDTPMTGPLVAGGLLTVCYVLTGRSADLELERATDVKWDDQAEISGSSPILSITISEDGSMSIKNEEEEQTLTILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGKAELEDGAYRIKQKGILGYSQIGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFRTNTGTIGAVSLDFSPGTSGSPIVDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPIRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWNSGHEWVTDFKGKTVWFVPSIKTGNDIAACLRKNGKRVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAGPMPVTHSSAAQRRGRIGRNPRNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRLRGEARKTFVDLMRRGDLPVWLAYKVAAEGINYADRRWCFDGTRNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGKAYNHALSELPETLETLLLLTLLATVTGGIFLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVIIAILTVVAATMANEMGFLEKTKKDLGLGNIATQQPESNILDIDLRPASAWTLYAVATTFITPMLRHSIENSSVNVSLTAIANQATVLMGLGKGWPLSKMDIGVPLLAIGCYSQVNPITLTAALLLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDPIPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPVSTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIMKNTTSTRRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNLVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFVPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCVKVLNPYMPSVIERMETLQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESETPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMVNGVVRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFTKKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILREVSKKEGGAMYADDTAGWDTRITIEDLKNEEMITNHMAGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGIFKSIQHLTASEEIAVQDWLARVGRERLSRMAISGDDCVVKPLDDRFARALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFCSHHFHELIMKDGRTLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHASHEWMTTEDMLTVWNKVWILENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQVRSLIGNEEYTDYMPSMKRFRREEEEAGVLW [Source organism chain A]=Dengue virus type 2 [UniProt ID chain B]=P12823 [UniProt boundaries chain B]=21-100 [UniProt coverage chain B]=2% [Name chain B]=Genome polyprotein [UniProt sequence chain B]=MNDQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRTAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTKDGTNMCTLMAMDLGELCEDTITYKCPFLKQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETWILRHPGFTIMAAILAYTIGTTHFQRVLIFILLTAIAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTDSRCPTQGEPTLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFTCKKNMEGKIVQPENLEYTVVITPHSGEEHAVGNDTGKHGKEVKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQMKDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKTPFEIMDLEKRHVLGRLTTVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLDWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFVTDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITSELNHILSENEVKLTIMTGDIKGIMQVGKRSLRPQPTELRYSWKTWGKAKMLSTELHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLRLREKQDAFCDSKLMSAAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMVIPKNFAGPVSQHNNRPGYHTQTAGPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVSSLVTAGHGQIDNFSLGILGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDLGRVMVMVGATMTDDIGMGVTYLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSSIPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAILCVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVSILASSLLKNDTPMTGPLVAGGLLTVCYVLTGRSADLELERATDVKWDDQAEISGSSPILSITISEDGSMSIKNEEEEQTLTILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGKAELEDGAYRIKQKGILGYSQIGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFRTNTGTIGAVSLDFSPGTSGSPIVDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPIRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWNSGHEWVTDFKGKTVWFVPSIKTGNDIAACLRKNGKRVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAGPMPVTHSSAAQRRGRIGRNPRNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRLRGEARKTFVDLMRRGDLPVWLAYKVAAEGINYADRRWCFDGTRNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGKAYNHALSELPETLETLLLLTLLATVTGGIFLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVIIAILTVVAATMANEMGFLEKTKKDLGLGNIATQQPESNILDIDLRPASAWTLYAVATTFITPMLRHSIENSSVNVSLTAIANQATVLMGLGKGWPLSKMDIGVPLLAIGCYSQVNPITLTAALLLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDPIPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPVSTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIMKNTTSTRRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNLVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFVPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCVKVLNPYMPSVIERMETLQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESETPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMVNGVVRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFTKKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILREVSKKEGGAMYADDTAGWDTRITIEDLKNEEMITNHMAGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGIFKSIQHLTASEEIAVQDWLARVGRERLSRMAISGDDCVVKPLDDRFARALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFCSHHFHELIMKDGRTLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHASHEWMTTEDMLTVWNKVWILENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQVRSLIGNEEYTDYMPSMKRFRREEEEAGVLW [Source organism chain B]=Dengue virus type 2 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Dengue virus type 2 [Accession]=MF2140015 [Entry] [Entry number]=167 [Entry name]=ID2 HLH homodimer [PDB ID]=4aya [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Basic helix-loop-helix (bHLH) [Sequence domain]=Helix-loop-helix DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294, PMID:9488706). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100009,MF2110021,MF2110023,MF2100010,MF7000192,MF7000402,MF7000403,MF7000444,MF7000371 [UniProt ID chain A]=Q02363 [UniProt boundaries chain A]=30-82 [UniProt coverage chain A]=39% [Name chain A]=DNA-binding protein inhibitor ID-2 [UniProt sequence chain A]=MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKALCG [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q02363 [UniProt boundaries chain B]=35-82 [UniProt coverage chain B]=35% [Name chain B]=DNA-binding protein inhibitor ID-2 [UniProt sequence chain B]=MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKALCG [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Homo sapiens [Accession]=MF2110021 [Entry] [Entry number]=168 [Entry name]=Cobra venom nerve growth factor (NGF) [PDB ID]=4ec7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=NGF-like [Sequence domain]=Cystine-knot cytokine/NGF-like [Evidence level]=Direct evidence [Evidence text]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110010,MF2200009,MF2100007,MF2100008,MF2201009,MF2110022,MF2110011,MF7000016,MF7000017 [UniProt ID chain A]=P61898 [UniProt boundaries chain A]=9-116 [UniProt coverage chain A]=93% [Name chain A]=Venom nerve growth factor [UniProt sequence chain A]=EDHPVHNLGEHSVCDSVSAWVTKTTATDIKGNTVTVMENVNLDNKVYKEYFFETKCKNPNPEPSGCRGIDSSHWNSYCTETDTFIKALTMEGNQASWRFIRIETACVCVITKKKGN [Source organism chain A]=Naja atra [UniProt ID chain B]=P61898 [UniProt boundaries chain B]=9-116 [UniProt coverage chain B]=93% [Name chain B]=Venom nerve growth factor [UniProt sequence chain B]=EDHPVHNLGEHSVCDSVSAWVTKTTATDIKGNTVTVMENVNLDNKVYKEYFFETKCKNPNPEPSGCRGIDSSHWNSYCTETDTFIKALTMEGNQASWRFIRIETACVCVITKKKGN [Source organism chain B]=Naja atra [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Naja atra [Accession]=MF2110022 [Entry] [Entry number]=169 [Entry name]=SopB dimerization domain [PDB ID]=3kz5 [Chains]=B,E [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain E]=The region(s) described in DP02863 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP02863 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain E]=P62558 [UniProt boundaries chain E]=276-319 [UniProt coverage chain E]=13% [Name chain E]=Protein SopB [UniProt sequence chain E]=MKRAPVIPKHTLNTQPVEDTSLSTPAAPMVDSLIARVGVMARGNAITLPVCGRDVKFTLEVLRGDSVEKTSRVWSGNERDQELLTEDALDDLIPSFLLTGQQTPAFGRRVSGVIEIADGSRRRKAAALTESDYRVLVGELDDEQMAALSRLGNDYRPTSAYERGQRYASRLQNEFAGNISALADAENISRKIITRCINTAKLPKSVVALFSHPGELSARSGDALQKAFTDKEELLKQQASNLHEQKKAGVIFEAEEVITLLTSVLKTSSASRTSLSSRHQFAPGATVLYKGDKMVLNLDRSRVPTECIEKIEAILKELEKPAP [Source organism chain E]=Escherichia coli [UniProt ID chain B]=P62558 [UniProt boundaries chain B]=276-319 [UniProt coverage chain B]=13% [Name chain B]=Protein SopB [UniProt sequence chain B]=MKRAPVIPKHTLNTQPVEDTSLSTPAAPMVDSLIARVGVMARGNAITLPVCGRDVKFTLEVLRGDSVEKTSRVWSGNERDQELLTEDALDDLIPSFLLTGQQTPAFGRRVSGVIEIADGSRRRKAAALTESDYRVLVGELDDEQMAALSRLGNDYRPTSAYERGQRYASRLQNEFAGNISALADAENISRKIITRCINTAKLPKSVVALFSHPGELSARSGDALQKAFTDKEELLKQQASNLHEQKKAGVIFEAEEVITLLTSVLKTSSASRTSLSSRHQFAPGATVLYKGDKMVLNLDRSRVPTECIEKIEAILKELEKPAP [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.58 [Source organism]=Escherichia coli [Accession]=MF2120031 [Entry] [Entry number]=170 [Entry name]=Basic HLH/leucine zipper domain of apo MITF [PDB ID]=4ath [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Basic helix-loop-helix (bHLH) [Sequence domain]=Helix-loop-helix DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294, PMID:9488706). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100009,MF2110021,MF2110023,MF2100010,MF7000192,MF7000402,MF7000403,MF7000444,MF7000371 [UniProt ID chain A]=Q08874 [UniProt boundaries chain A]=324-402 [UniProt coverage chain A]=15% [Name chain A]=Microphthalmia-associated transcription factor [UniProt sequence chain A]=MQSESGIVADFEVGEEFHEEPKTYYELKSQPLKSSSSAEHSGASKPPLSSSTMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVAVSQTPAINVSVPTTLPSATQVPMEVLKVQTHLENPTKYHIQQAQRHQVKQYLSTTLANKHASQVLSSPCPNQPGDHAMPPVPGSSAPNSPMAMLTLNSNCEKEAFYKFEEQSRAESECPGMNTHSRASCMQMDDVIDDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYSNQGLPPPGLTISNSCPANLPNIKRELTACIFPTESEARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQREQQRAKDLENRQKKLEHANRHLLLRVQELEMQARAHGLSLIPSTGLCSPDLVNRIIKQEPVLENCSQELVQHQADLTCTTTLDLTDGTITFTNNLGTMPESSPAYSIPRKMGSNLEDILMDDALSPVGVTDPLLSSVSPGASKTSSRRSSMSAEETEHAC [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q08874 [UniProt boundaries chain B]=324-402 [UniProt coverage chain B]=15% [Name chain B]=Microphthalmia-associated transcription factor [UniProt sequence chain B]=MQSESGIVADFEVGEEFHEEPKTYYELKSQPLKSSSSAEHSGASKPPLSSSTMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVAVSQTPAINVSVPTTLPSATQVPMEVLKVQTHLENPTKYHIQQAQRHQVKQYLSTTLANKHASQVLSSPCPNQPGDHAMPPVPGSSAPNSPMAMLTLNSNCEKEAFYKFEEQSRAESECPGMNTHSRASCMQMDDVIDDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYSNQGLPPPGLTISNSCPANLPNIKRELTACIFPTESEARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQREQQRAKDLENRQKKLEHANRHLLLRVQELEMQARAHGLSLIPSTGLCSPDLVNRIIKQEPVLENCSQELVQHQADLTCTTTLDLTDGTITFTNNLGTMPESSPAYSIPRKMGSNLEDILMDDALSPVGVTDPLLSSVSPGASKTSSRRSSMSAEETEHAC [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Mus musculus [Accession]=MF2110023 [Entry] [Entry number]=171 [Entry name]=Vimentin coil 1B fragment (trimeric) [PDB ID]=4ypc [Chains]=A-3,A,A-2 [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (trimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:26795465). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-3]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P08670 [UniProt boundaries chain A]=161-243 [UniProt coverage chain A]=17% [Name chain A]=Vimentin [UniProt sequence chain A]=MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE [Source organism chain A]=Homo sapiens [UniProt ID chain A-3]=P08670 [UniProt boundaries chain A-3]=161-243 [UniProt coverage chain A-3]=17% [Name chain A-3]=Vimentin [UniProt sequence chain A-3]=MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE [Source organism chain A-3]=Homo sapiens [UniProt ID chain A-2]=P08670 [UniProt boundaries chain A-2]=161-243 [UniProt coverage chain A-2]=17% [Name chain A-2]=Vimentin [UniProt sequence chain A-2]=MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.44 [Source organism]=Homo sapiens [Accession]=MF3100003 [Entry] [Entry number]=172 [Entry name]=Methionyl-tRNA synthetase from Pyrococcus abyssi [PDB ID]=1mkh [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The C-terminal dimerization region of methionyl-tRNA synthetase is highly mobile evading structure determination by X-ray (PMID: 14992601). In MetRS-C12K, the dimer interface mainly results from antiparallel beta-strand interactions. In addition, the two R1 helices are packed together, and the N-termini are in contact through hydrogen bonds involving the carbonyl group of M1 of one monomer and the side chain of N67 of the other monomer. Beta strand interactions involve the beta10 C-terminal strand of one monomer, which contacts the beta8 strand of the other monomer. Enhancement of tRNA-binding affinity conferred by the C-terminal domain is only expressed when the enzyme is in the dimeric state (PMID:12390027), so it is likely an obligate dimer. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q9V011 [UniProt boundaries chain A]=616-722 [UniProt coverage chain A]=14% [Name chain A]=Methionine--tRNA ligase [UniProt sequence chain A]=MVRYMVTSALPYANGPIHAGHLAGAYLPADIFVRYLRLKGEDVVFICGTDEHGTPISFRALKEGRSPREIVDEFHEQIKITFQRAKISFDFFGRTELPIHYKLSQEFFLKAYENGHLVKKVTKQAYCEHDKMFLPDRFVIGTCPYCGAEDQKGDQCEVCGRPLTPEILINPRCAICGRPISFRDSAHYYIKMQDFAERLKRWIEKQPWKPNVKNMVLSWIEEGLEERAITRDLNWGIPVPLDEEDMKGKVLYVWFEAPIGYISITIEHFKRIGKPNEWKKYWLNIDGQTRVIHFIGKDNIPFHAIFWPAFLMAYGKYKDEEVEAEWNLPYDIPANEYLTLEGKKFSTSRNWAIWVHEFLDVFPADYLRYYLTTIMPETRDSDFSFSDFKVRINEELVNNLGNFVHRALTFVNRYFDGVVPERGELDELDREALEEIEKAFKEVGELIMNYRFKDALKRVMSLASFGNRYFDHKQPWKTAKEDKVRTGTTVNISLQIVKALGILLEPFLPDASEKIWHLLNLDEVKRWEFRELPAGHKVRKPEILFKKVTDDQIIYFILNYMAKGNPEGARILLDKYYKREDVIRVAKEKFGDEAEVVLRRVYKDIKLKEKKEGKEMYVKFDDFAKLDLRVGKIIEVKDHPNADKLYVVKVDLGDEVRTLVAGLKKYYKPEELLNRYVVVVANLEPKKLRGIGSQGMLLAADDGERVALLMPDKEVKLGAKVR [Source organism chain A]=Pyrococcus abyssi [UniProt ID chain A-2]=Q9V011 [UniProt boundaries chain A-2]=616-722 [UniProt coverage chain A-2]=14% [Name chain A-2]=Methionine--tRNA ligase [UniProt sequence chain A-2]=MVRYMVTSALPYANGPIHAGHLAGAYLPADIFVRYLRLKGEDVVFICGTDEHGTPISFRALKEGRSPREIVDEFHEQIKITFQRAKISFDFFGRTELPIHYKLSQEFFLKAYENGHLVKKVTKQAYCEHDKMFLPDRFVIGTCPYCGAEDQKGDQCEVCGRPLTPEILINPRCAICGRPISFRDSAHYYIKMQDFAERLKRWIEKQPWKPNVKNMVLSWIEEGLEERAITRDLNWGIPVPLDEEDMKGKVLYVWFEAPIGYISITIEHFKRIGKPNEWKKYWLNIDGQTRVIHFIGKDNIPFHAIFWPAFLMAYGKYKDEEVEAEWNLPYDIPANEYLTLEGKKFSTSRNWAIWVHEFLDVFPADYLRYYLTTIMPETRDSDFSFSDFKVRINEELVNNLGNFVHRALTFVNRYFDGVVPERGELDELDREALEEIEKAFKEVGELIMNYRFKDALKRVMSLASFGNRYFDHKQPWKTAKEDKVRTGTTVNISLQIVKALGILLEPFLPDASEKIWHLLNLDEVKRWEFRELPAGHKVRKPEILFKKVTDDQIIYFILNYMAKGNPEGARILLDKYYKREDVIRVAKEKFGDEAEVVLRRVYKDIKLKEKKEGKEMYVKFDDFAKLDLRVGKIIEVKDHPNADKLYVVKVDLGDEVRTLVAGLKKYYKPEELLNRYVVVVANLEPKKLRGIGSQGMLLAADDGERVALLMPDKEVKLGAKVR [Source organism chain A-2]=Pyrococcus abyssi [ExpTech]=X-ray [Resolution]=2.01 [Source organism]=Pyrococcus abyssi [Accession]=MF2130002 [Entry] [Entry number]=173 [Entry name]=PE25-PPE41 heterodimer from M. tuberculosis [PDB ID]=4w4k [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Both proteins involved in the interaction evade successful expression, purification and crystallization in their monomeric form, owing to the fact that both proteins are disordered and are extremely susceptible to degradation (PMID:16690741). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=A0A0H3LBR3 [UniProt boundaries chain A]=8-89 [UniProt coverage chain A]=82% [Name chain A]=PE family protein [UniProt sequence chain A]=MSFVITNPEALTVAATEVRRIRDRAIQSDAQVAPMTTAVRPPAADLVSEKAATFLVEYARKYRQTIAAAAVVLEEFAHALTTGADKYATAEADNIKTFS [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=A0A0H3LBN6 [UniProt boundaries chain B]=2-174 [UniProt coverage chain B]=89% [Name chain B]=PPE family protein [UniProt sequence chain B]=MHFEAYPPEVNSANIYAGPGPDSMLAAARAWRSLDVEMTAVQRSFNRTLLSLMDAWAGPVVMQLMEAAKPFVRWLTDLCVQLSEVERQIHEIVRAYEWAHHDMVPLAQIYNNRAERQILIDNNALGQFTAQIADLDQEYDDFWDEDGEVMRDYRLRVSDALSKLTPWKAPPPIAHSTVLVAPVSPSTASSRTDT [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Mycobacterium tuberculosis [Accession]=MF2220002 [Entry] [Entry number]=174 [Entry name]=Vimentin coil 1B fragment (dimeric) [PDB ID]=3ssu [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:22869704). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P08670 [UniProt boundaries chain A]=144-189 [UniProt coverage chain A]=9% [Name chain A]=Vimentin [UniProt sequence chain A]=MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P08670 [UniProt boundaries chain B]=149-187 [UniProt coverage chain B]=8% [Name chain B]=Vimentin [UniProt sequence chain B]=MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Homo sapiens [Accession]=MF2100015 [Entry] [Entry number]=176 [Entry name]=OPTN:TBK1 complex [PDB ID]=5eof [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:27620379). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=Q96CV9 [UniProt boundaries chain A]=29-102 [UniProt coverage chain A]=12% [Name chain A]=Optineurin [UniProt sequence chain A]=MSHQPLSCLTEKEDSPSESTGNGPPHLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVVRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTGTALSKYRSRSADGAKNYFEHEELTVSQLLLCLREGNQKVERLEVALKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAIPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDSDQQAYLVQRGAEDRDWRQQRNIPIHSCPKCGEVLPDIDTLQIHVMDCII [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q96CV9 [UniProt boundaries chain B]=29-102 [UniProt coverage chain B]=12% [Name chain B]=Optineurin [UniProt sequence chain B]=MSHQPLSCLTEKEDSPSESTGNGPPHLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVVRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTGTALSKYRSRSADGAKNYFEHEELTVSQLLLCLREGNQKVERLEVALKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAIPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDSDQQAYLVQRGAEDRDWRQQRNIPIHSCPKCGEVLPDIDTLQIHVMDCII [Source organism chain B]=Homo sapiens [UniProt ID chain C]=Q9UHD2 [UniProt boundaries chain C]=678-720 [UniProt coverage chain C]=5% [Name chain C]=Serine/threonine-protein kinase TBK1 [UniProt sequence chain C]=MQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGLIYEKISLPKVHPRYDLDGDASMAKAITGVVCYACRIASTLLLYQELMRKGIRWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEKLMKINLEAAELGEISDIHTKLLRLSSSQGTIETSLQDIDSRLSPGGSLADAWAHQEGTHPKDRNVEKLQVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMTHFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNELQETLPQKMFTASSGIKHTMTPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL [Source organism chain C]=Homo sapiens [UniProt ID chain D]=Q9UHD2 [UniProt boundaries chain D]=679-719 [UniProt coverage chain D]=5% [Name chain D]=Serine/threonine-protein kinase TBK1 [UniProt sequence chain D]=MQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGLIYEKISLPKVHPRYDLDGDASMAKAITGVVCYACRIASTLLLYQELMRKGIRWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEKLMKINLEAAELGEISDIHTKLLRLSSSQGTIETSLQDIDSRLSPGGSLADAWAHQEGTHPKDRNVEKLQVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMTHFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNELQETLPQKMFTASSGIKHTMTPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Homo sapiens [Accession]=MF4200001 [Entry] [Entry number]=177 [Entry name]=p63/p73 hetero-tetramerization domain (human) [PDB ID]=2nb1 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=p53 tetramerization [Sequence domain]=P53 tetramerisation domain [Evidence level]=Direct evidence [Evidence text]=p53, p63, p73 and their homologues are all members of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF4100003,MF4100005,MF4110007,MF4110009,MF4200002 [UniProt ID chain A]=Q9H3D4 [UniProt boundaries chain A]=397-455 [UniProt coverage chain A]=8% [Name chain A]=Tumor protein 63 [UniProt sequence chain A]=MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSTKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEEGE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O15350 [UniProt boundaries chain B]=351-398 [UniProt coverage chain B]=7% [Name chain B]=Tumor protein p73 [UniProt sequence chain B]=MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH [Source organism chain B]=Homo sapiens [UniProt ID chain C]=Q9H3D4 [UniProt boundaries chain C]=397-455 [UniProt coverage chain C]=8% [Name chain C]=Tumor protein 63 [UniProt sequence chain C]=MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSTKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEEGE [Source organism chain C]=Homo sapiens [UniProt ID chain D]=O15350 [UniProt boundaries chain D]=351-398 [UniProt coverage chain D]=7% [Name chain D]=Tumor protein p73 [UniProt sequence chain D]=MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH [Source organism chain D]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF4200002 [Entry] [Entry number]=180 [Entry name]=Leukemia Fusion Target AF9 in complex with Dot1L [PDB ID]=2mv7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=AF9 is an intrinsically disordered protein, which binds competing disordered partners, most notably AF4, Dot1L, BCoR and hPC3. The two interacting protein regions undergo mutual synergistic folding (PMID:23260655). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01070 covers 100% of the sequence present in the structure [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P42568 [UniProt boundaries chain A]=500-568 [UniProt coverage chain A]=12% [Name chain A]=Protein AF-9 [UniProt sequence chain A]=MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKAGGDPNRSIHTSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSTSFSKPHKLMKEHKEKPSKDSREHKSAFKEPSRDHNKSSKESSKKPKENKPLKEEKIVPKMAFKEPKPMSKEPKPDSNLLTITSGQDKKAPSKRPPISDSEELSAKKRKKSSSEALFKSFSSAPPLILTCSADKKQIKDKSHVKMGKVKIESETSEKKKSTLPPFDDIVDPNDSDVEENISSKSDSEQPSPASSSSSSSSSFTPSQTRQQGPLRSIMKDLHSDDNEEESDEVEDNDNDSEMERPVNRGGSRSRRVSLSDGSDSESSSASSPLHHEPPPPLLKTNNNQILEVKSPIKQSKSDKQIKNGECDKAYLDELVELHRRLMTLRERHILQQIVNLIEETGHFHITNTTFDFDLCSLDKTTVRKLQSYLETSGTS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q8TEK3 [UniProt boundaries chain B]=877-900 [UniProt coverage chain B]=1% [Name chain B]=Histone-lysine N-methyltransferase, H3 lysine-79 specific [UniProt sequence chain B]=MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTANPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQRHSPNPLLVAPTPPALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKSCVPPDDALSLHLRGKGALGRELEPDASRLHLELDCTKFSLPHLSSMSPELSMNGQAAGYELCGVLSRPSSKQNTPQYLASPLDQEVVPCTPSHVGRPRLEKLSGLAAPDYTRLSPAKIVLRRHLSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRERAYGSSGELITSLPISIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVLQPRDPSSTLEKQIGANAHGAGSRSLALAPAGFSYAGSVAISGALAGSPASLTPGAEPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLNSMVSNINQPLEITAISSPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSPLQASSALSQNSLFTFRPALEEPSADAKLAAHPRKGFPGSLSGADGLSPGTNPANGCTFGGGLAADLSLHSFSDGASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLKGEGSRGKEAGEGGLPLCGPTDKTPLLSGKAAKARDREVDLKNGHNLFISAAAVPPGSLLSGPGLAPAASSAGGAASSAQTHRSFLGPFPPGPQFALGPMSLQANLGSVAGSSVLQSLFSSVPAAAGLVHVSSAATRLTNSHAMGSFSGVAGGTVGGN [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2200014 [Entry] [Entry number]=181 [Entry name]=SARS-Coronavirus HR2 Domain (prefusion, trimeric form) [PDB ID]=2fxp [Chains]=A,B,C [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (trimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:16507566). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Evidence chain C]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=P59594 [UniProt boundaries chain A]=1141-1193 [UniProt coverage chain A]=4% [Name chain A]=Spike glycoprotein [UniProt sequence chain A]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain A]=Severe acute respiratory syndrome coronavirus [UniProt ID chain B]=P59594 [UniProt boundaries chain B]=1141-1193 [UniProt coverage chain B]=4% [Name chain B]=Spike glycoprotein [UniProt sequence chain B]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain B]=Severe acute respiratory syndrome coronavirus [UniProt ID chain C]=P59594 [UniProt boundaries chain C]=1141-1193 [UniProt coverage chain C]=4% [Name chain C]=Spike glycoprotein [UniProt sequence chain C]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain C]=Severe acute respiratory syndrome coronavirus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Severe acute respiratory syndrome coronavirus [Accession]=MF3140002 [Entry] [Entry number]=182 [Entry name]=C-terminal coiled coil domain of Transient receptor potential (TRP) channel subfamily P member 2 [PDB ID]=3hrn [Chains]=A-3,A,A-2 [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (trimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:19556541). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-3]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q13563 [UniProt boundaries chain A]=833-895 [UniProt coverage chain A]=6% [Name chain A]=Polycystin-2 [UniProt sequence chain A]=MVNSSRVQPQQPGDAKRPPAPRAPDPGRLMAGCAAVGASLAAPGGLCEQRGLEIEMQRIRQAAARDPPAGAAASPSPPLSSCSRQAWSRDNPGFEAEEEEEEVEGEEGGMVVEMDVEWRPGSRRSAASSAVSSVGARSRGLGGYHGAGHPSGRRRRREDQGPPCPSPVGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESSTNREKYLKSVLRELVTYLLFLIVLCILTYGMMSSNVYYYTRMMSQLFLDTPVSKTEKTNFKTLSSMEDFWKFTEGSLLDGLYWKMQPSNQTEADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGTRATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLIRYVTTFDFFLAACEIIFCFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLEDQNTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEVKSDLAQQKAEMELSDLIRKGYHKALVKLKLKKNTVDDISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQMRDDLEKEREDLDLDHSSLPRPMSSRSFPRSLDDSEEDDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDERLGRDSEIHREQMERLVREELERWESDDAASQISHGLGTPVGLNGQPRPRSSRPSSSQSTEGMEGAGGNGSSNVHV [Source organism chain A]=Homo sapiens [UniProt ID chain A-3]=Q13563 [UniProt boundaries chain A-3]=833-895 [UniProt coverage chain A-3]=6% [Name chain A-3]=Polycystin-2 [UniProt sequence chain A-3]=MVNSSRVQPQQPGDAKRPPAPRAPDPGRLMAGCAAVGASLAAPGGLCEQRGLEIEMQRIRQAAARDPPAGAAASPSPPLSSCSRQAWSRDNPGFEAEEEEEEVEGEEGGMVVEMDVEWRPGSRRSAASSAVSSVGARSRGLGGYHGAGHPSGRRRRREDQGPPCPSPVGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESSTNREKYLKSVLRELVTYLLFLIVLCILTYGMMSSNVYYYTRMMSQLFLDTPVSKTEKTNFKTLSSMEDFWKFTEGSLLDGLYWKMQPSNQTEADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGTRATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLIRYVTTFDFFLAACEIIFCFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLEDQNTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEVKSDLAQQKAEMELSDLIRKGYHKALVKLKLKKNTVDDISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQMRDDLEKEREDLDLDHSSLPRPMSSRSFPRSLDDSEEDDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDERLGRDSEIHREQMERLVREELERWESDDAASQISHGLGTPVGLNGQPRPRSSRPSSSQSTEGMEGAGGNGSSNVHV [Source organism chain A-3]=Homo sapiens [UniProt ID chain A-2]=Q13563 [UniProt boundaries chain A-2]=833-895 [UniProt coverage chain A-2]=6% [Name chain A-2]=Polycystin-2 [UniProt sequence chain A-2]=MVNSSRVQPQQPGDAKRPPAPRAPDPGRLMAGCAAVGASLAAPGGLCEQRGLEIEMQRIRQAAARDPPAGAAASPSPPLSSCSRQAWSRDNPGFEAEEEEEEVEGEEGGMVVEMDVEWRPGSRRSAASSAVSSVGARSRGLGGYHGAGHPSGRRRRREDQGPPCPSPVGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESSTNREKYLKSVLRELVTYLLFLIVLCILTYGMMSSNVYYYTRMMSQLFLDTPVSKTEKTNFKTLSSMEDFWKFTEGSLLDGLYWKMQPSNQTEADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGTRATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLIRYVTTFDFFLAACEIIFCFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLEDQNTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEVKSDLAQQKAEMELSDLIRKGYHKALVKLKLKKNTVDDISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQMRDDLEKEREDLDLDHSSLPRPMSSRSFPRSLDDSEEDDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDERLGRDSEIHREQMERLVREELERWESDDAASQISHGLGTPVGLNGQPRPRSSRPSSSQSTEGMEGAGGNGSSNVHV [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Homo sapiens [Accession]=MF3100004 [Entry] [Entry number]=183 [Entry name]=L27 domain complex (D. melanogaster) [PDB ID]=4rp3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=L27 domains [Subclass]=L27_1 type [Sequence domain]=L27_1 [Evidence level]=Direct evidence [Evidence text]=The interacting chains form half of a heterotetrameric L27 complex (a dimer of dimers) (PMID:16147993). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110024,MF7000341,MF7000342 [UniProt ID chain A]=P31007 [UniProt boundaries chain A]=5-95 [UniProt coverage chain A]=9% [Name chain A]=Disks large 1 tumor suppressor protein [UniProt sequence chain A]=MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIFKSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWEKDGQAVKIADFIKSSNLNRNCAYEFNNDASSNQTNQSALNQNPIANNVSAQAQAEALSRTFKSELEEILNQRMRIESDTENAKEPTVEQQQKQQQAQQRSSRSPQQQNPQQQQGSKSRSGSQTVNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIYITKLISGGAAAADGRLSINDIIVSVNDVSVVDVPHASAVDALKKAGNVVKLHVKRKRGTATTPAAGSAAGDARDSAASGPKVIEIDLVKGGKGLGFSIAGGIGNQHIPGDNGIYVTKLMDGGAAQVDGRLSIGDKLIAVRTNGSEKNLENVTHELAVATLKSITDKVTLIIGKTQHLTTSASGGGGGGLSSGQQLSQSQSQLATSQSQSQVHQQQHATPMVNSQSTEPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGPQGLGFNIVGGEDGQGIYVSFILAGGPADLGSELKRGDQLLSVNNVNLTHATHEEAAQALKTSGGVVTLLAQYRPEEYNRFEARIQELKQQAALGAGGSGTLLRTTQKRSLYVRALFDYDPNRDDGLPSRGLPFKHGDILHVTNASDDEWWQARRVLGDNEDEQIGIVPSKRRWERKMRARDRSVKFQGHAAANNNLDKQSTLDRKKKNFTFSRKFPFMKSRDEKNEDGSDQEPFMLCYTQDDANAEGASEENVLSYEAVQRLSINYTRPVIILGPLKDRINDDLISEYPDKFGSCVPHTTRPKREYEVDGRDYHFVSSREQMERDIQNHLFIEAGQYNDNLYGTSVASVREVAEKGKHCILDVSGNAIKRLQVAQLYPVAVFIKPKSVDSVMEMNRRMTEEQAKKTYERAIKMEQEFGEYFTGVVQGDTIEEIYSKVKSMIWSQSGPTIWVPSKESL [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=P31007 [UniProt boundaries chain B]=6-95 [UniProt coverage chain B]=9% [Name chain B]=Disks large 1 tumor suppressor protein [UniProt sequence chain B]=MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIFKSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWEKDGQAVKIADFIKSSNLNRNCAYEFNNDASSNQTNQSALNQNPIANNVSAQAQAEALSRTFKSELEEILNQRMRIESDTENAKEPTVEQQQKQQQAQQRSSRSPQQQNPQQQQGSKSRSGSQTVNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIYITKLISGGAAAADGRLSINDIIVSVNDVSVVDVPHASAVDALKKAGNVVKLHVKRKRGTATTPAAGSAAGDARDSAASGPKVIEIDLVKGGKGLGFSIAGGIGNQHIPGDNGIYVTKLMDGGAAQVDGRLSIGDKLIAVRTNGSEKNLENVTHELAVATLKSITDKVTLIIGKTQHLTTSASGGGGGGLSSGQQLSQSQSQLATSQSQSQVHQQQHATPMVNSQSTEPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGPQGLGFNIVGGEDGQGIYVSFILAGGPADLGSELKRGDQLLSVNNVNLTHATHEEAAQALKTSGGVVTLLAQYRPEEYNRFEARIQELKQQAALGAGGSGTLLRTTQKRSLYVRALFDYDPNRDDGLPSRGLPFKHGDILHVTNASDDEWWQARRVLGDNEDEQIGIVPSKRRWERKMRARDRSVKFQGHAAANNNLDKQSTLDRKKKNFTFSRKFPFMKSRDEKNEDGSDQEPFMLCYTQDDANAEGASEENVLSYEAVQRLSINYTRPVIILGPLKDRINDDLISEYPDKFGSCVPHTTRPKREYEVDGRDYHFVSSREQMERDIQNHLFIEAGQYNDNLYGTSVASVREVAEKGKHCILDVSGNAIKRLQVAQLYPVAVFIKPKSVDSVMEMNRRMTEEQAKKTYERAIKMEQEFGEYFTGVVQGDTIEEIYSKVKSMIWSQSGPTIWVPSKESL [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=1.36 [Source organism]=Drosophila melanogaster [Accession]=MF2110024 [Entry] [Entry number]=184 [Entry name]=Tropomyosin dimer (Gallus gallus) [PDB ID]=1ic2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Tropomyosin [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:11438684). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110025,MF2110020 [UniProt ID chain A]=P04268 [UniProt boundaries chain A]=1-79 [UniProt coverage chain A]=27% [Name chain A]=Tropomyosin alpha-1 chain [UniProt sequence chain A]=MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEERSKQLEDELVALQKKLKGTEDELDKYSESLKDAQEKLELADKKATDAESEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAQKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERAEERAELSESKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI [Source organism chain A]=Gallus gallus [UniProt ID chain B]=P04268 [UniProt boundaries chain B]=1-77 [UniProt coverage chain B]=27% [Name chain B]=Tropomyosin alpha-1 chain [UniProt sequence chain B]=MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEERSKQLEDELVALQKKLKGTEDELDKYSESLKDAQEKLELADKKATDAESEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAQKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERAEERAELSESKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI [Source organism chain B]=Gallus gallus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Gallus gallus [Accession]=MF2110025 [Entry] [Entry number]=185 [Entry name]=N-Terminal dimerization domain Lis1 [PDB ID]=1uuj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Lis1 was shown to be a dimer under native conditions. Monitoring the chemically induced unfolding of the protein by fluorescence and by circular dichroism revealed that the reaction follows a single and coincident transition. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P63005 [UniProt boundaries chain A]=2-77 [UniProt coverage chain A]=18% [Name chain A]=Platelet-activating factor acetylhydrolase IB subunit beta [UniProt sequence chain A]=MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR [Source organism chain A]=Mus musculus [UniProt ID chain B]=P63005 [UniProt boundaries chain B]=2-75 [UniProt coverage chain B]=18% [Name chain B]=Platelet-activating factor acetylhydrolase IB subunit beta [UniProt sequence chain B]=MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.75 [Source organism]=Mus musculus [Accession]=MF2110026 [Entry] [Entry number]=186 [Entry name]=Mannose-binding lectin (Hyacinthoides hispanica) [PDB ID]=1b2p [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=According to the most probable oligomerization state stored in PDBe A-2,B chains were not considered. [Class]=Bulb-type lectin domain [Subclass]=Homodimeric lectin [Sequence domain]=Bulb-type lectin domain [Evidence level]=Direct evidence [Evidence text]=A closely homologous lectin of the same type sharing a high degree of sequence and structural similarity has been shown to follow a two-state folding process (PMID:11401577). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=MF2110027,MF2210010,MF2210012,MF2110015 [UniProt ID chain A]=Q9ZP49 [UniProt boundaries chain A]=22-140 [UniProt coverage chain A]=76% [Name chain A]=Lectin SCAman [UniProt sequence chain A]=CILSLIVIFGILTQLSLICNANNIIFSKQPDDNHPQILHATESLEILYGTHVYRFIMQTDCNLVLYDNNNPIWATNTGGLGNGCRAVLQPDGVLVVITNENVTVWQSPVAGKAGHYVLVLQPDRNVVIYGDALWATQTVRGGSGVMPLLKTRQIE [Source organism chain A]=Hyacinthoides hispanica [UniProt ID chain B-2]=Q9ZP49 [UniProt boundaries chain B-2]=22-140 [UniProt coverage chain B-2]=76% [Name chain B-2]=Lectin SCAman [UniProt sequence chain B-2]=CILSLIVIFGILTQLSLICNANNIIFSKQPDDNHPQILHATESLEILYGTHVYRFIMQTDCNLVLYDNNNPIWATNTGGLGNGCRAVLQPDGVLVVITNENVTVWQSPVAGKAGHYVLVLQPDRNVVIYGDALWATQTVRGGSGVMPLLKTRQIE [Source organism chain B-2]=Hyacinthoides hispanica [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Hyacinthoides hispanica [Accession]=MF2110027 [Entry] [Entry number]=187 [Entry name]=Dimerization domain of the type I alpha regulatory subunit of protein kinase A [PDB ID]=2ezw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P00514 [UniProt boundaries chain A]=13-62 [UniProt coverage chain A]=13% [Name chain A]=cAMP-dependent protein kinase type I-alpha regulatory subunit [UniProt sequence chain A]=MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV [Source organism chain A]=Bos taurus [UniProt ID chain B]=P00514 [UniProt boundaries chain B]=13-62 [UniProt coverage chain B]=13% [Name chain B]=cAMP-dependent protein kinase type I-alpha regulatory subunit [UniProt sequence chain B]=MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV [Source organism chain B]=Bos taurus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bos taurus [Accession]=MF2110028 [Entry] [Entry number]=188 [Entry name]=Coiled Coil Domain of Pawr [PDB ID]=5fiy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions. Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP00940 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP00940 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=Q62627 [UniProt boundaries chain A]=254-331 [UniProt coverage chain A]=23% [Name chain A]=PRKC apoptosis WT1 regulator protein [UniProt sequence chain A]=MATGGYRSSGSTTDFLEEWKAKREKMRAKQNPVGPGSSGGDPAAKSPAGPLAQTTAAGTSELNHGPAGAAAPAAPGPGALNCAHGSSALPRGAPGSRRPEDECPIAAGAAGAPASRGDEEEPDSAPEKGRSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAASLPDPGTSYLPQDPSRTVPGRYKSTISAPEEEILNRYPRTDRSGFSRHNRDTSAPANFASSSTLEKRIEDLEKEVLRERQENLRLTRLMQDKEEMIGKLKEEIDLLNRDLDDMEDENEQLKQENKTLLKVVGQLTR [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=Q62627 [UniProt boundaries chain B]=255-332 [UniProt coverage chain B]=23% [Name chain B]=PRKC apoptosis WT1 regulator protein [UniProt sequence chain B]=MATGGYRSSGSTTDFLEEWKAKREKMRAKQNPVGPGSSGGDPAAKSPAGPLAQTTAAGTSELNHGPAGAAAPAAPGPGALNCAHGSSALPRGAPGSRRPEDECPIAAGAAGAPASRGDEEEPDSAPEKGRSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAASLPDPGTSYLPQDPSRTVPGRYKSTISAPEEEILNRYPRTDRSGFSRHNRDTSAPANFASSSTLEKRIEDLEKEVLRERQENLRLTRLMQDKEEMIGKLKEEIDLLNRDLDDMEDENEQLKQENKTLLKVVGQLTR [Source organism chain B]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Rattus norvegicus [Accession]=MF2110029 [Entry] [Entry number]=189 [Entry name]=p53/p73-b homo-tetramerization domain (Ciona intestinalis) [PDB ID]=2mw4 [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=p53 tetramerization [Sequence domain]=P53 tetramerisation domain [Evidence level]=Direct evidence [Evidence text]=p53, p63, p73 and their homologues are all members of the p53 protein family. The tetramerization region of p53, p63 and p73 are closely homologous to each other, having very similar sequences, structures and biological functions (PMID:25185827,PMID:18289041,PMID:20379196), all containing the same Pfam domain (PF07710). The tetramerization domain of p53 exhibits a four-helix bundle structure bound by hydrophobic and electrostatic interactions (PMID:8023159). The tetramer is formed as a dimer of dimers and follows a two state folding and binding process, demonstrated in several chemical and thermal denaturation/refolding experiments (PMID:9582268,PMID:18410249,PMID:19913028). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF4100003,MF4100005,MF4110007,MF4110009,MF4200002 [UniProt ID chain A]=F6SSG7 [UniProt boundaries chain A]=374-419 [UniProt coverage chain A]=10% [Name chain A]=Cellular tumor antigen p53 [UniProt sequence chain A]=MAVADTSELNFPDSQESFSDFWMNTLSENNELPSWQTDLNQEYDQCKETVDVLQLDTTKANDIEFPVSEFLTSSQASQQSIGDLFAQSLPSTQCGGNSQVTTVSKHEYPDSGYVMTLPNNSVLAELQTSSLQTEVSLLPNNEYPGIYNFEINFGEKTESAPKSAPFTYSYSLQKLFVKMNENCPIKFRCSPQPPSGCVIRAIPVFEKPNNVTEIVTRCFNHRNECRTESSDSNTPNSHLIRVESKSNNIQYCLTHEGRECVVVPYEPPHSGSEYMALLYRFMCLSSCRTETGINRRPLLTIFNLESETGELLGKRVVSTRICACPGRDRTQEEEKKNVTSQNKSRKRLCKSATNSKSIPVVQKNEENKVDNDDDGDVVYTLNIRGKRKFEKVKEYKEALDLLDYVQPDVKKACCQRNQI [Source organism chain A]=Ciona intestinalis [UniProt ID chain B]=F6SSG7 [UniProt boundaries chain B]=374-419 [UniProt coverage chain B]=10% [Name chain B]=Cellular tumor antigen p53 [UniProt sequence chain B]=MAVADTSELNFPDSQESFSDFWMNTLSENNELPSWQTDLNQEYDQCKETVDVLQLDTTKANDIEFPVSEFLTSSQASQQSIGDLFAQSLPSTQCGGNSQVTTVSKHEYPDSGYVMTLPNNSVLAELQTSSLQTEVSLLPNNEYPGIYNFEINFGEKTESAPKSAPFTYSYSLQKLFVKMNENCPIKFRCSPQPPSGCVIRAIPVFEKPNNVTEIVTRCFNHRNECRTESSDSNTPNSHLIRVESKSNNIQYCLTHEGRECVVVPYEPPHSGSEYMALLYRFMCLSSCRTETGINRRPLLTIFNLESETGELLGKRVVSTRICACPGRDRTQEEEKKNVTSQNKSRKRLCKSATNSKSIPVVQKNEENKVDNDDDGDVVYTLNIRGKRKFEKVKEYKEALDLLDYVQPDVKKACCQRNQI [Source organism chain B]=Ciona intestinalis [UniProt ID chain C]=F6SSG7 [UniProt boundaries chain C]=374-419 [UniProt coverage chain C]=10% [Name chain C]=Cellular tumor antigen p53 [UniProt sequence chain C]=MAVADTSELNFPDSQESFSDFWMNTLSENNELPSWQTDLNQEYDQCKETVDVLQLDTTKANDIEFPVSEFLTSSQASQQSIGDLFAQSLPSTQCGGNSQVTTVSKHEYPDSGYVMTLPNNSVLAELQTSSLQTEVSLLPNNEYPGIYNFEINFGEKTESAPKSAPFTYSYSLQKLFVKMNENCPIKFRCSPQPPSGCVIRAIPVFEKPNNVTEIVTRCFNHRNECRTESSDSNTPNSHLIRVESKSNNIQYCLTHEGRECVVVPYEPPHSGSEYMALLYRFMCLSSCRTETGINRRPLLTIFNLESETGELLGKRVVSTRICACPGRDRTQEEEKKNVTSQNKSRKRLCKSATNSKSIPVVQKNEENKVDNDDDGDVVYTLNIRGKRKFEKVKEYKEALDLLDYVQPDVKKACCQRNQI [Source organism chain C]=Ciona intestinalis [UniProt ID chain D]=F6SSG7 [UniProt boundaries chain D]=374-419 [UniProt coverage chain D]=10% [Name chain D]=Cellular tumor antigen p53 [UniProt sequence chain D]=MAVADTSELNFPDSQESFSDFWMNTLSENNELPSWQTDLNQEYDQCKETVDVLQLDTTKANDIEFPVSEFLTSSQASQQSIGDLFAQSLPSTQCGGNSQVTTVSKHEYPDSGYVMTLPNNSVLAELQTSSLQTEVSLLPNNEYPGIYNFEINFGEKTESAPKSAPFTYSYSLQKLFVKMNENCPIKFRCSPQPPSGCVIRAIPVFEKPNNVTEIVTRCFNHRNECRTESSDSNTPNSHLIRVESKSNNIQYCLTHEGRECVVVPYEPPHSGSEYMALLYRFMCLSSCRTETGINRRPLLTIFNLESETGELLGKRVVSTRICACPGRDRTQEEEKKNVTSQNKSRKRLCKSATNSKSIPVVQKNEENKVDNDDDGDVVYTLNIRGKRKFEKVKEYKEALDLLDYVQPDVKKACCQRNQI [Source organism chain D]=Ciona intestinalis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Ciona intestinalis [Accession]=MF4110009 [Entry] [Entry number]=190 [Entry name]=Human respiratory syncytial virus fusion protein core [PDB ID]=1g2c [Chains]=A,B,C,D,E,F [Total number of chains]=6 [Assembly]=Hexamer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (hexameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:11106388). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Evidence chain E]=N/A [Evidence chain F]=N/A [Similar structures]=None [UniProt ID chain A]=P11209 [UniProt boundaries chain A]=160-209 [UniProt coverage chain A]=8% [Name chain A]=Fusion glycoprotein F0 [UniProt sequence chain A]=MELPILKTNAITAILAAVTLCFASSQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKSAVTELQLLMQSTPATNNRARRELPRFMNYTLNNTKNTNVTLSKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPLAETCKVQSNRVFCDTMNSLTLPSEVNLCNIDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKDRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLSLIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN [Source organism chain A]=Human respiratory syncytial virus A [UniProt ID chain B]=P11209 [UniProt boundaries chain B]=480-519 [UniProt coverage chain B]=6% [Name chain B]=Fusion glycoprotein F0 [UniProt sequence chain B]=MELPILKTNAITAILAAVTLCFASSQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKSAVTELQLLMQSTPATNNRARRELPRFMNYTLNNTKNTNVTLSKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPLAETCKVQSNRVFCDTMNSLTLPSEVNLCNIDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKDRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLSLIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN [Source organism chain B]=Human respiratory syncytial virus A [UniProt ID chain C]=P11209 [UniProt boundaries chain C]=160-207 [UniProt coverage chain C]=8% [Name chain C]=Fusion glycoprotein F0 [UniProt sequence chain C]=MELPILKTNAITAILAAVTLCFASSQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKSAVTELQLLMQSTPATNNRARRELPRFMNYTLNNTKNTNVTLSKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPLAETCKVQSNRVFCDTMNSLTLPSEVNLCNIDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKDRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLSLIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN [Source organism chain C]=Human respiratory syncytial virus A [UniProt ID chain D]=P11209 [UniProt boundaries chain D]=480-515 [UniProt coverage chain D]=6% [Name chain D]=Fusion glycoprotein F0 [UniProt sequence chain D]=MELPILKTNAITAILAAVTLCFASSQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKSAVTELQLLMQSTPATNNRARRELPRFMNYTLNNTKNTNVTLSKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPLAETCKVQSNRVFCDTMNSLTLPSEVNLCNIDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKDRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLSLIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN [Source organism chain D]=Human respiratory syncytial virus A [UniProt ID chain E]=P11209 [UniProt boundaries chain E]=160-207 [UniProt coverage chain E]=8% [Name chain E]=Fusion glycoprotein F0 [UniProt sequence chain E]=MELPILKTNAITAILAAVTLCFASSQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKSAVTELQLLMQSTPATNNRARRELPRFMNYTLNNTKNTNVTLSKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPLAETCKVQSNRVFCDTMNSLTLPSEVNLCNIDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKDRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLSLIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN [Source organism chain E]=Human respiratory syncytial virus A [UniProt ID chain F]=P11209 [UniProt boundaries chain F]=480-515 [UniProt coverage chain F]=6% [Name chain F]=Fusion glycoprotein F0 [UniProt sequence chain F]=MELPILKTNAITAILAAVTLCFASSQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKSAVTELQLLMQSTPATNNRARRELPRFMNYTLNNTKNTNVTLSKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPLAETCKVQSNRVFCDTMNSLTLPSEVNLCNIDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKDRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLSLIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN [Source organism chain F]=Human respiratory syncytial virus A [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Human respiratory syncytial virus A [Accession]=MF6240001 [Entry] [Entry number]=191 [Entry name]=Measles virus phosphoprotein tetramerization domain [PDB ID]=4bhv [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:23576502). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=P35974 [UniProt boundaries chain A]=307-360 [UniProt coverage chain A]=10% [Name chain A]=Phosphoprotein [UniProt sequence chain A]=MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKKGTERRLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPEYVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQPKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK [Source organism chain A]=panencephalitis virus) [UniProt ID chain B]=P35974 [UniProt boundaries chain B]=307-360 [UniProt coverage chain B]=10% [Name chain B]=Phosphoprotein [UniProt sequence chain B]=MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKKGTERRLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPEYVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQPKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK [Source organism chain B]=panencephalitis virus) [UniProt ID chain C]=P35974 [UniProt boundaries chain C]=307-360 [UniProt coverage chain C]=10% [Name chain C]=Phosphoprotein [UniProt sequence chain C]=MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKKGTERRLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPEYVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQPKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK [Source organism chain C]=panencephalitis virus) [UniProt ID chain D]=P35974 [UniProt boundaries chain D]=307-360 [UniProt coverage chain D]=10% [Name chain D]=Phosphoprotein [UniProt sequence chain D]=MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKKGTERRLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPEYVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQPKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK [Source organism chain D]=panencephalitis virus) [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=panencephalitis virus) [Accession]=MF4140003 [Entry] [Entry number]=192 [Entry name]=Core (C) protein from West Nile Virus [PDB ID]=1sfk [Chains]=A,B,C,D [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Capsid proteins [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=None [UniProt ID chain A]=P14335 [UniProt boundaries chain A]=25-97 [UniProt coverage chain A]=2% [Name chain A]=Genome polyprotein [UniProt sequence chain A]=MSKKPGGPGKSRAVNMLKRGMPRVLSLTGLKRAMLSLIDGRGPTRFVLALLAFFRFTAIAPTRAVLDRWRSVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAFMIGLIAGVGAVTLSNFQGKVMMTVNATDVTDIITIPPAAGKNLCIVRAMDVGHMCDDTITYECPVLSAGNDPEDIDCWCTKLAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLSNKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSELSTKAACPTMGEAHNDKRADPSFVCKQGVVDRGWGNGCGLFGKGSIDTCAKFACSTKATGRTILKENIKYEVAIFVHGPTTVESHGNYFTQTGAAQAGRFSITPAAPSYTLKLGEYGEVTVDCEPRSGIDTSAYYVMTVGTKTFLVHREWFMDLNLPWSSAESNVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFRFLGTPADTGHGTVVLELQYTGTDGPCKIPISSVASLNDLTPVGRLVTVNPFVSVSTANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTATLKGAQRLAALGDTAWDFGSVGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDISRQELRCGSGVFIHNDVEAWIDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSIVVEKQEGMYKSAPRRLTATTEKLEIGWKAWGKSILFAPELANNTFVIDGPETKECPTQNRAWNNLEVEDFGFGLTSTRMFLRVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRFNDTWKLERAVLGEVKSCTWPETHTLWGDGVLESDLIIPITLAGPRSNHNRRPGYKTQSQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDNGCWYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRYVILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAAFFQMAYYDARQILLWEMPDVLNSLAVAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGFFNPMILAAGLVACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWEGDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKRGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPVPAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVAREHNGNEIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTRVELGEAAAIFMTATPPGTSDPFPESNAPISDLQTEIPDRAWNSGYEWITEYIGKTVWFVPSVKMGNEIALCLQRAGKKVIQLNRKSYETEYPKCKNDDWDFVVTTDISEMGANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRTGRNPSQAGDEYCYGGHTNEDDSNCAHWTEARIMLDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWIDARVYSDHQALKSFKDFASGKRSQIGFIEVLGKMPEHFMGKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGVVLGAATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKSDISGLFGQRIETKENFSIGEFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYITTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTSATLLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQVMLILVSLAALVVNPSVKTVREAGILITAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLVKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFIRYRKEAITEVDRSAAKHARKERNITGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTLRVLEMVEDWLHRGPKEFCVKVLCPYMPKVIEKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKKTWKGPQYEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPKFWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILREVGTRPGGRIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLSENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVTPCRGQDELVGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDKTPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRSIIGDEKYVDYMSSLKRYEDTTLVEDTVL [Source organism chain A]=Kunjin virus [UniProt ID chain B]=P14335 [UniProt boundaries chain B]=41-97 [UniProt coverage chain B]=1% [Name chain B]=Genome polyprotein [UniProt sequence chain B]=MSKKPGGPGKSRAVNMLKRGMPRVLSLTGLKRAMLSLIDGRGPTRFVLALLAFFRFTAIAPTRAVLDRWRSVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAFMIGLIAGVGAVTLSNFQGKVMMTVNATDVTDIITIPPAAGKNLCIVRAMDVGHMCDDTITYECPVLSAGNDPEDIDCWCTKLAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLSNKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSELSTKAACPTMGEAHNDKRADPSFVCKQGVVDRGWGNGCGLFGKGSIDTCAKFACSTKATGRTILKENIKYEVAIFVHGPTTVESHGNYFTQTGAAQAGRFSITPAAPSYTLKLGEYGEVTVDCEPRSGIDTSAYYVMTVGTKTFLVHREWFMDLNLPWSSAESNVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFRFLGTPADTGHGTVVLELQYTGTDGPCKIPISSVASLNDLTPVGRLVTVNPFVSVSTANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTATLKGAQRLAALGDTAWDFGSVGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDISRQELRCGSGVFIHNDVEAWIDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSIVVEKQEGMYKSAPRRLTATTEKLEIGWKAWGKSILFAPELANNTFVIDGPETKECPTQNRAWNNLEVEDFGFGLTSTRMFLRVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRFNDTWKLERAVLGEVKSCTWPETHTLWGDGVLESDLIIPITLAGPRSNHNRRPGYKTQSQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDNGCWYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRYVILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAAFFQMAYYDARQILLWEMPDVLNSLAVAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGFFNPMILAAGLVACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWEGDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKRGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPVPAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVAREHNGNEIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTRVELGEAAAIFMTATPPGTSDPFPESNAPISDLQTEIPDRAWNSGYEWITEYIGKTVWFVPSVKMGNEIALCLQRAGKKVIQLNRKSYETEYPKCKNDDWDFVVTTDISEMGANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRTGRNPSQAGDEYCYGGHTNEDDSNCAHWTEARIMLDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWIDARVYSDHQALKSFKDFASGKRSQIGFIEVLGKMPEHFMGKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGVVLGAATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKSDISGLFGQRIETKENFSIGEFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYITTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTSATLLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQVMLILVSLAALVVNPSVKTVREAGILITAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLVKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFIRYRKEAITEVDRSAAKHARKERNITGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTLRVLEMVEDWLHRGPKEFCVKVLCPYMPKVIEKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKKTWKGPQYEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPKFWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILREVGTRPGGRIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLSENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVTPCRGQDELVGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDKTPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRSIIGDEKYVDYMSSLKRYEDTTLVEDTVL [Source organism chain B]=Kunjin virus [UniProt ID chain C]=P14335 [UniProt boundaries chain C]=25-97 [UniProt coverage chain C]=2% [Name chain C]=Genome polyprotein [UniProt sequence chain C]=MSKKPGGPGKSRAVNMLKRGMPRVLSLTGLKRAMLSLIDGRGPTRFVLALLAFFRFTAIAPTRAVLDRWRSVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAFMIGLIAGVGAVTLSNFQGKVMMTVNATDVTDIITIPPAAGKNLCIVRAMDVGHMCDDTITYECPVLSAGNDPEDIDCWCTKLAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLSNKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSELSTKAACPTMGEAHNDKRADPSFVCKQGVVDRGWGNGCGLFGKGSIDTCAKFACSTKATGRTILKENIKYEVAIFVHGPTTVESHGNYFTQTGAAQAGRFSITPAAPSYTLKLGEYGEVTVDCEPRSGIDTSAYYVMTVGTKTFLVHREWFMDLNLPWSSAESNVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFRFLGTPADTGHGTVVLELQYTGTDGPCKIPISSVASLNDLTPVGRLVTVNPFVSVSTANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTATLKGAQRLAALGDTAWDFGSVGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDISRQELRCGSGVFIHNDVEAWIDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSIVVEKQEGMYKSAPRRLTATTEKLEIGWKAWGKSILFAPELANNTFVIDGPETKECPTQNRAWNNLEVEDFGFGLTSTRMFLRVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRFNDTWKLERAVLGEVKSCTWPETHTLWGDGVLESDLIIPITLAGPRSNHNRRPGYKTQSQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDNGCWYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRYVILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAAFFQMAYYDARQILLWEMPDVLNSLAVAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGFFNPMILAAGLVACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWEGDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKRGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPVPAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVAREHNGNEIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTRVELGEAAAIFMTATPPGTSDPFPESNAPISDLQTEIPDRAWNSGYEWITEYIGKTVWFVPSVKMGNEIALCLQRAGKKVIQLNRKSYETEYPKCKNDDWDFVVTTDISEMGANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRTGRNPSQAGDEYCYGGHTNEDDSNCAHWTEARIMLDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWIDARVYSDHQALKSFKDFASGKRSQIGFIEVLGKMPEHFMGKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGVVLGAATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKSDISGLFGQRIETKENFSIGEFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYITTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTSATLLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQVMLILVSLAALVVNPSVKTVREAGILITAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLVKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFIRYRKEAITEVDRSAAKHARKERNITGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTLRVLEMVEDWLHRGPKEFCVKVLCPYMPKVIEKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKKTWKGPQYEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPKFWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILREVGTRPGGRIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLSENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVTPCRGQDELVGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDKTPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRSIIGDEKYVDYMSSLKRYEDTTLVEDTVL [Source organism chain C]=Kunjin virus [UniProt ID chain D]=P14335 [UniProt boundaries chain D]=25-97 [UniProt coverage chain D]=2% [Name chain D]=Genome polyprotein [UniProt sequence chain D]=MSKKPGGPGKSRAVNMLKRGMPRVLSLTGLKRAMLSLIDGRGPTRFVLALLAFFRFTAIAPTRAVLDRWRSVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAFMIGLIAGVGAVTLSNFQGKVMMTVNATDVTDIITIPPAAGKNLCIVRAMDVGHMCDDTITYECPVLSAGNDPEDIDCWCTKLAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLSNKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSELSTKAACPTMGEAHNDKRADPSFVCKQGVVDRGWGNGCGLFGKGSIDTCAKFACSTKATGRTILKENIKYEVAIFVHGPTTVESHGNYFTQTGAAQAGRFSITPAAPSYTLKLGEYGEVTVDCEPRSGIDTSAYYVMTVGTKTFLVHREWFMDLNLPWSSAESNVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFRFLGTPADTGHGTVVLELQYTGTDGPCKIPISSVASLNDLTPVGRLVTVNPFVSVSTANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTATLKGAQRLAALGDTAWDFGSVGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDISRQELRCGSGVFIHNDVEAWIDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSIVVEKQEGMYKSAPRRLTATTEKLEIGWKAWGKSILFAPELANNTFVIDGPETKECPTQNRAWNNLEVEDFGFGLTSTRMFLRVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRFNDTWKLERAVLGEVKSCTWPETHTLWGDGVLESDLIIPITLAGPRSNHNRRPGYKTQSQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDNGCWYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRYVILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAAFFQMAYYDARQILLWEMPDVLNSLAVAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGFFNPMILAAGLVACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWEGDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKRGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPVPAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVAREHNGNEIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTRVELGEAAAIFMTATPPGTSDPFPESNAPISDLQTEIPDRAWNSGYEWITEYIGKTVWFVPSVKMGNEIALCLQRAGKKVIQLNRKSYETEYPKCKNDDWDFVVTTDISEMGANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRTGRNPSQAGDEYCYGGHTNEDDSNCAHWTEARIMLDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWIDARVYSDHQALKSFKDFASGKRSQIGFIEVLGKMPEHFMGKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGVVLGAATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKSDISGLFGQRIETKENFSIGEFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYITTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTSATLLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQVMLILVSLAALVVNPSVKTVREAGILITAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLVKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFIRYRKEAITEVDRSAAKHARKERNITGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTLRVLEMVEDWLHRGPKEFCVKVLCPYMPKVIEKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKKTWKGPQYEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPKFWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILREVGTRPGGRIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLSENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVTPCRGQDELVGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDKTPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRSIIGDEKYVDYMSSLKRYEDTTLVEDTVL [Source organism chain D]=Kunjin virus [ExpTech]=X-ray [Resolution]=3.20 [Source organism]=Kunjin virus [Accession]=MF4140004 [Entry] [Entry number]=193 [Entry name]=C-terminal domain of the end-binding protein 1 (EB1) [PDB ID]=1wu9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=EB1-like C-terminal motif [Evidence level]=Direct evidence [Evidence text]=EB1 is a stable dimer with a parallel coiled coil and show that dimerization is essential for the formation of its C-terminal domain (EB1-C) (PMID:15616574). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100017,MF7000115,MF7000116,MF7000112,MF7000113 [UniProt ID chain A]=Q15691 [UniProt boundaries chain A]=191-249 [UniProt coverage chain A]=22% [Name chain A]=Microtubule-associated protein RP/EB family member 1 [UniProt sequence chain A]=MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKDYDPVAARQGQETAVAPSLVAPALNKPKKPLTSSSAAPQRPISTQRTAAAPKAGPGVVRKNPGVGNGDDEAAELMQQVNVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q15691 [UniProt boundaries chain B]=191-257 [UniProt coverage chain B]=25% [Name chain B]=Microtubule-associated protein RP/EB family member 1 [UniProt sequence chain B]=MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKDYDPVAARQGQETAVAPSLVAPALNKPKKPLTSSSAAPQRPISTQRTAAAPKAGPGVVRKNPGVGNGDDEAAELMQQVNVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.54 [Source organism]=Homo sapiens [Accession]=MF2100017 [Entry] [Entry number]=194 [Entry name]=SARS-Coronavirus HR2 Domain (post-fusion, hexameric form) [PDB ID]=1zv8 [Chains]=A,B,C,D,E,F [Total number of chains]=6 [Assembly]=Hexamer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:16698550). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Evidence chain C]=N/A [Evidence chain D]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Evidence chain E]=N/A [Evidence chain F]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=P59594 [UniProt boundaries chain A]=901-949 [UniProt coverage chain A]=3% [Name chain A]=Spike glycoprotein [UniProt sequence chain A]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain A]=Severe acute respiratory syndrome coronavirus [UniProt ID chain B]=P59594 [UniProt boundaries chain B]=1154-1180 [UniProt coverage chain B]=2% [Name chain B]=Spike glycoprotein [UniProt sequence chain B]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain B]=Severe acute respiratory syndrome coronavirus [UniProt ID chain C]=P59594 [UniProt boundaries chain C]=902-947 [UniProt coverage chain C]=3% [Name chain C]=Spike glycoprotein [UniProt sequence chain C]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain C]=Severe acute respiratory syndrome coronavirus [UniProt ID chain D]=P59594 [UniProt boundaries chain D]=1154-1182 [UniProt coverage chain D]=2% [Name chain D]=Spike glycoprotein [UniProt sequence chain D]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain D]=Severe acute respiratory syndrome coronavirus [UniProt ID chain E]=P59594 [UniProt boundaries chain E]=901-949 [UniProt coverage chain E]=3% [Name chain E]=Spike glycoprotein [UniProt sequence chain E]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain E]=Severe acute respiratory syndrome coronavirus [UniProt ID chain F]=P59594 [UniProt boundaries chain F]=1153-1182 [UniProt coverage chain F]=2% [Name chain F]=Spike glycoprotein [UniProt sequence chain F]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain F]=Severe acute respiratory syndrome coronavirus [ExpTech]=X-ray [Resolution]=1.94 [Source organism]=Severe acute respiratory syndrome coronavirus [Accession]=MF6140001 [Entry] [Entry number]=196 [Entry name]=H2A-H2B histone dimer (S. cerevisiae), containing histone variants H2A.2 and H2B.1 [PDB ID]=4kud [Chains]=C,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,K,F,B,L,I,J,E,A,G chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain C]=P04912 [UniProt boundaries chain C]=17-119 [UniProt coverage chain C]=78% [Name chain C]=Histone H2A.2 [UniProt sequence chain C]=MSGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQEL [Source organism chain C]=Saccharomyces cerevisiae [UniProt ID chain D]=P02293 [UniProt boundaries chain D]=38-130 [UniProt coverage chain D]=70% [Name chain D]=Histone H2B.1 [UniProt sequence chain D]=MSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA [Source organism chain D]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=3.20 [Source organism]=Saccharomyces cerevisiae [Accession]=MF2210015 [Entry] [Entry number]=197 [Entry name]=Escherichia coli proline utilization A (PutA) DNA-binding domain [PDB ID]=2ay0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=PutA, RHH domain [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:17001030). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2120033,MF7000170,MF7000171 [UniProt ID chain A]=P09546 [UniProt boundaries chain A]=3-45 [UniProt coverage chain A]=3% [Name chain A]=Bifunctional protein PutA [UniProt sequence chain A]=MGTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLENSDTLPELPALLSGAANESDEAPTPAEEPHQPFLDFAEQILPQSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRNQKNASGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNEASLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEESDRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVTAVEKLAQQEGQTGLPHPKIPLPRDLYGHGRDNSAGLDLANEHRLASLSSALLNSALQKWQALPMLEQPVAAGEMSPVINPAEPKDIVGYVREATPREVEQALESAVNNAPIWFATPPAERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRSKGRPVFQAVRENSEDAREWQSGTFVAPTLIELDDFAELQKEVFGPVLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLANRPESALAVTLARQDAKYPVDAQLKAALTQPLNALREWAANRPELQALCTQYGELAQAGTQRLLPGPTGERNTWTLLPRERVLCIADDEQDALTQLAAVLAVGSQVLWPDDALHRQLVKALPSAVSERIQLAKAENITAQPFDAVIFHGDSDQLRALCEAVAARDGTIVSVQGFARGESNILLERLYIERSLSVNTAAAGGNASLMTIG [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P09546 [UniProt boundaries chain B]=3-44 [UniProt coverage chain B]=3% [Name chain B]=Bifunctional protein PutA [UniProt sequence chain B]=MGTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLENSDTLPELPALLSGAANESDEAPTPAEEPHQPFLDFAEQILPQSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRNQKNASGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNEASLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEESDRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVTAVEKLAQQEGQTGLPHPKIPLPRDLYGHGRDNSAGLDLANEHRLASLSSALLNSALQKWQALPMLEQPVAAGEMSPVINPAEPKDIVGYVREATPREVEQALESAVNNAPIWFATPPAERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRSKGRPVFQAVRENSEDAREWQSGTFVAPTLIELDDFAELQKEVFGPVLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLANRPESALAVTLARQDAKYPVDAQLKAALTQPLNALREWAANRPELQALCTQYGELAQAGTQRLLPGPTGERNTWTLLPRERVLCIADDEQDALTQLAAVLAVGSQVLWPDDALHRQLVKALPSAVSERIQLAKAENITAQPFDAVIFHGDSDQLRALCEAVAARDGTIVSVQGFARGESNILLERLYIERSLSVNTAAAGGNASLMTIG [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Escherichia coli [Accession]=MF2120033 [Entry] [Entry number]=198 [Entry name]=SARS-Coronavirus HR2 Domain (post-fusion, tetrameric form) [PDB ID]=1zv7 [Chains]=A,B-2,B,A-2 [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (tetrameric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:16698550). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Evidence chain B-2]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Evidence chain A-2]=The region(s) described in DP02879 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=P59594 [UniProt boundaries chain A]=1150-1187 [UniProt coverage chain A]=3% [Name chain A]=Spike glycoprotein [UniProt sequence chain A]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain A]=Severe acute respiratory syndrome coronavirus [UniProt ID chain B]=P59594 [UniProt boundaries chain B]=1153-1185 [UniProt coverage chain B]=2% [Name chain B]=Spike glycoprotein [UniProt sequence chain B]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain B]=Severe acute respiratory syndrome coronavirus [UniProt ID chain B-2]=P59594 [UniProt boundaries chain B-2]=1153-1185 [UniProt coverage chain B-2]=2% [Name chain B-2]=Spike glycoprotein [UniProt sequence chain B-2]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain B-2]=Severe acute respiratory syndrome coronavirus [UniProt ID chain A-2]=P59594 [UniProt boundaries chain A-2]=1153-1185 [UniProt coverage chain A-2]=2% [Name chain A-2]=Spike glycoprotein [UniProt sequence chain A-2]=MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT [Source organism chain A-2]=Severe acute respiratory syndrome coronavirus [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Severe acute respiratory syndrome coronavirus [Accession]=MF4140005 [Entry] [Entry number]=199 [Entry name]=H2A-H2B histone dimer (human), containing histone variants H2A type 1-A and H2B type 1-J [PDB ID]=5gt0 [Chains]=C,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,B,I,J,E,A,G chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain C]=Q96QV6 [UniProt boundaries chain C]=15-120 [UniProt coverage chain C]=80% [Name chain C]=Histone H2A type 1-A [UniProt sequence chain C]=MSGRGKQGGKARAKSKSRSSRAGLQFPVGRIHRLLRKGNYAERIGAGAPVYLAAVLEYLTAEILELAGNASRDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTESHHHKAQSK [Source organism chain C]=Homo sapiens [UniProt ID chain D]=P62807 [UniProt boundaries chain D]=29-126 [UniProt coverage chain D]=77% [Name chain D]=Histone H2B type 1-C/E/F/G/I [UniProt sequence chain D]=MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.82 [Source organism]=Homo sapiens [Accession]=MF2200015 [Entry] [Entry number]=200 [Entry name]=H2A-H2B histone dimer (human), containing histone variants H2A type 1-D and H2B type 1-A [PDB ID]=5gt3 [Chains]=C,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,B,I,J,E,A,G chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone dimers [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain D]=N/A [Similar structures]=MF2210001,MF2210002,MF2210015,MF2200015,MF2200016,MF2211001,MF2201005,MF2200003,MF2200004,MF2201007 [UniProt ID chain C]=P20671 [UniProt boundaries chain C]=14-119 [UniProt coverage chain C]=81% [Name chain C]=Histone H2A type 1-D [UniProt sequence chain C]=MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK [Source organism chain C]=Homo sapiens [UniProt ID chain D]=Q96A08 [UniProt boundaries chain D]=33-127 [UniProt coverage chain D]=74% [Name chain D]=Histone H2B type 1-A [UniProt sequence chain D]=MPEVSSKGATISKKGFKKAVVKTQKKEGKKRKRTRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYSKRSTISSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK [Source organism chain D]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.91 [Source organism]=Homo sapiens [Accession]=MF2200016 [Entry] [Entry number]=201 [Entry name]=H3-H4 histone dimer (human), containing histone variant H3.3C [PDB ID]=4z5t [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=According to the most probable oligomerization state stored in PDBe H,F,I,J,E,D,G,C chains were not considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=Core histone domain [Evidence level]=Direct evidence [Evidence text]=Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2210005,MF2200005,MF2200007,MF2200006,MF2200008,MF2200017 [UniProt ID chain A]=Q6NXT2 [UniProt boundaries chain A]=38-134 [UniProt coverage chain A]=71% [Name chain A]=Histone H3.3C [UniProt sequence chain A]=MARTKQTARKSTGGKAPRKQLATKAARKSTPSTCGVKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFNTDLRFQSAAVGALQEASEAYLVGLLEDTNLCAIHAKRVTIMPKDIQLARRIRGERA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P62805 [UniProt boundaries chain B]=21-103 [UniProt coverage chain B]=80% [Name chain B]=Histone H4 [UniProt sequence chain B]=MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Homo sapiens [Accession]=MF2200017 [Entry] [Entry number]=202 [Entry name]=Bacillus subtilis antitoxin MazE [PDB ID]=4me7 [Chains]=E,F [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=According to the most probable oligomerization state stored in PDBe B,A,D,C chains were not considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Ribbon-helix-helix protein, copG family [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:24120662). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain E]=N/A [Evidence chain F]=N/A [Similar structures]=MF2120006,MF2120034,MF7000918 [UniProt ID chain E]=P96621 [UniProt boundaries chain E]=6-83 [UniProt coverage chain E]=83% [Name chain E]=Antitoxin EndoAI [UniProt sequence chain E]=MSESSARTEMKISLPENLVAELDGVAMREKRSRNELISQAVRAYVSERTTRHNRDLMRRGYMEMAKINLNISSEAHFAECEAETTVERLVSGG [Source organism chain E]=Bacillus subtilis [UniProt ID chain F]=P96621 [UniProt boundaries chain F]=7-85 [UniProt coverage chain F]=84% [Name chain F]=Antitoxin EndoAI [UniProt sequence chain F]=MSESSARTEMKISLPENLVAELDGVAMREKRSRNELISQAVRAYVSERTTRHNRDLMRRGYMEMAKINLNISSEAHFAECEAETTVERLVSGG [Source organism chain F]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=2.92 [Source organism]=Bacillus subtilis [Accession]=MF2120034 [Entry] [Entry number]=203 [Entry name]=Dimeric cytoplasmic domain of syndecan-4 [PDB ID]=1ejp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=None [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01434 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01434 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=P31431 [UniProt boundaries chain A]=171-198 [UniProt coverage chain A]=14% [Name chain A]=Syndecan-4 [UniProt sequence chain A]=MAPARLFALLLFFVGGVAESIRETEVIDPQDLLEGRYFSGALPDDEDVVGPGQESDDFELSGSGDLDDLEDSMIGPEVVHPLVPLDNHIPERAGSGSQVPTEPKKLEENEVIPKRISPVEESEDVSNKVSMSSTVQGSNIFERTEVLAALIVGGIVGILFAVFLILLLMYRMKKKDEGSYDLGKKPIYKKAPTNEFYA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P31431 [UniProt boundaries chain B]=171-198 [UniProt coverage chain B]=14% [Name chain B]=Syndecan-4 [UniProt sequence chain B]=MAPARLFALLLFFVGGVAESIRETEVIDPQDLLEGRYFSGALPDDEDVVGPGQESDDFELSGSGDLDDLEDSMIGPEVVHPLVPLDNHIPERAGSGSQVPTEPKKLEENEVIPKRISPVEESEDVSNKVSMSSTVQGSNIFERTEVLAALIVGGIVGILFAVFLILLLMYRMKKKDEGSYDLGKKPIYKKAPTNEFYA [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2100018 [Entry] [Entry number]=204 [Entry name]=Yeast elongin C in complex with a von Hippel-Lindau peptide [PDB ID]=1hv2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Both elongin C and the interacting region of VHL are dynamically unstable in isolation and only adopt a stable conformation upon interaction (PMID:11545595). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q03071 [UniProt boundaries chain A]=1-99 [UniProt coverage chain A]=100% [Name chain A]=Elongin-C [UniProt sequence chain A]=MSQDFVTLVSKDDKEYEISRSAAMISPTLKAMIEGPFRESKGRIELKQFDSHILEKAVEYLNYNLKYSGVSEDDDEIPEFEIPTEMSLELLLAADYLSI [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P40338 [UniProt boundaries chain B]=123-137 [UniProt coverage chain B]=8% [Name chain B]=von Hippel-Lindau disease tumor suppressor [UniProt sequence chain B]=MPRKAASPEEAAGEPGPEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPLWLNFDGEPQPYPILPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDYPSVRKDIQRLSQEHLESQHLEEEP [Source organism chain B]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharomyces cerevisiae ;Mus musculus [Accession]=MF2211003 [Entry] [Entry number]=205 [Entry name]=T-cell surface glycoprotein CD4 and proto-oncogene tyrosine-protein kinase LCK fragments [PDB ID]=1q68 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting regions of CD4 and Lck were shown using NMR to undergo cooperative folding as a result of the binding (PMID:14500983). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P01730 [UniProt boundaries chain A]=421-458 [UniProt coverage chain A]=8% [Name chain A]=T-cell surface glycoprotein CD4 [UniProt sequence chain A]=MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P06239 [UniProt boundaries chain B]=7-35 [UniProt coverage chain B]=5% [Name chain B]=Tyrosine-protein kinase Lck [UniProt sequence chain B]=MGCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYQLMRLCWKERPEDRPTFDYLRSVLEDFFTATEGQYQPQP [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF2200018 [Entry] [Entry number]=206 [Entry name]=Archaeal histone hMfB [PDB ID]=1a7w [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) and archaeal histone [Evidence level]=Direct evidence [Evidence text]=Data on the GdmCl-induced unfolding and refolding transitions of the dimer (monitored by stopped-flow far UV CD) fitted to a two-state model (PMID:15313621). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF2130001,MF7000001,MF7000002,MF7000004,MF7000005,MF7000384,MF7000385 [UniProt ID chain A]=P19267 [UniProt boundaries chain A]=1-68 [UniProt coverage chain A]=98% [Name chain A]=DNA-binding protein HMf-2 [UniProt sequence chain A]=MELPIAPIGRIIKDAGAERVSDDARITLAKILEEMGRDIASEAIKLARHAGRKTIKAEDIELAVRRFKK [Source organism chain A]=Methanothermus fervidus [UniProt ID chain A-2]=P19267 [UniProt boundaries chain A-2]=1-68 [UniProt coverage chain A-2]=98% [Name chain A-2]=DNA-binding protein HMf-2 [UniProt sequence chain A-2]=MELPIAPIGRIIKDAGAERVSDDARITLAKILEEMGRDIASEAIKLARHAGRKTIKAEDIELAVRRFKK [Source organism chain A-2]=Methanothermus fervidus [ExpTech]=X-ray [Resolution]=1.55 [Source organism]=Methanothermus fervidus [Accession]=MF7000001 [Entry] [Entry number]=207 [Entry name]=Archaeal histone hMfB, selenomethionine variant [PDB ID]=1b6w [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) and archaeal histone [Evidence level]=Direct evidence [Evidence text]=Data on the GdmCl-induced unfolding and refolding transitions of the dimer (monitored by stopped-flow far UV CD) fitted to a two-state model (PMID:15313621). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF2130001,MF7000001,MF7000002,MF7000004,MF7000005,MF7000384,MF7000385 [UniProt ID chain A]=P19267 [UniProt boundaries chain A]=1-68 [UniProt coverage chain A]=98% [Name chain A]=DNA-binding protein HMf-2 [UniProt sequence chain A]=MELPIAPIGRIIKDAGAERVSDDARITLAKILEEMGRDIASEAIKLARHAGRKTIKAEDIELAVRRFKK [Source organism chain A]=Methanothermus fervidus [UniProt ID chain A-2]=P19267 [UniProt boundaries chain A-2]=1-68 [UniProt coverage chain A-2]=98% [Name chain A-2]=DNA-binding protein HMf-2 [UniProt sequence chain A-2]=MELPIAPIGRIIKDAGAERVSDDARITLAKILEEMGRDIASEAIKLARHAGRKTIKAEDIELAVRRFKK [Source organism chain A-2]=Methanothermus fervidus [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Methanothermus fervidus [Accession]=MF7000002 [Entry] [Entry number]=208 [Entry name]=Archaeal histone hMfA [PDB ID]=1b67 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) and archaeal histone [Evidence level]=Direct evidence [Evidence text]=Data on the GdmCl-induced unfolding and refolding transitions of the dimer (monitored by stopped-flow far UV CD) fitted to a two-state model (PMID:15313621). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2130001,MF7000001,MF7000002,MF7000004,MF7000005,MF7000384,MF7000385 [UniProt ID chain A]=P48781 [UniProt boundaries chain A]=2-69 [UniProt coverage chain A]=98% [Name chain A]=DNA-binding protein HMf-1 [UniProt sequence chain A]=MGELPIAPIGRIIKNAGAERVSDDARIALAKVLEEMGEEIASEAVKLAKHAGRKTIKAEDIELARKMFK [Source organism chain A]=Methanothermus fervidus [UniProt ID chain B]=P48781 [UniProt boundaries chain B]=3-67 [UniProt coverage chain B]=94% [Name chain B]=DNA-binding protein HMf-1 [UniProt sequence chain B]=MGELPIAPIGRIIKNAGAERVSDDARIALAKVLEEMGEEIASEAVKLAKHAGRKTIKAEDIELARKMFK [Source organism chain B]=Methanothermus fervidus [ExpTech]=X-ray [Resolution]=1.48 [Source organism]=Methanothermus fervidus [Accession]=MF7000004 [Entry] [Entry number]=209 [Entry name]=Archaeal histone hMfA [PDB ID]=1hta [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) and archaeal histone [Evidence level]=Direct evidence [Evidence text]=Data on the GdmCl-induced unfolding and refolding transitions of the dimer (monitored by stopped-flow far UV CD) fitted to a two-state model (PMID:15313621). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF2130001,MF7000001,MF7000002,MF7000004,MF7000005,MF7000384,MF7000385 [UniProt ID chain A]=P48781 [UniProt boundaries chain A]=1-68 [UniProt coverage chain A]=98% [Name chain A]=DNA-binding protein HMf-1 [UniProt sequence chain A]=MGELPIAPIGRIIKNAGAERVSDDARIALAKVLEEMGEEIASEAVKLAKHAGRKTIKAEDIELARKMFK [Source organism chain A]=Methanothermus fervidus [UniProt ID chain A-2]=P48781 [UniProt boundaries chain A-2]=1-68 [UniProt coverage chain A-2]=98% [Name chain A-2]=DNA-binding protein HMf-1 [UniProt sequence chain A-2]=MGELPIAPIGRIIKNAGAERVSDDARIALAKVLEEMGEEIASEAVKLAKHAGRKTIKAEDIELARKMFK [Source organism chain A-2]=Methanothermus fervidus [ExpTech]=X-ray [Resolution]=1.55 [Source organism]=Methanothermus fervidus [Accession]=MF7000005 [Entry] [Entry number]=210 [Entry name]=Recombinant histone HPhA (Pyrococcus horikoshii OT3) [PDB ID]=1ku5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histones [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Archeal (hyperthermophilic) core histone dimer (PMID:12527306). Histones form parts of the nucleosome particle by dimerization and subsequent multimerization (PMID:1946434). The dimer contains both histone subunits in a highly intertwined conformation reflecting the possible domain-swapped origins of the structure (PMID:17391511). Accordingly, this dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for H2A-H2B dimers (PMID:15588829) and H3-H4 dimers as well (PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics. E.g. in the case of H3-H4 histones, the dimerization is a complex process with the two monomers first adopting an intermediate state upon encounter and then reaching the classical histone fold through restructurization (PMID:12779337). However, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O74098 [UniProt boundaries chain A]=2-67 [UniProt coverage chain A]=98% [Name chain A]=Archaeal histone A [UniProt sequence chain A]=MGELPIAPVDRLIRKAGAERVSEQAAKVLAEYLEEYAIEIAKKAVEFARHAGRKTVKVEDIKLAIKS [Source organism chain A]=100139 / OT-3) [UniProt ID chain B]=O74098 [UniProt boundaries chain B]=2-67 [UniProt coverage chain B]=98% [Name chain B]=Archaeal histone A [UniProt sequence chain B]=MGELPIAPVDRLIRKAGAERVSEQAAKVLAEYLEEYAIEIAKKAVEFARHAGRKTVKVEDIKLAIKS [Source organism chain B]=100139 / OT-3) [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=100139 / OT-3) [Accession]=MF7000006 [Entry] [Entry number]=211 [Entry name]=c-Myc-Max heterodimeric leucine zipper [PDB ID]=2a93 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=Myc leucine zipper domain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:9680483). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2211002,MF7000007 [UniProt ID chain A]=P01106 [UniProt boundaries chain A]=420-449 [UniProt coverage chain A]=6% [Name chain A]=Myc proto-oncogene protein [UniProt sequence chain A]=MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P28574 [UniProt boundaries chain B]=74-102 [UniProt coverage chain B]=18% [Name chain B]=Protein max [UniProt sequence chain B]=MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGGTISAFDGGSDSSSESEPEEPQSRKKLRMEAS [Source organism chain B]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF7000007 [Entry] [Entry number]=212 [Entry name]=Coiled coil domain of Striatin-3 [PDB ID]=4n6j [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:24550388). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q13033 [UniProt boundaries chain A]=86-130 [UniProt coverage chain A]=5% [Name chain A]=Striatin-3 [UniProt sequence chain A]=MDELAGGGGGGPGMAAPPRQQQGPGGNLGLSPGGNGAAGGGGPPASEGAGPAAGPELSRPQQYTIPGILHYIQHEWARFEMERAHWEVERAELQARIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDLKMPTFESEETKDTEAPTAPQNSQLTWKQGRQLLRQYLQEVGYTDTILDVRSQRVRSLLGLSNSEPNGSVETKNLEQILNGGESPKQKGQEIKRSSGDVLETFNFLENADDSDEDEENDMIEGIPEGKDKHRMNKHKIGNEGLAADLTDDPDTEEALKEFDFLVTAEDGEGAGEARSSGDGTEWDKDDLSPTAEVWDVDQGLISKLKEQYKKERKGKKGVKRANRTKLYDMIADLGDDELPHIPSGIINQSRSASTRMTDHEGARAEEAEPITFPSGGGKSFIMGSDDVLLSVLGLGDLADLTVTNDADYSYDLPANKDAFRKTWNPKYTLRSHFDGVRALAFHPVEPVLVTASEDHTLKLWNLQKTVPAKKSASLDVEPIYTFRAHIGPVLSLAISSNGEQCFSGGIDATIQWWNMPSPSVDPYDTYEPNVLAGTLVGHTDAVWGLAYSGIKNQLLSCSADGTVRLWNPQEKLPCICTYNGDKKHGIPTSVDFIGCDPAHMVTSFNTGSAVIYDLETSQSLVILSSQVDSGLQSNNHINRVVSHPTLPVTITAHEDRHIKFFDNKTGKMIHSMVAHLDAVTSLAVDPNGIYLMSGSHDCSIRLWNLDSKTCVQEITAHRKKLDESIYDVAFHSSKAYIASAGADALAKVFV [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q13033 [UniProt boundaries chain B]=86-130 [UniProt coverage chain B]=5% [Name chain B]=Striatin-3 [UniProt sequence chain B]=MDELAGGGGGGPGMAAPPRQQQGPGGNLGLSPGGNGAAGGGGPPASEGAGPAAGPELSRPQQYTIPGILHYIQHEWARFEMERAHWEVERAELQARIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDLKMPTFESEETKDTEAPTAPQNSQLTWKQGRQLLRQYLQEVGYTDTILDVRSQRVRSLLGLSNSEPNGSVETKNLEQILNGGESPKQKGQEIKRSSGDVLETFNFLENADDSDEDEENDMIEGIPEGKDKHRMNKHKIGNEGLAADLTDDPDTEEALKEFDFLVTAEDGEGAGEARSSGDGTEWDKDDLSPTAEVWDVDQGLISKLKEQYKKERKGKKGVKRANRTKLYDMIADLGDDELPHIPSGIINQSRSASTRMTDHEGARAEEAEPITFPSGGGKSFIMGSDDVLLSVLGLGDLADLTVTNDADYSYDLPANKDAFRKTWNPKYTLRSHFDGVRALAFHPVEPVLVTASEDHTLKLWNLQKTVPAKKSASLDVEPIYTFRAHIGPVLSLAISSNGEQCFSGGIDATIQWWNMPSPSVDPYDTYEPNVLAGTLVGHTDAVWGLAYSGIKNQLLSCSADGTVRLWNPQEKLPCICTYNGDKKHGIPTSVDFIGCDPAHMVTSFNTGSAVIYDLETSQSLVILSSQVDSGLQSNNHINRVVSHPTLPVTITAHEDRHIKFFDNKTGKMIHSMVAHLDAVTSLAVDPNGIYLMSGSHDCSIRLWNLDSKTCVQEITAHRKKLDESIYDVAFHSSKAYIASAGADALAKVFV [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000009 [Entry] [Entry number]=213 [Entry name]=Arc repressor [PDB ID]=1arr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Arc-like DNA binding domain [Evidence level]=Direct evidence [Evidence text]=The Arc repressor protein has been experimentally shown to be a molten globule in monomeric form (PMID:8446590,PMID:7696567). Adopting the proper three dimensional structure is linked to dimerization (PMID:8110744,PMID:10889040). The Mnt repressor shows a high degree of sequential and structural similarity with the Arc and MetJ repressors (PMID:7999761) that both have been shown to adopt a stable structure only via dimerization (PMID:8110744,PMID:1390748). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Similar structures]=MF7000013,MF2140011,MF2140001,MF7000011,MF7000015,MF7000012,MF7000014 [UniProt ID chain A]=P03050 [UniProt boundaries chain A]=1-53 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional repressor arc [UniProt sequence chain A]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain A]=Salmonella phage P22 [UniProt ID chain B]=P03050 [UniProt boundaries chain B]=1-53 [UniProt coverage chain B]=100% [Name chain B]=Transcriptional repressor arc [UniProt sequence chain B]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain B]=Salmonella phage P22 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella phage P22 [Accession]=MF7000011 [Entry] [Entry number]=214 [Entry name]=Arc repressor (MYL mutant) [PDB ID]=1b28 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Arc-like DNA binding domain [Evidence level]=Direct evidence [Evidence text]=The Arc repressor protein has been experimentally shown to be a molten globule in monomeric form (PMID:8446590,PMID:7696567). Adopting the proper three dimensional structure is linked to dimerization (PMID:8110744,PMID:10889040). The Mnt repressor shows a high degree of sequential and structural similarity with the Arc and MetJ repressors (PMID:7999761) that both have been shown to adopt a stable structure only via dimerization (PMID:8110744,PMID:1390748). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Similar structures]=MF7000013,MF2140011,MF2140001,MF7000011,MF7000015,MF7000012,MF7000014 [UniProt ID chain A]=P03050 [UniProt boundaries chain A]=1-53 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional repressor arc [UniProt sequence chain A]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain A]=Salmonella phage P22 [UniProt ID chain B]=P03050 [UniProt boundaries chain B]=1-53 [UniProt coverage chain B]=100% [Name chain B]=Transcriptional repressor arc [UniProt sequence chain B]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain B]=Salmonella phage P22 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella phage P22 [Accession]=MF7000012 [Entry] [Entry number]=215 [Entry name]=Arc repressor (PL8 mutant) [PDB ID]=1myk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Arc-like DNA binding domain [Evidence level]=Direct evidence [Evidence text]=The Arc repressor protein has been experimentally shown to be a molten globule in monomeric form (PMID:8446590,PMID:7696567). Adopting the proper three dimensional structure is linked to dimerization (PMID:8110744,PMID:10889040). The Mnt repressor shows a high degree of sequential and structural similarity with the Arc and MetJ repressors (PMID:7999761) that both have been shown to adopt a stable structure only via dimerization (PMID:8110744,PMID:1390748). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Similar structures]=MF7000013,MF2140011,MF2140001,MF7000011,MF7000015,MF7000012,MF7000014 [UniProt ID chain A]=P03050 [UniProt boundaries chain A]=6-52 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional repressor arc [UniProt sequence chain A]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain A]=Salmonella phage P22 [UniProt ID chain B]=P03050 [UniProt boundaries chain B]=6-50 [UniProt coverage chain B]=84% [Name chain B]=Transcriptional repressor arc [UniProt sequence chain B]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain B]=Salmonella phage P22 [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Salmonella phage P22 [Accession]=MF7000013 [Entry] [Entry number]=216 [Entry name]=Arc repressor (Beta-ribbon replacement mutant) [PDB ID]=1nla [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Arc-like DNA binding domain [Evidence level]=Direct evidence [Evidence text]=The Arc repressor protein has been experimentally shown to be a molten globule in monomeric form (PMID:8446590,PMID:7696567). Adopting the proper three dimensional structure is linked to dimerization (PMID:8110744,PMID:10889040). The Mnt repressor shows a high degree of sequential and structural similarity with the Arc and MetJ repressors (PMID:7999761) that both have been shown to adopt a stable structure only via dimerization (PMID:8110744,PMID:1390748). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Similar structures]=MF7000013,MF2140011,MF2140001,MF7000011,MF7000015,MF7000012,MF7000014 [UniProt ID chain A]=P03050 [UniProt boundaries chain A]=1-53 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional repressor arc [UniProt sequence chain A]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain A]=Salmonella phage P22 [UniProt ID chain B]=P03050 [UniProt boundaries chain B]=1-53 [UniProt coverage chain B]=100% [Name chain B]=Transcriptional repressor arc [UniProt sequence chain B]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain B]=Salmonella phage P22 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella phage P22 [Accession]=MF7000014 [Entry] [Entry number]=217 [Entry name]=Arc repressor (Double "switch" mutant) [PDB ID]=1qtg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Arc-like DNA binding domain [Evidence level]=Direct evidence [Evidence text]=The Arc repressor protein has been experimentally shown to be a molten globule in monomeric form (PMID:8446590,PMID:7696567). Adopting the proper three dimensional structure is linked to dimerization (PMID:8110744,PMID:10889040). The Mnt repressor shows a high degree of sequential and structural similarity with the Arc and MetJ repressors (PMID:7999761) that both have been shown to adopt a stable structure only via dimerization (PMID:8110744,PMID:1390748). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Evidence chain B]=The region(s) described in DP01512 covers 100% of the sequence present in the structure [Similar structures]=MF7000013,MF2140011,MF2140001,MF7000011,MF7000015,MF7000012,MF7000014 [UniProt ID chain A]=P03050 [UniProt boundaries chain A]=1-53 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional repressor arc [UniProt sequence chain A]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain A]=Salmonella phage P22 [UniProt ID chain B]=P03050 [UniProt boundaries chain B]=1-53 [UniProt coverage chain B]=100% [Name chain B]=Transcriptional repressor arc [UniProt sequence chain B]=MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA [Source organism chain B]=Salmonella phage P22 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella phage P22 [Accession]=MF7000015 [Entry] [Entry number]=218 [Entry name]=Nerve growth factor (NGF) [PDB ID]=4xpj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=NGF-like [Sequence domain]=Cystine-knot cytokine/NGF-like [Evidence level]=Direct evidence [Evidence text]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110010,MF2200009,MF2100007,MF2100008,MF2201009,MF2110022,MF2110011,MF7000016,MF7000017 [UniProt ID chain A]=P01139 [UniProt boundaries chain A]=131-235 [UniProt coverage chain A]=43% [Name chain A]=Beta-nerve growth factor [UniProt sequence chain A]=MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG [Source organism chain A]=Mus musculus [UniProt ID chain B]=P01139 [UniProt boundaries chain B]=132-236 [UniProt coverage chain B]=43% [Name chain B]=Beta-nerve growth factor [UniProt sequence chain B]=MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.61 [Source organism]=Mus musculus [Accession]=MF7000016 [Entry] [Entry number]=219 [Entry name]=Nerve growth factor (NGF) [PDB ID]=5lsd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=NGF-like [Sequence domain]=Cystine-knot cytokine/NGF-like [Evidence level]=Direct evidence [Evidence text]=Various dimeric members of neurotrophic factors (including human/mouse nerve growth factor, human brain-derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4/5 (NT-4/5)) have been shown to fold and dimerize at the same time via a two-state process (PMID:8161524). While the members of this family show a significant variance in sequence, they adopt a highly similar structure upon binding and behave almost identically in unfolding/refolding experiments. Thus the two-state folding/binding nature seems to be a hallmark of NGF and closely related proteins. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110010,MF2200009,MF2100007,MF2100008,MF2201009,MF2110022,MF2110011,MF7000016,MF7000017 [UniProt ID chain A]=P01139 [UniProt boundaries chain A]=122-239 [UniProt coverage chain A]=48% [Name chain A]=Beta-nerve growth factor [UniProt sequence chain A]=MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG [Source organism chain A]=Mus musculus [UniProt ID chain B]=P01139 [UniProt boundaries chain B]=122-239 [UniProt coverage chain B]=48% [Name chain B]=Beta-nerve growth factor [UniProt sequence chain B]=MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG [Source organism chain B]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus [Accession]=MF7000017 [Entry] [Entry number]=220 [Entry name]=HU DNA-binding protein [PDB ID]=1b8z [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=IHF-like DNA-binding domain [Sequence domain]=IHF-like DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding from dimers to unfolded monomers proved experimentally (PMID:15066175). High stability of the dimer (PMID:15063721). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000052,MF7000051,MF7000024,MF7000050,MF7000310,MF7000311,MF7000026,MF7000025 [UniProt ID chain A]=P36206 [UniProt boundaries chain A]=1-90 [UniProt coverage chain A]=100% [Name chain A]=DNA-binding protein HU [UniProt sequence chain A]=MTKKELIDRVAKKAGAKKKDVKLILDTILETITEALAKGEKVQIVGFGSFEVRKAAARKGVNPQTRKPITIPERKVPKFKPGKALKEKVK [Source organism chain A]=/ MSB8) [UniProt ID chain B]=P36206 [UniProt boundaries chain B]=1-90 [UniProt coverage chain B]=100% [Name chain B]=DNA-binding protein HU [UniProt sequence chain B]=MTKKELIDRVAKKAGAKKKDVKLILDTILETITEALAKGEKVQIVGFGSFEVRKAAARKGVNPQTRKPITIPERKVPKFKPGKALKEKVK [Source organism chain B]=/ MSB8) [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=/ MSB8) [Accession]=MF7000024 [Entry] [Entry number]=221 [Entry name]=HU DNA-binding protein [PDB ID]=5eka [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=IHF-like DNA-binding domain [Sequence domain]=IHF-like DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding from dimers to unfolded monomers proved experimentally (PMID:15066175). High stability of the dimer (PMID:15063721). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000052,MF7000051,MF7000024,MF7000050,MF7000310,MF7000311,MF7000026,MF7000025 [UniProt ID chain A]=P19436 [UniProt boundaries chain A]=2-97 [UniProt coverage chain A]=98% [Name chain A]=DNA-binding protein HU [UniProt sequence chain A]=MAAKKTVTKADLVDQVAQATGLKKKDVKAMVDALLAKVEEALANGSKVQLTGFGTFEVRKRKARTGVKPGTKEKIKIPATQYPAFKPGKALKDKVKK [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=P19436 [UniProt boundaries chain A-2]=2-97 [UniProt coverage chain A-2]=98% [Name chain A-2]=DNA-binding protein HU [UniProt sequence chain A-2]=MAAKKTVTKADLVDQVAQATGLKKKDVKAMVDALLAKVEEALANGSKVQLTGFGTFEVRKRKARTGVKPGTKEKIKIPATQYPAFKPGKALKDKVKK [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.69 [Source organism]=Thermus thermophilus [Accession]=MF7000025 [Entry] [Entry number]=222 [Entry name]=Histone-like protein dimer (HLP) [PDB ID]=5fbm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=IHF-like DNA-binding domain [Sequence domain]=IHF-like DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding from dimers to unfolded monomers proved experimentally (PMID:15066175). High stability of the dimer (PMID:15063721). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000052,MF7000051,MF7000024,MF7000050,MF7000310,MF7000311,MF7000026,MF7000025 [UniProt ID chain A]=Q9XB21 [UniProt boundaries chain A]=2-91 [UniProt coverage chain A]=98% [Name chain A]=DNA-binding protein HU [UniProt sequence chain A]=MANKQDLIAKVAEATELTKKDSAAAVDAVFSAVSSYLAKGEKVQLIGFGNFEVRERAARKGRNPQTGEEIKIKASKVPAFKAGKALKDAVK [Source organism chain A]=Streptococcus mutans serotype c [UniProt ID chain B]=Q9XB21 [UniProt boundaries chain B]=2-91 [UniProt coverage chain B]=98% [Name chain B]=DNA-binding protein HU [UniProt sequence chain B]=MANKQDLIAKVAEATELTKKDSAAAVDAVFSAVSSYLAKGEKVQLIGFGNFEVRERAARKGRNPQTGEEIKIKASKVPAFKAGKALKDAVK [Source organism chain B]=Streptococcus mutans serotype c [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Streptococcus mutans serotype c [Accession]=MF7000026 [Entry] [Entry number]=223 [Entry name]=hTAF(II))28/hTAF(II)18 heterodimer [PDB ID]=1bh9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=TAF13-TAF11 heterodimer [Evidence level]=Direct evidence [Evidence text]=Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000027,MF7000028 [UniProt ID chain A]=Q15543 [UniProt boundaries chain A]=31-75 [UniProt coverage chain A]=36% [Name chain A]=Transcription initiation factor TFIID subunit 13 [UniProt sequence chain A]=MADEEEDPTFEEENEEIGGGAEGGQGKRKRLFSKELRCMMYGFGDDQNPYTESVDILEDLVIEFITEMTHKAMSIGRQGRVQVEDIVFLIRKDPRKFARVKDLLTMNEELKRARKAFDEANYGS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q15544 [UniProt boundaries chain B]=113-201 [UniProt coverage chain B]=42% [Name chain B]=Transcription initiation factor TFIID subunit 11 [UniProt sequence chain B]=MDDAHESPSDKGGETGESDETAAVPGDPGATDTDGIPEETDGDADVDLKEAAAEEGELESQDVSDLTTVEREDSSLLNPAAKKLKIDTKEKKEKKQKVDEDEIQKMQILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHMREAVRRLKSKGQIPNSKHKKIIFF [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Homo sapiens [Accession]=MF7000027 [Entry] [Entry number]=224 [Entry name]=hTAF(II))28/hTAF(II)18 heterodimer [PDB ID]=1bh8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=TAF13-TAF11 heterodimer [Evidence level]=Direct evidence [Evidence text]=Histone dimerization has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829, PMID:15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000027,MF7000028 [UniProt ID chain A]=Q15543 [UniProt boundaries chain A]=31-75 [UniProt coverage chain A]=36% [Name chain A]=Transcription initiation factor TFIID subunit 13 [UniProt sequence chain A]=MADEEEDPTFEEENEEIGGGAEGGQGKRKRLFSKELRCMMYGFGDDQNPYTESVDILEDLVIEFITEMTHKAMSIGRQGRVQVEDIVFLIRKDPRKFARVKDLLTMNEELKRARKAFDEANYGS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q15544 [UniProt boundaries chain B]=113-201 [UniProt coverage chain B]=42% [Name chain B]=Transcription initiation factor TFIID subunit 11 [UniProt sequence chain B]=MDDAHESPSDKGGETGESDETAAVPGDPGATDTDGIPEETDGDADVDLKEAAAEEGELESQDVSDLTTVEREDSSLLNPAAKKLKIDTKEKKEKKQKVDEDEIQKMQILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHMREAVRRLKSKGQIPNSKHKKIIFF [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Homo sapiens [Accession]=MF7000028 [Entry] [Entry number]=225 [Entry name]=Sensor histidine kinase EnvZ dimerization domain [PDB ID]=1joy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=4-helix bundle [Sequence domain]=His Kinase A (phospho-acceptor) domain [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The dimeric form is very stable, forming a four-helix bundle with a two-fold symmetry along the helical axis. Within the dimer, each subunit folds into a compact structure consisting of antiparallel helices (PMID:10426948). The monomers are most likely not stable on their own. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000029,MF7000030,MF7000031 [UniProt ID chain A]=P0AEJ4 [UniProt boundaries chain A]=223-289 [UniProt coverage chain A]=14% [Name chain A]=Sensor histidine kinase EnvZ [UniProt sequence chain A]=MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIETALYPGSIEVKMHPLSIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPVPVTRAQGTTKEG [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AEJ4 [UniProt boundaries chain B]=223-289 [UniProt coverage chain B]=14% [Name chain B]=Sensor histidine kinase EnvZ [UniProt sequence chain B]=MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIETALYPGSIEVKMHPLSIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPVPVTRAQGTTKEG [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF7000029 [Entry] [Entry number]=226 [Entry name]=Sensor histidine kinase EnvZ dimerization domain [PDB ID]=5b1n [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=4-helix bundle [Sequence domain]=His Kinase A (phospho-acceptor) domain [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The dimeric form is very stable, forming a four-helix bundle with a two-fold symmetry along the helical axis. Within the dimer, each subunit folds into a compact structure consisting of antiparallel helices (PMID:10426948). The monomers are most likely not stable on their own. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000029,MF7000030,MF7000031 [UniProt ID chain A]=P0AEJ4 [UniProt boundaries chain A]=231-289 [UniProt coverage chain A]=13% [Name chain A]=Sensor histidine kinase EnvZ [UniProt sequence chain A]=MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIETALYPGSIEVKMHPLSIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPVPVTRAQGTTKEG [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P0AEJ4 [UniProt boundaries chain A-2]=231-289 [UniProt coverage chain A-2]=13% [Name chain A-2]=Sensor histidine kinase EnvZ [UniProt sequence chain A-2]=MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIETALYPGSIEVKMHPLSIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPVPVTRAQGTTKEG [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.33 [Source organism]=Escherichia coli [Accession]=MF7000030 [Entry] [Entry number]=227 [Entry name]=Sensor histidine kinase EnvZ dimerization domain [PDB ID]=5b1o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=4-helix bundle [Sequence domain]=His Kinase A (phospho-acceptor) domain [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The dimeric form is very stable, forming a four-helix bundle with a two-fold symmetry along the helical axis. Within the dimer, each subunit folds into a compact structure consisting of antiparallel helices (PMID:10426948). The monomers are most likely not stable on their own. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000029,MF7000030,MF7000031 [UniProt ID chain A]=P0AEJ4 [UniProt boundaries chain A]=223-286 [UniProt coverage chain A]=14% [Name chain A]=Sensor histidine kinase EnvZ [UniProt sequence chain A]=MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIETALYPGSIEVKMHPLSIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPVPVTRAQGTTKEG [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AEJ4 [UniProt boundaries chain B]=229-286 [UniProt coverage chain B]=12% [Name chain B]=Sensor histidine kinase EnvZ [UniProt sequence chain B]=MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIETALYPGSIEVKMHPLSIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPVPVTRAQGTTKEG [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Escherichia coli [Accession]=MF7000031 [Entry] [Entry number]=228 [Entry name]=Rat Clara cell 17 kDa protein [PDB ID]=1ccd [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Uteroglobin [Sequence domain]=Uteroglobin family [Evidence level]=Indirect evidence [Evidence text]=Circular dichroism titration for human uteroglobin implies it is in a disordered state (PMID:9081543). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000032,MF7000035,MF7000034,MF7000033 [UniProt ID chain A]=P17559 [UniProt boundaries chain A]=20-96 [UniProt coverage chain A]=80% [Name chain A]=Uteroglobin [UniProt sequence chain A]=MKIAITITVLMLSICCSSASSDICPGFLQVLEALLLGSESNYEAALKPFNPASDLQNAGTQLKRLVDTLPQETRINIVKLTEKILTSPLCEQDLRV [Source organism chain A]=Rattus norvegicus [UniProt ID chain A-2]=P17559 [UniProt boundaries chain A-2]=20-96 [UniProt coverage chain A-2]=80% [Name chain A-2]=Uteroglobin [UniProt sequence chain A-2]=MKIAITITVLMLSICCSSASSDICPGFLQVLEALLLGSESNYEAALKPFNPASDLQNAGTQLKRLVDTLPQETRINIVKLTEKILTSPLCEQDLRV [Source organism chain A-2]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Rattus norvegicus [Accession]=MF7000032 [Entry] [Entry number]=229 [Entry name]=Uteroglobin-PCB complex [PDB ID]=1utr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Uteroglobin [Sequence domain]=Uteroglobin family [Evidence level]=Indirect evidence [Evidence text]=Circular dichroism titration for human uteroglobin implies it is in a disordered state (PMID:9081543). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000032,MF7000035,MF7000034,MF7000033 [UniProt ID chain A]=P17559 [UniProt boundaries chain A]=23-90 [UniProt coverage chain A]=70% [Name chain A]=Uteroglobin [UniProt sequence chain A]=MKIAITITVLMLSICCSSASSDICPGFLQVLEALLLGSESNYEAALKPFNPASDLQNAGTQLKRLVDTLPQETRINIVKLTEKILTSPLCEQDLRV [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P17559 [UniProt boundaries chain B]=23-90 [UniProt coverage chain B]=70% [Name chain B]=Uteroglobin [UniProt sequence chain B]=MKIAITITVLMLSICCSSASSDICPGFLQVLEALLLGSESNYEAALKPFNPASDLQNAGTQLKRLVDTLPQETRINIVKLTEKILTSPLCEQDLRV [Source organism chain B]=Rattus norvegicus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Rattus norvegicus [Accession]=MF7000033 [Entry] [Entry number]=230 [Entry name]=Uteroglobin (oxidized) [PDB ID]=1utg [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Uteroglobin [Sequence domain]=Uteroglobin family [Evidence level]=Indirect evidence [Evidence text]=Circular dichroism titration for human uteroglobin implies it is in a disordered state (PMID:9081543). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000032,MF7000035,MF7000034,MF7000033 [UniProt ID chain A]=P02779 [UniProt boundaries chain A]=22-91 [UniProt coverage chain A]=76% [Name chain A]=Uteroglobin [UniProt sequence chain A]=MKLAITLALVTLALLCSPASAGICPRFAHVIENLLLGTPSSYETSLKEFEPDDTMKDAGMQMKKVLDSLPQTTRENIMKLTEKIVKSPLCM [Source organism chain A]=Oryctolagus cuniculus [UniProt ID chain A-2]=P02779 [UniProt boundaries chain A-2]=22-91 [UniProt coverage chain A-2]=76% [Name chain A-2]=Uteroglobin [UniProt sequence chain A-2]=MKLAITLALVTLALLCSPASAGICPRFAHVIENLLLGTPSSYETSLKEFEPDDTMKDAGMQMKKVLDSLPQTTRENIMKLTEKIVKSPLCM [Source organism chain A-2]=Oryctolagus cuniculus [ExpTech]=X-ray [Resolution]=1.34 [Source organism]=Oryctolagus cuniculus [Accession]=MF7000034 [Entry] [Entry number]=231 [Entry name]=Uteroglobin (oxidized, P21 form) [PDB ID]=2utg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Uteroglobin [Sequence domain]=Uteroglobin family [Evidence level]=Indirect evidence [Evidence text]=Circular dichroism titration for human uteroglobin implies it is in a disordered state (PMID:9081543). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000032,MF7000035,MF7000034,MF7000033 [UniProt ID chain A]=P02779 [UniProt boundaries chain A]=22-91 [UniProt coverage chain A]=76% [Name chain A]=Uteroglobin [UniProt sequence chain A]=MKLAITLALVTLALLCSPASAGICPRFAHVIENLLLGTPSSYETSLKEFEPDDTMKDAGMQMKKVLDSLPQTTRENIMKLTEKIVKSPLCM [Source organism chain A]=Oryctolagus cuniculus [UniProt ID chain B]=P02779 [UniProt boundaries chain B]=22-91 [UniProt coverage chain B]=76% [Name chain B]=Uteroglobin [UniProt sequence chain B]=MKLAITLALVTLALLCSPASAGICPRFAHVIENLLLGTPSSYETSLKEFEPDDTMKDAGMQMKKVLDSLPQTTRENIMKLTEKIVKSPLCM [Source organism chain B]=Oryctolagus cuniculus [ExpTech]=X-ray [Resolution]=1.64 [Source organism]=Oryctolagus cuniculus [Accession]=MF7000035 [Entry] [Entry number]=232 [Entry name]=N-terminal domain of ribosomal protein L7 [PDB ID]=1rqt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=Around one third of the constituting fragments are disordered according to DisProt:DP01650. The dimeric N-terminal domain (residues 1-32) consists of two antiparallel alpha-alpha-hairpins forming a symmetrical four-helical bundle with extensive interface (PMID:14960595). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P0A7K2 [UniProt boundaries chain A]=2-38 [UniProt coverage chain A]=30% [Name chain A]=Large ribosomal subunit protein bL12 [UniProt sequence chain A]=MSITKDQIIEAVAAMSVMDVVELISAMEEKFGVSAAAAVAVAAGPVEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKALEEAGAEVEVK [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0A7K2 [UniProt boundaries chain B]=2-38 [UniProt coverage chain B]=30% [Name chain B]=Large ribosomal subunit protein bL12 [UniProt sequence chain B]=MSITKDQIIEAVAAMSVMDVVELISAMEEKFGVSAAAAVAVAAGPVEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKALEEAGAEVEVK [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF7000036 [Entry] [Entry number]=233 [Entry name]=IFN-γ (bovine) [PDB ID]=1d9c [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=Interferon gamma [Evidence level]=Direct evidence [Evidence text]=Authors describe the dimeric structure as compact, globular and highly intertwined. They sugges that the dimer probably could not be separated without significant disruptions in the tertiary structures of the individual subunits (PMID:1902591). The structural integrity of each domain of interferon gamma (IFN-gamma) is dependent on the intertwining of helices from each peptide chain (PMID:7547951). The dimeric structure is intimately linked, the authors suggest that this type of intertwining between subunits is similar to what has been reported for Trp repressor, which is also a dimer in which the subunits are primarily a helical. (The folding and dimerization of the Trp repressor were shown to be linked by both experimental (PMID:10329154, PMID:2223756, PMID:7578063) and computational studies (PMID:10465773)). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000037,MF7000038,MF7000039 [UniProt ID chain A]=P07353 [UniProt boundaries chain A]=24-144 [UniProt coverage chain A]=72% [Name chain A]=Interferon gamma [UniProt sequence chain A]=MKYTSYFLALLLCGLLGFSGSYGQGQFFREIENLKEYFNASSPDVAKGGPLFSEILKNWKDESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKKLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRRASM [Source organism chain A]=Bos taurus [UniProt ID chain B]=P07353 [UniProt boundaries chain B]=26-144 [UniProt coverage chain B]=71% [Name chain B]=Interferon gamma [UniProt sequence chain B]=MKYTSYFLALLLCGLLGFSGSYGQGQFFREIENLKEYFNASSPDVAKGGPLFSEILKNWKDESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKKLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRRASM [Source organism chain B]=Bos taurus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Bos taurus [Accession]=MF7000037 [Entry] [Entry number]=234 [Entry name]=IFN-γ (bovine) [PDB ID]=1d9g [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=Interferon gamma [Evidence level]=Direct evidence [Evidence text]=Authors describe the dimeric structure as compact, globular and highly intertwined. They sugges that the dimer probably could not be separated without significant disruptions in the tertiary structures of the individual subunits (PMID:1902591). The structural integrity of each domain of interferon gamma (IFN-gamma) is dependent on the intertwining of helices from each peptide chain (PMID:7547951). The dimeric structure is intimately linked, the authors suggest that this type of intertwining between subunits is similar to what has been reported for Trp repressor, which is also a dimer in which the subunits are primarily a helical. (The folding and dimerization of the Trp repressor were shown to be linked by both experimental (PMID:10329154, PMID:2223756, PMID:7578063) and computational studies (PMID:10465773)). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000037,MF7000038,MF7000039 [UniProt ID chain A]=P07353 [UniProt boundaries chain A]=24-144 [UniProt coverage chain A]=72% [Name chain A]=Interferon gamma [UniProt sequence chain A]=MKYTSYFLALLLCGLLGFSGSYGQGQFFREIENLKEYFNASSPDVAKGGPLFSEILKNWKDESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKKLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRRASM [Source organism chain A]=Bos taurus [UniProt ID chain B]=P07353 [UniProt boundaries chain B]=26-144 [UniProt coverage chain B]=71% [Name chain B]=Interferon gamma [UniProt sequence chain B]=MKYTSYFLALLLCGLLGFSGSYGQGQFFREIENLKEYFNASSPDVAKGGPLFSEILKNWKDESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKKLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRRASM [Source organism chain B]=Bos taurus [ExpTech]=X-ray [Resolution]=2.90 [Source organism]=Bos taurus [Accession]=MF7000038 [Entry] [Entry number]=235 [Entry name]=IFN-γ (bovine) [PDB ID]=1rfb [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=Interferon gamma [Evidence level]=Direct evidence [Evidence text]=Authors describe the dimeric structure as compact, globular and highly intertwined. They sugges that the dimer probably could not be separated without significant disruptions in the tertiary structures of the individual subunits (PMID:1902591). The structural integrity of each domain of interferon gamma (IFN-gamma) is dependent on the intertwining of helices from each peptide chain (PMID:7547951). The dimeric structure is intimately linked, the authors suggest that this type of intertwining between subunits is similar to what has been reported for Trp repressor, which is also a dimer in which the subunits are primarily a helical. (The folding and dimerization of the Trp repressor were shown to be linked by both experimental (PMID:10329154, PMID:2223756, PMID:7578063) and computational studies (PMID:10465773)). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000037,MF7000038,MF7000039 [UniProt ID chain A]=P07353 [UniProt boundaries chain A]=24-142 [UniProt coverage chain A]=71% [Name chain A]=Interferon gamma [UniProt sequence chain A]=MKYTSYFLALLLCGLLGFSGSYGQGQFFREIENLKEYFNASSPDVAKGGPLFSEILKNWKDESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKKLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRRASM [Source organism chain A]=Bos taurus [UniProt ID chain B]=P07353 [UniProt boundaries chain B]=24-142 [UniProt coverage chain B]=71% [Name chain B]=Interferon gamma [UniProt sequence chain B]=MKYTSYFLALLLCGLLGFSGSYGQGQFFREIENLKEYFNASSPDVAKGGPLFSEILKNWKDESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKKLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRRASM [Source organism chain B]=Bos taurus [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Bos taurus [Accession]=MF7000039 [Entry] [Entry number]=237 [Entry name]=IFN-γ (grass carp) [PDB ID]=7x45 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The structural integrity of each domain of interferon gamma (IFN-gamma) is dependent on the intertwining of helices from each peptide chain (PMID:7547951). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=C0LEE1 [UniProt boundaries chain A]=31-163 [UniProt coverage chain A]=79% [Name chain A]=Interferon gamma [UniProt sequence chain A]=MDSWLNMMLLCGLLLIASLQTTNAFRFRRSKSEMTHLETNIHSLQEHYKTRGTEWVSKSVFVPHLNQLNSKASCTCQALLLERMLNIYEELFQDMKSEHKEGRKDLDHLMDEVKKLRGNYKEEHKVWKELQEMNSVKVKNGTIRGGALNDFLMVFDRASTEKHKKVQ [Source organism chain A]=Ctenopharyngodon idella [UniProt ID chain B]=C0LEE1 [UniProt boundaries chain B]=32-163 [UniProt coverage chain B]=79% [Name chain B]=Interferon gamma [UniProt sequence chain B]=MDSWLNMMLLCGLLLIASLQTTNAFRFRRSKSEMTHLETNIHSLQEHYKTRGTEWVSKSVFVPHLNQLNSKASCTCQALLLERMLNIYEELFQDMKSEHKEGRKDLDHLMDEVKKLRGNYKEEHKVWKELQEMNSVKVKNGTIRGGALNDFLMVFDRASTEKHKKVQ [Source organism chain B]=Ctenopharyngodon idella [ExpTech]=X-ray [Resolution]=2.26 [Source organism]=Ctenopharyngodon idella [Accession]=MF7000041 [Entry] [Entry number]=239 [Entry name]=IFN-γ (olive flounder) [PDB ID]=6f1e [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The structural integrity of each domain of interferon gamma (IFN-gamma) is dependent on the intertwining of helices from each peptide chain (PMID:7547951). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=B3IXK1 [UniProt boundaries chain A]=25-186 [UniProt coverage chain A]=81% [Name chain A]=Interferon gamma [UniProt sequence chain A]=MMVSTARAVVCLSLCLCVCQVRGSHIPARMNKTIQNLLQHYNISNKDRFNGKPVFPKEPLSGRMETKMLFMGGVLETYEKLIGQMLEQLPNTTPPTAGSREGLNSAAPEVSVRTDLNYILKKVQELRTNRFKEQSKLLQGLHDLGDIKMNNFIIQSKALWELQWMYEEASSLSNNTKMQRRRRRRRRQARKVKTPTRA [Source organism chain A]=Paralichthys olivaceus [UniProt ID chain B]=B3IXK1 [UniProt boundaries chain B]=28-175 [UniProt coverage chain B]=74% [Name chain B]=Interferon gamma [UniProt sequence chain B]=MMVSTARAVVCLSLCLCVCQVRGSHIPARMNKTIQNLLQHYNISNKDRFNGKPVFPKEPLSGRMETKMLFMGGVLETYEKLIGQMLEQLPNTTPPTAGSREGLNSAAPEVSVRTDLNYILKKVQELRTNRFKEQSKLLQGLHDLGDIKMNNFIIQSKALWELQWMYEEASSLSNNTKMQRRRRRRRRQARKVKTPTRA [Source organism chain B]=Paralichthys olivaceus [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Paralichthys olivaceus [Accession]=MF7000043 [Entry] [Entry number]=241 [Entry name]=MinE (Escherichia coli) [PDB ID]=1ev0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=MinE superfamily [Sequence domain]=Septum formation topological specificity factor MinE [Evidence level]=Direct evidence [Evidence text]=MinE is an example of IDP that undergoes disorder to order transition on self-assembly (Review: https://doi.org/10.3389/fphy.2019.00010). Tight dimer, there is beta sheet augmentation between the monomers. There is no evidence for monomeric state even at very low concentrations, only dimeric form could be detected (PMID:31772021). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000045,MF7000048,MF7000049,MF7000835,MF7000836,MF7000046,MF7000047 [UniProt ID chain A]=P0A734 [UniProt boundaries chain A]=31-88 [UniProt coverage chain A]=65% [Name chain A]=Cell division topological specificity factor [UniProt sequence chain A]=MALLDFFLSRKKNTANIAKERLQIIVAERRRSDAEPHYLPQLRKDILEVICKYVQIDPEMVTVQLEQKDGDISILELNVTLPEAEELK [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0A734 [UniProt boundaries chain B]=31-88 [UniProt coverage chain B]=65% [Name chain B]=Cell division topological specificity factor [UniProt sequence chain B]=MALLDFFLSRKKNTANIAKERLQIIVAERRRSDAEPHYLPQLRKDILEVICKYVQIDPEMVTVQLEQKDGDISILELNVTLPEAEELK [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF7000045 [Entry] [Entry number]=242 [Entry name]=Δ30-ngMinE (Neisseria gonorrheae) [PDB ID]=6u6r [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=MinE superfamily [Sequence domain]=Septum formation topological specificity factor MinE [Evidence level]=Direct evidence [Evidence text]=MinE is an example of IDP that undergoes disorder to order transition on self-assembly (Review: https://doi.org/10.3389/fphy.2019.00010). Tight dimer, there is beta sheet augmentation between the monomers. There is no evidence for monomeric state even at very low concentrations, only dimeric form could be detected (PMID:31772021). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000045,MF7000048,MF7000049,MF7000835,MF7000836,MF7000046,MF7000047 [UniProt ID chain A]=P58152 [UniProt boundaries chain A]=38-81 [UniProt coverage chain A]=50% [Name chain A]=Cell division topological specificity factor [UniProt sequence chain A]=MSLIELLFGRKQKTATVARDRLQIIIAQERAQEGQTPDYLPTLRKELMEVLSKYVNVSLDNIRISQEKQDGMDVLELNITLPEQKKV [Source organism chain A]=Neisseria gonorrhoeae [UniProt ID chain B]=P58152 [UniProt boundaries chain B]=38-81 [UniProt coverage chain B]=50% [Name chain B]=Cell division topological specificity factor [UniProt sequence chain B]=MSLIELLFGRKQKTATVARDRLQIIIAQERAQEGQTPDYLPTLRKELMEVLSKYVNVSLDNIRISQEKQDGMDVLELNITLPEQKKV [Source organism chain B]=Neisseria gonorrhoeae [ExpTech]=Solid state NMR [Resolution]=N/A [Source organism]=Neisseria gonorrhoeae [Accession]=MF7000046 [Entry] [Entry number]=243 [Entry name]=I24N-Δ10-ngMinE (Neisseria gonorrheae) [PDB ID]=6u6s [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=MinE superfamily [Sequence domain]=Septum formation topological specificity factor MinE [Evidence level]=Direct evidence [Evidence text]=MinE is an example of IDP that undergoes disorder to order transition on self-assembly (Review: https://doi.org/10.3389/fphy.2019.00010). Tight dimer, there is beta sheet augmentation between the monomers. There is no evidence for monomeric state even at very low concentrations, only dimeric form could be detected (PMID:31772021). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000045,MF7000048,MF7000049,MF7000835,MF7000836,MF7000046,MF7000047 [UniProt ID chain A]=P58152 [UniProt boundaries chain A]=38-81 [UniProt coverage chain A]=50% [Name chain A]=Cell division topological specificity factor [UniProt sequence chain A]=MSLIELLFGRKQKTATVARDRLQIIIAQERAQEGQTPDYLPTLRKELMEVLSKYVNVSLDNIRISQEKQDGMDVLELNITLPEQKKV [Source organism chain A]=Neisseria gonorrhoeae [UniProt ID chain B]=P58152 [UniProt boundaries chain B]=38-81 [UniProt coverage chain B]=50% [Name chain B]=Cell division topological specificity factor [UniProt sequence chain B]=MSLIELLFGRKQKTATVARDRLQIIIAQERAQEGQTPDYLPTLRKELMEVLSKYVNVSLDNIRISQEKQDGMDVLELNITLPEQKKV [Source organism chain B]=Neisseria gonorrhoeae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Neisseria gonorrhoeae [Accession]=MF7000047 [Entry] [Entry number]=244 [Entry name]=MinE (Helicobacter pylori) [PDB ID]=3ku7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=MinE superfamily [Sequence domain]=Septum formation topological specificity factor MinE [Evidence level]=Direct evidence [Evidence text]=MinE is an example of IDP that undergoes disorder to order transition on self-assembly (Review: https://doi.org/10.3389/fphy.2019.00010). Tight dimer, there is beta sheet augmentation between the monomers. There is no evidence for monomeric state even at very low concentrations, only dimeric form could be detected (PMID:31772021). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000045,MF7000048,MF7000049,MF7000835,MF7000836,MF7000046,MF7000047 [UniProt ID chain A]=O25099 [UniProt boundaries chain A]=13-76 [UniProt coverage chain A]=83% [Name chain A]=Cell division topological specificity factor [UniProt sequence chain A]=MSLFDFFKNKGSAATATDRLKLILAKERTLNLPYMEEMRKEIIAVIQKYTKSSDIHFKTLDSNQSVETIEVEIILPR [Source organism chain A]=Helicobacter pylori [UniProt ID chain B]=O25099 [UniProt boundaries chain B]=16-77 [UniProt coverage chain B]=80% [Name chain B]=Cell division topological specificity factor [UniProt sequence chain B]=MSLFDFFKNKGSAATATDRLKLILAKERTLNLPYMEEMRKEIIAVIQKYTKSSDIHFKTLDSNQSVETIEVEIILPR [Source organism chain B]=Helicobacter pylori [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Helicobacter pylori [Accession]=MF7000048 [Entry] [Entry number]=245 [Entry name]=MinE (Helicobacter pylori) [PDB ID]=3mcd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=MinE superfamily [Sequence domain]=Septum formation topological specificity factor MinE [Evidence level]=Direct evidence [Evidence text]=MinE is an example of IDP that undergoes disorder to order transition on self-assembly (Review: https://doi.org/10.3389/fphy.2019.00010). Tight dimer, there is beta sheet augmentation between the monomers. There is no evidence for monomeric state even at very low concentrations, only dimeric form could be detected (PMID:31772021). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000045,MF7000048,MF7000049,MF7000835,MF7000836,MF7000046,MF7000047 [UniProt ID chain A]=O25099 [UniProt boundaries chain A]=16-76 [UniProt coverage chain A]=79% [Name chain A]=Cell division topological specificity factor [UniProt sequence chain A]=MSLFDFFKNKGSAATATDRLKLILAKERTLNLPYMEEMRKEIIAVIQKYTKSSDIHFKTLDSNQSVETIEVEIILPR [Source organism chain A]=Helicobacter pylori [UniProt ID chain B]=O25099 [UniProt boundaries chain B]=16-76 [UniProt coverage chain B]=79% [Name chain B]=Cell division topological specificity factor [UniProt sequence chain B]=MSLFDFFKNKGSAATATDRLKLILAKERTLNLPYMEEMRKEIIAVIQKYTKSSDIHFKTLDSNQSVETIEVEIILPR [Source organism chain B]=Helicobacter pylori [ExpTech]=X-ray [Resolution]=3.20 [Source organism]=Helicobacter pylori [Accession]=MF7000049 [Entry] [Entry number]=246 [Entry name]=Transcription Factor 1 (mutant) [PDB ID]=1exe [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=IHF-like DNA-binding domain [Sequence domain]=IHF-like DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding from dimers to unfolded monomers proved experimentally (PMID:15066175). High stability of the dimer (PMID:15063721). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000052,MF7000051,MF7000024,MF7000050,MF7000310,MF7000311,MF7000026,MF7000025 [UniProt ID chain A]=P04445 [UniProt boundaries chain A]=1-99 [UniProt coverage chain A]=100% [Name chain A]=Transcription factor 1 [UniProt sequence chain A]=MNKTELIKAIAQDTELTQVSVSKMLASFEKITTETVAKGDKVQLTGFLNIKPVARQARKGFNPQTQEALEIAPSVGVSVKPGESLKKAAEGLKYEDFAK [Source organism chain A]=Bacillus phage SP01 [UniProt ID chain B]=P04445 [UniProt boundaries chain B]=1-99 [UniProt coverage chain B]=100% [Name chain B]=Transcription factor 1 [UniProt sequence chain B]=MNKTELIKAIAQDTELTQVSVSKMLASFEKITTETVAKGDKVQLTGFLNIKPVARQARKGFNPQTQEALEIAPSVGVSVKPGESLKKAAEGLKYEDFAK [Source organism chain B]=Bacillus phage SP01 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus phage SP01 [Accession]=MF7000050 [Entry] [Entry number]=247 [Entry name]=Transcription Factor 1 [PDB ID]=1wtu [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=IHF-like DNA-binding domain [Sequence domain]=IHF-like DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding from dimers to unfolded monomers proved experimentally (PMID:15066175). High stability of the dimer (PMID:15063721). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000052,MF7000051,MF7000024,MF7000050,MF7000310,MF7000311,MF7000026,MF7000025 [UniProt ID chain A]=P04445 [UniProt boundaries chain A]=1-99 [UniProt coverage chain A]=100% [Name chain A]=Transcription factor 1 [UniProt sequence chain A]=MNKTELIKAIAQDTELTQVSVSKMLASFEKITTETVAKGDKVQLTGFLNIKPVARQARKGFNPQTQEALEIAPSVGVSVKPGESLKKAAEGLKYEDFAK [Source organism chain A]=Bacillus phage SP01 [UniProt ID chain B]=P04445 [UniProt boundaries chain B]=1-99 [UniProt coverage chain B]=100% [Name chain B]=Transcription factor 1 [UniProt sequence chain B]=MNKTELIKAIAQDTELTQVSVSKMLASFEKITTETVAKGDKVQLTGFLNIKPVARQARKGFNPQTQEALEIAPSVGVSVKPGESLKKAAEGLKYEDFAK [Source organism chain B]=Bacillus phage SP01 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus phage SP01 [Accession]=MF7000051 [Entry] [Entry number]=248 [Entry name]=HU protein [PDB ID]=1hue [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=IHF-like DNA-binding domain [Sequence domain]=IHF-like DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding from dimers to unfolded monomers proved experimentally (PMID:15066175). High stability of the dimer (PMID:15063721). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000052,MF7000051,MF7000024,MF7000050,MF7000310,MF7000311,MF7000026,MF7000025 [UniProt ID chain A]=P0A3H0 [UniProt boundaries chain A]=1-90 [UniProt coverage chain A]=100% [Name chain A]=DNA-binding protein HU [UniProt sequence chain A]=MNKTELINAVAETSGLSKKDATKAVDAVFDSITEALRKGDKVQLIGFGNFEVRERAARKGRNPQTGEEMEIPASKVPAFKPGKALKDAVK [Source organism chain A]=Geobacillus stearothermophilus [UniProt ID chain B]=P0A3H0 [UniProt boundaries chain B]=1-90 [UniProt coverage chain B]=100% [Name chain B]=DNA-binding protein HU [UniProt sequence chain B]=MNKTELINAVAETSGLSKKDATKAVDAVFDSITEALRKGDKVQLIGFGNFEVRERAARKGRNPQTGEEMEIPASKVPAFKPGKALKDAVK [Source organism chain B]=Geobacillus stearothermophilus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Geobacillus stearothermophilus [Accession]=MF7000052 [Entry] [Entry number]=249 [Entry name]=PLGF-1 [PDB ID]=1fzv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=PDGF/VEGF-like [Sequence domain]=Cystine-knot cytokine/PDGF/VEGF-like [Evidence level]=Direct evidence [Evidence text]=Cystine-knot motif growth factors show two-state unfolding from dimers to unfolded monomers (PMID:34689403). The hydrophobic core is formed by both monomers, there is a large, hydrophobic interafce and the homodimer is covalently linked by two interchain disulfide bonds (PMID:16616187). There is a cystine-knot motif, positioned symmetrically, at the opposite end of each monomer (PMID:11069911). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000053,MF7000054,MF7000055,MF7000885,MF7000886 [UniProt ID chain A]=P49763 [UniProt boundaries chain A]=35-134 [UniProt coverage chain A]=45% [Name chain A]=Placenta growth factor [UniProt sequence chain A]=MPVMRLFPCFLQLLAGLALPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCRALERLVDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSGDRPSYVELTFSQHVRCECRHSPGRQSPDMPGDFRADAPSFLPPRRSLPMLFRMEWGCALTGSQSAVWPSSPVPEEIPRMHPGRNGKKQQRKPLREKMKPERCGDAVPRR [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P49763 [UniProt boundaries chain B]=35-134 [UniProt coverage chain B]=45% [Name chain B]=Placenta growth factor [UniProt sequence chain B]=MPVMRLFPCFLQLLAGLALPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCRALERLVDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSGDRPSYVELTFSQHVRCECRHSPGRQSPDMPGDFRADAPSFLPPRRSLPMLFRMEWGCALTGSQSAVWPSSPVPEEIPRMHPGRNGKKQQRKPLREKMKPERCGDAVPRR [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000053 [Entry] [Entry number]=250 [Entry name]=Vammin VEGF-F (Vipera venom) [PDB ID]=1wq8 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=PDGF/VEGF-like [Sequence domain]=Cystine-knot cytokine/PDGF/VEGF-like [Evidence level]=Direct evidence [Evidence text]=Cystine-knot motif growth factors show two-state unfolding from dimers to unfolded monomers (PMID:34689403). The hydrophobic core is formed by both monomers, there is a large, hydrophobic interafce and the homodimer is covalently linked by two interchain disulfide bonds (PMID:16616187). There is a cystine-knot motif, positioned symmetrically, at the opposite end of each monomer (PMID:11069911). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000053,MF7000054,MF7000055,MF7000885,MF7000886 [UniProt ID chain A]=P67863 [UniProt boundaries chain A]=25-124 [UniProt coverage chain A]=68% [Name chain A]=Snake venom vascular endothelial growth factor toxin vammin [UniProt sequence chain A]=MAAYLLAVAILFCIQGWPSGTVQGQVRPFLEVHERSACQARETLVPILQEYPDEISDIFRPSCVAVLRCSGCCTDESLKCTPVGKHTVDLQIMRVNPRTQSSKMEVMKFTEHTACECRPRRKQGEPDGPKEKPRRGGVRARFPFV [Source organism chain A]=Vipera ammodytes ammodytes [UniProt ID chain A-2]=P67863 [UniProt boundaries chain A-2]=25-124 [UniProt coverage chain A-2]=68% [Name chain A-2]=Snake venom vascular endothelial growth factor toxin vammin [UniProt sequence chain A-2]=MAAYLLAVAILFCIQGWPSGTVQGQVRPFLEVHERSACQARETLVPILQEYPDEISDIFRPSCVAVLRCSGCCTDESLKCTPVGKHTVDLQIMRVNPRTQSSKMEVMKFTEHTACECRPRRKQGEPDGPKEKPRRGGVRARFPFV [Source organism chain A-2]=Vipera ammodytes ammodytes [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Vipera ammodytes ammodytes [Accession]=MF7000054 [Entry] [Entry number]=251 [Entry name]=VR-1 VEGF-F (Vipera venom) [PDB ID]=1wq9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=PDGF/VEGF-like [Sequence domain]=Cystine-knot cytokine/PDGF/VEGF-like [Evidence level]=Direct evidence [Evidence text]=Cystine-knot motif growth factors show two-state unfolding from dimers to unfolded monomers (PMID:34689403). The hydrophobic core is formed by both monomers, there is a large, hydrophobic interafce and the homodimer is covalently linked by two interchain disulfide bonds (PMID:16616187). There is a cystine-knot motif, positioned symmetrically, at the opposite end of each monomer (PMID:11069911). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000053,MF7000054,MF7000055,MF7000885,MF7000886 [UniProt ID chain A]=P67861 [UniProt boundaries chain A]=25-119 [UniProt coverage chain A]=65% [Name chain A]=Snake venom vascular endothelial growth factor toxin VR-1 [UniProt sequence chain A]=MAAYLLAVAILFCIQGWPSGTVQGQVRPFLDVYERSACQTRETLVSILQEHPDEISDIFRPSCVAVLRCSGCCTDESMKCTPVGKHTADIQIMRMNPRTHSSKMEVMKFMEHTACECRPRWKQGEPEGPKEPRRGGVRAKFPFD [Source organism chain A]=Daboia russelii [UniProt ID chain B]=P67861 [UniProt boundaries chain B]=25-119 [UniProt coverage chain B]=65% [Name chain B]=Snake venom vascular endothelial growth factor toxin VR-1 [UniProt sequence chain B]=MAAYLLAVAILFCIQGWPSGTVQGQVRPFLDVYERSACQTRETLVSILQEHPDEISDIFRPSCVAVLRCSGCCTDESMKCTPVGKHTADIQIMRMNPRTHSSKMEVMKFMEHTACECRPRWKQGEPEGPKEPRRGGVRAKFPFD [Source organism chain B]=Daboia russelii [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Daboia russelii [Accession]=MF7000055 [Entry] [Entry number]=252 [Entry name]=ADP-ribose pyrophosphatase [PDB ID]=1g0s [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q93K97 [UniProt boundaries chain A]=1-209 [UniProt coverage chain A]=100% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIHGLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNEWA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=Q93K97 [UniProt boundaries chain B]=8-209 [UniProt coverage chain B]=96% [Name chain B]=ADP-ribose pyrophosphatase [UniProt sequence chain B]=MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIHGLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNEWA [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Escherichia coli [Accession]=MF7000056 [Entry] [Entry number]=253 [Entry name]=ADP-ribose pyrophosphatase/ADP-ribose complex [PDB ID]=1g9q [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q93K97 [UniProt boundaries chain A]=1-209 [UniProt coverage chain A]=100% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIHGLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNEWA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=Q93K97 [UniProt boundaries chain B]=8-209 [UniProt coverage chain B]=96% [Name chain B]=ADP-ribose pyrophosphatase [UniProt sequence chain B]=MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIHGLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNEWA [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Escherichia coli [Accession]=MF7000057 [Entry] [Entry number]=254 [Entry name]=ADP-ribose pyrophosphatase/GD+3 complex [PDB ID]=1ga7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q93K97 [UniProt boundaries chain A]=1-209 [UniProt coverage chain A]=100% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIHGLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNEWA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=Q93K97 [UniProt boundaries chain B]=8-209 [UniProt coverage chain B]=96% [Name chain B]=ADP-ribose pyrophosphatase [UniProt sequence chain B]=MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIHGLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNEWA [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.71 [Source organism]=Escherichia coli [Accession]=MF7000058 [Entry] [Entry number]=255 [Entry name]=ADPR-ase/AMPCPR complex [PDB ID]=1khz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q93K97 [UniProt boundaries chain A]=1-209 [UniProt coverage chain A]=100% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIHGLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNEWA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=Q93K97 [UniProt boundaries chain B]=8-209 [UniProt coverage chain B]=96% [Name chain B]=ADP-ribose pyrophosphatase [UniProt sequence chain B]=MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIHGLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNEWA [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.04 [Source organism]=Escherichia coli [Accession]=MF7000059 [Entry] [Entry number]=256 [Entry name]=FlhD [PDB ID]=1g8e [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=The 83-116 region described in DisProt entry DisProt:DP02700 covers 37% of the residues present in the structure. The FlhD protein is dimeric. The dimer is tightly coupled, with an intimate contact surface, implying that the dimer does not easily dissociate (PMID:11169099). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P0A8S9 [UniProt boundaries chain A]=1-98 [UniProt coverage chain A]=84% [Name chain A]=Flagellar transcriptional regulator FlhD [UniProt sequence chain A]=MHTSELLKHIYDINLSYLLLAQRLIVQDKASAMFRLGINEEMATTLAALTLPQMVKLAETNQLVCHFRFDSHQTITQLTQDSRVDDLQQIHTGIMLSTRLLNDVNQPEEALRKKRA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0A8S9 [UniProt boundaries chain B]=3-82 [UniProt coverage chain B]=68% [Name chain B]=Flagellar transcriptional regulator FlhD [UniProt sequence chain B]=MHTSELLKHIYDINLSYLLLAQRLIVQDKASAMFRLGINEEMATTLAALTLPQMVKLAETNQLVCHFRFDSHQTITQLTQDSRVDDLQQIHTGIMLSTRLLNDVNQPEEALRKKRA [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Escherichia coli [Accession]=MF7000060 [Entry] [Entry number]=257 [Entry name]=YdcE [PDB ID]=1gyj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Tautomerase enzyme [Evidence level]=Direct evidence [Evidence text]=Two-state unfolding from dimers to unfolded monomers proved experimentally (PMID:11914096). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000061,MF7000062,MF7000063 [UniProt ID chain A]=P31992 [UniProt boundaries chain A]=2-77 [UniProt coverage chain A]=98% [Name chain A]=Tautomerase PptA [UniProt sequence chain A]=MPHIDIKCFPRELDEQQKAALAADITDVIIRHLNSKDSSISIALQQIQPESWQAIWDAEIAPQMEALIKKPGYSMNA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P31992 [UniProt boundaries chain B]=2-77 [UniProt coverage chain B]=98% [Name chain B]=Tautomerase PptA [UniProt sequence chain B]=MPHIDIKCFPRELDEQQKAALAADITDVIIRHLNSKDSSISIALQQIQPESWQAIWDAEIAPQMEALIKKPGYSMNA [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Escherichia coli [Accession]=MF7000061 [Entry] [Entry number]=258 [Entry name]=YdcE [PDB ID]=1gyx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Tautomerase enzyme [Evidence level]=Direct evidence [Evidence text]=Two-state unfolding from dimers to unfolded monomers proved experimentally (PMID:11914096). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000061,MF7000062,MF7000063 [UniProt ID chain A]=P31992 [UniProt boundaries chain A]=2-77 [UniProt coverage chain A]=98% [Name chain A]=Tautomerase PptA [UniProt sequence chain A]=MPHIDIKCFPRELDEQQKAALAADITDVIIRHLNSKDSSISIALQQIQPESWQAIWDAEIAPQMEALIKKPGYSMNA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P31992 [UniProt boundaries chain B]=2-77 [UniProt coverage chain B]=98% [Name chain B]=Tautomerase PptA [UniProt sequence chain B]=MPHIDIKCFPRELDEQQKAALAADITDVIIRHLNSKDSSISIALQQIQPESWQAIWDAEIAPQMEALIKKPGYSMNA [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=Escherichia coli [Accession]=MF7000062 [Entry] [Entry number]=259 [Entry name]=YdcE [PDB ID]=1gyy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Tautomerase enzyme [Evidence level]=Direct evidence [Evidence text]=Two-state unfolding from dimers to unfolded monomers proved experimentally (PMID:11914096). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000061,MF7000062,MF7000063 [UniProt ID chain A]=P31992 [UniProt boundaries chain A]=2-77 [UniProt coverage chain A]=98% [Name chain A]=Tautomerase PptA [UniProt sequence chain A]=MPHIDIKCFPRELDEQQKAALAADITDVIIRHLNSKDSSISIALQQIQPESWQAIWDAEIAPQMEALIKKPGYSMNA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P31992 [UniProt boundaries chain B]=2-77 [UniProt coverage chain B]=98% [Name chain B]=Tautomerase PptA [UniProt sequence chain B]=MPHIDIKCFPRELDEQQKAALAADITDVIIRHLNSKDSSISIALQQIQPESWQAIWDAEIAPQMEALIKKPGYSMNA [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=Escherichia coli [Accession]=MF7000063 [Entry] [Entry number]=260 [Entry name]=Coiled coil domain from Bovine IF1 [PDB ID]=1hf9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:11327770). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P01096 [UniProt boundaries chain A]=69-109 [UniProt coverage chain A]=37% [Name chain A]=ATPase inhibitor, mitochondrial [UniProt sequence chain A]=MAATALAARTRQAVWSVWAMQGRGFGSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEIERLQKEIERHKQSIKKLKQSEDDD [Source organism chain A]=Bos taurus [UniProt ID chain B]=P01096 [UniProt boundaries chain B]=69-109 [UniProt coverage chain B]=37% [Name chain B]=ATPase inhibitor, mitochondrial [UniProt sequence chain B]=MAATALAARTRQAVWSVWAMQGRGFGSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEIERLQKEIERHKQSIKKLKQSEDDD [Source organism chain B]=Bos taurus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bos taurus [Accession]=MF7000064 [Entry] [Entry number]=261 [Entry name]=IL-10 [PDB ID]=1ilk [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=Interleukin 10 [Evidence level]=Direct evidence [Evidence text]=The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain (PMID:7547951). One monomer of IL-10 consists of six helices, A-F, from which E and F are switched between the monomers and contribute to the formation of the compact six-helix bundle-like domains of the IL-10 dimer. An extended hydrophobic core is located inside of each domain, to which both chains contribute (PMID:8897595). The monomeric form of IL-10 could only be created if the Cys62–Cys114 disulfide bond were to be reduced, or if the structure were otherwise seriously distorted (PMID:8590020). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000066,MF7000065,MF7000068,MF7000069,MF7000067 [UniProt ID chain A]=P22301 [UniProt boundaries chain A]=28-178 [UniProt coverage chain A]=84% [Name chain A]=Interleukin-10 [UniProt sequence chain A]=MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P22301 [UniProt boundaries chain A-2]=28-178 [UniProt coverage chain A-2]=84% [Name chain A-2]=Interleukin-10 [UniProt sequence chain A-2]=MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF7000065 [Entry] [Entry number]=262 [Entry name]=IL-10 homodimer [PDB ID]=1inr [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=Interleukin 10 [Evidence level]=Direct evidence [Evidence text]=The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain (PMID:7547951). One monomer of IL-10 consists of six helices, A-F, from which E and F are switched between the monomers and contribute to the formation of the compact six-helix bundle-like domains of the IL-10 dimer. An extended hydrophobic core is located inside of each domain, to which both chains contribute (PMID:8897595). The monomeric form of IL-10 could only be created if the Cys62–Cys114 disulfide bond were to be reduced, or if the structure were otherwise seriously distorted (PMID:8590020). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000066,MF7000065,MF7000068,MF7000069,MF7000067 [UniProt ID chain A]=P22301 [UniProt boundaries chain A]=36-177 [UniProt coverage chain A]=79% [Name chain A]=Interleukin-10 [UniProt sequence chain A]=MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P22301 [UniProt boundaries chain A-2]=36-177 [UniProt coverage chain A-2]=79% [Name chain A-2]=Interleukin-10 [UniProt sequence chain A-2]=MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000066 [Entry] [Entry number]=263 [Entry name]=IL-10 [PDB ID]=2h24 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=Interleukin 10 [Evidence level]=Direct evidence [Evidence text]=The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain (PMID:7547951). One monomer of IL-10 consists of six helices, A-F, from which E and F are switched between the monomers and contribute to the formation of the compact six-helix bundle-like domains of the IL-10 dimer. An extended hydrophobic core is located inside of each domain, to which both chains contribute (PMID:8897595). The monomeric form of IL-10 could only be created if the Cys62–Cys114 disulfide bond were to be reduced, or if the structure were otherwise seriously distorted (PMID:8590020). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000066,MF7000065,MF7000068,MF7000069,MF7000067 [UniProt ID chain A]=P22301 [UniProt boundaries chain A]=36-177 [UniProt coverage chain A]=79% [Name chain A]=Interleukin-10 [UniProt sequence chain A]=MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P22301 [UniProt boundaries chain A-2]=36-177 [UniProt coverage chain A-2]=79% [Name chain A-2]=Interleukin-10 [UniProt sequence chain A-2]=MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000067 [Entry] [Entry number]=264 [Entry name]=IL-10 [PDB ID]=2ilk [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=Interleukin 10 [Evidence level]=Direct evidence [Evidence text]=The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain (PMID:7547951). One monomer of IL-10 consists of six helices, A-F, from which E and F are switched between the monomers and contribute to the formation of the compact six-helix bundle-like domains of the IL-10 dimer. An extended hydrophobic core is located inside of each domain, to which both chains contribute (PMID:8897595). The monomeric form of IL-10 could only be created if the Cys62–Cys114 disulfide bond were to be reduced, or if the structure were otherwise seriously distorted (PMID:8590020). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000066,MF7000065,MF7000068,MF7000069,MF7000067 [UniProt ID chain A]=P22301 [UniProt boundaries chain A]=24-178 [UniProt coverage chain A]=87% [Name chain A]=Interleukin-10 [UniProt sequence chain A]=MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P22301 [UniProt boundaries chain A-2]=24-178 [UniProt coverage chain A-2]=87% [Name chain A-2]=Interleukin-10 [UniProt sequence chain A-2]=MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Homo sapiens [Accession]=MF7000068 [Entry] [Entry number]=265 [Entry name]=IL-10 (Human gammaherpesvirus 4) [PDB ID]=1vlk [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=Interleukin 10 [Evidence level]=Direct evidence [Evidence text]=The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain (PMID:7547951). One monomer of IL-10 consists of six helices, A-F, from which E and F are switched between the monomers and contribute to the formation of the compact six-helix bundle-like domains of the IL-10 dimer. An extended hydrophobic core is located inside of each domain, to which both chains contribute (PMID:8897595). The monomeric form of IL-10 could only be created if the Cys62–Cys114 disulfide bond were to be reduced, or if the structure were otherwise seriously distorted (PMID:8590020). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000066,MF7000065,MF7000068,MF7000069,MF7000067 [UniProt ID chain A]=P03180 [UniProt boundaries chain A]=27-168 [UniProt coverage chain A]=83% [Name chain A]=Viral interleukin-10 homolog [UniProt sequence chain A]=MERRLVVTLQCLVLLYLAPECGGTDQCDNFPQMLRDLRDAFSRVKTFFQTKDEVDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPEAKDHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQIKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTIKAR [Source organism chain A]=Epstein-Barr virus [UniProt ID chain A-2]=P03180 [UniProt boundaries chain A-2]=27-168 [UniProt coverage chain A-2]=83% [Name chain A-2]=Viral interleukin-10 homolog [UniProt sequence chain A-2]=MERRLVVTLQCLVLLYLAPECGGTDQCDNFPQMLRDLRDAFSRVKTFFQTKDEVDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPEAKDHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQIKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTIKAR [Source organism chain A-2]=Epstein-Barr virus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Epstein-Barr virus [Accession]=MF7000069 [Entry] [Entry number]=266 [Entry name]=Sulerythrin [PDB ID]=1j30 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=3-143 [UniProt coverage chain A]=97% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=3-139 [UniProt coverage chain B]=95% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.70 [Source organism]= [Accession]=MF7000070 [Entry] [Entry number]=267 [Entry name]=Sulerythrin (apo-state) [PDB ID]=7o89 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=3-143 [UniProt coverage chain A]=97% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain A-2]=F9VPE5 [UniProt boundaries chain A-2]=3-143 [UniProt coverage chain A-2]=97% [Name chain A-2]=Sulerythrin [UniProt sequence chain A-2]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A-2]= [ExpTech]=X-ray [Resolution]=1.16 [Source organism]= [Accession]=MF7000071 [Entry] [Entry number]=268 [Entry name]=Sulerythrin (oxidized) [PDB ID]=7o8d [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=1-143 [UniProt coverage chain A]=99% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=1-142 [UniProt coverage chain B]=98% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.12 [Source organism]= [Accession]=MF7000072 [Entry] [Entry number]=269 [Entry name]=Sulerythrin (mono-Fe) [PDB ID]=7o90 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=3-143 [UniProt coverage chain A]=97% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=2-142 [UniProt coverage chain B]=97% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.49 [Source organism]= [Accession]=MF7000073 [Entry] [Entry number]=270 [Entry name]=Sulerythrin (diMn) [PDB ID]=7o93 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=1-144 [UniProt coverage chain A]=100% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=1-142 [UniProt coverage chain B]=98% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.17 [Source organism]= [Accession]=MF7000074 [Entry] [Entry number]=271 [Entry name]=Sulerythrin (diMn) [PDB ID]=7o99 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=3-142 [UniProt coverage chain A]=97% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=1-143 [UniProt coverage chain B]=99% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.24 [Source organism]= [Accession]=MF7000075 [Entry] [Entry number]=272 [Entry name]=Sulerythrin (diNi) [PDB ID]=7o9c [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=2-143 [UniProt coverage chain A]=98% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=1-143 [UniProt coverage chain B]=99% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.60 [Source organism]= [Accession]=MF7000076 [Entry] [Entry number]=273 [Entry name]=Sulerythrin (diCo) [PDB ID]=7o9d [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=3-143 [UniProt coverage chain A]=97% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=1-141 [UniProt coverage chain B]=97% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.28 [Source organism]= [Accession]=MF7000077 [Entry] [Entry number]=274 [Entry name]=Sulerythrin (diNi) [PDB ID]=7o9e [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=2-143 [UniProt coverage chain A]=98% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=1-143 [UniProt coverage chain B]=99% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.25 [Source organism]= [Accession]=MF7000078 [Entry] [Entry number]=275 [Entry name]=Sulerythrin (diFe) [PDB ID]=7ppt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=1-143 [UniProt coverage chain A]=99% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=1-142 [UniProt coverage chain B]=98% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.42 [Source organism]= [Accession]=MF7000079 [Entry] [Entry number]=276 [Entry name]=Sulerythrin (diFe) [PDB ID]=7ppu [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=1-143 [UniProt coverage chain A]=99% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=1-142 [UniProt coverage chain B]=98% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.34 [Source organism]= [Accession]=MF7000080 [Entry] [Entry number]=277 [Entry name]=Sulerythrin (diFe) [PDB ID]=7ppv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=F9VPE5 [UniProt boundaries chain A]=1-142 [UniProt coverage chain A]=98% [Name chain A]=Sulerythrin [UniProt sequence chain A]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain A]= [UniProt ID chain B]=F9VPE5 [UniProt boundaries chain B]=1-141 [UniProt coverage chain B]=97% [Name chain B]=Sulerythrin [UniProt sequence chain B]=MKDLKGTKTAENLKQGFIGESMANRRYLYFAKRADEEGYPEIAGLLRSIAEGETAHAFGHLDFIRQGGLTDPATDKPIGTLEQMIESAIAGETYEWTQMYPGFAKVAREEGFPEVAEWFETLARAEKSHAEKFQNVLKQLKGGT [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.36 [Source organism]= [Accession]=MF7000081 [Entry] [Entry number]=278 [Entry name]=MRD [PDB ID]=1kll [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=O05205 [UniProt boundaries chain A]=3-130 [UniProt coverage chain A]=98% [Name chain A]=Mitomycin-binding protein [UniProt sequence chain A]=MSARISLFAVVVEDMAKSLEFYRKLGVEIPAEADSAPHTEAVLDGGIRLAWDTVETVRSYDPEWQAPTGGHRFAIAFEFPDTASVDKKYAELVDAGYEGHLKPWNAVWGQRYAIVKDPDGNVVDLFAPLP [Source organism chain A]=Streptomyces lavendulae [UniProt ID chain A-2]=O05205 [UniProt boundaries chain A-2]=3-130 [UniProt coverage chain A-2]=98% [Name chain A-2]=Mitomycin-binding protein [UniProt sequence chain A-2]=MSARISLFAVVVEDMAKSLEFYRKLGVEIPAEADSAPHTEAVLDGGIRLAWDTVETVRSYDPEWQAPTGGHRFAIAFEFPDTASVDKKYAELVDAGYEGHLKPWNAVWGQRYAIVKDPDGNVVDLFAPLP [Source organism chain A-2]=Streptomyces lavendulae [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Streptomyces lavendulae [Accession]=MF7000082 [Entry] [Entry number]=279 [Entry name]=Mitomycin C-Binding Protein/Copper(II)-Bleomycin A2 complex [PDB ID]=2a4w [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=O05205 [UniProt boundaries chain A]=2-129 [UniProt coverage chain A]=98% [Name chain A]=Mitomycin-binding protein [UniProt sequence chain A]=MSARISLFAVVVEDMAKSLEFYRKLGVEIPAEADSAPHTEAVLDGGIRLAWDTVETVRSYDPEWQAPTGGHRFAIAFEFPDTASVDKKYAELVDAGYEGHLKPWNAVWGQRYAIVKDPDGNVVDLFAPLP [Source organism chain A]=Streptomyces lavendulae [UniProt ID chain B]=O05205 [UniProt boundaries chain B]=2-130 [UniProt coverage chain B]=99% [Name chain B]=Mitomycin-binding protein [UniProt sequence chain B]=MSARISLFAVVVEDMAKSLEFYRKLGVEIPAEADSAPHTEAVLDGGIRLAWDTVETVRSYDPEWQAPTGGHRFAIAFEFPDTASVDKKYAELVDAGYEGHLKPWNAVWGQRYAIVKDPDGNVVDLFAPLP [Source organism chain B]=Streptomyces lavendulae [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Streptomyces lavendulae [Accession]=MF7000083 [Entry] [Entry number]=280 [Entry name]=Mitomycin C-Binding Protein/Metal-Free Bleomycin A2 complex [PDB ID]=2a4x [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=O05205 [UniProt boundaries chain A]=2-130 [UniProt coverage chain A]=99% [Name chain A]=Mitomycin-binding protein [UniProt sequence chain A]=MSARISLFAVVVEDMAKSLEFYRKLGVEIPAEADSAPHTEAVLDGGIRLAWDTVETVRSYDPEWQAPTGGHRFAIAFEFPDTASVDKKYAELVDAGYEGHLKPWNAVWGQRYAIVKDPDGNVVDLFAPLP [Source organism chain A]=Streptomyces lavendulae [UniProt ID chain B]=O05205 [UniProt boundaries chain B]=2-129 [UniProt coverage chain B]=98% [Name chain B]=Mitomycin-binding protein [UniProt sequence chain B]=MSARISLFAVVVEDMAKSLEFYRKLGVEIPAEADSAPHTEAVLDGGIRLAWDTVETVRSYDPEWQAPTGGHRFAIAFEFPDTASVDKKYAELVDAGYEGHLKPWNAVWGQRYAIVKDPDGNVVDLFAPLP [Source organism chain B]=Streptomyces lavendulae [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Streptomyces lavendulae [Accession]=MF7000084 [Entry] [Entry number]=281 [Entry name]=DNA-binding protein (M. jannaschii) [PDB ID]=1ku9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=Q58958 [UniProt boundaries chain A]=1-151 [UniProt coverage chain A]=99% [Name chain A]=Putative HTH-type transcriptional regulator MJ1563 [UniProt sequence chain A]=MIIMEEAKKLIIELFSELAKIHGLNKSVGAVYAILYLSDKPLTISDIMEELKISKGNVSMSLKKLEELGFVRKVWIKGERKNYYEAVDGFSSIKDIAKRKHDLIAKTYEDLKKLEEKCNEEEKEFIKQKIKGIERMKKISEKILEALNDLDN [Source organism chain A]=10045 / NBRC 100440) [UniProt ID chain B]=Q58958 [UniProt boundaries chain B]=1-151 [UniProt coverage chain B]=99% [Name chain B]=Putative HTH-type transcriptional regulator MJ1563 [UniProt sequence chain B]=MIIMEEAKKLIIELFSELAKIHGLNKSVGAVYAILYLSDKPLTISDIMEELKISKGNVSMSLKKLEELGFVRKVWIKGERKNYYEAVDGFSSIKDIAKRKHDLIAKTYEDLKKLEEKCNEEEKEFIKQKIKGIERMKKISEKILEALNDLDN [Source organism chain B]=10045 / NBRC 100440) [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=10045 / NBRC 100440) [Accession]=MF7000085 [Entry] [Entry number]=282 [Entry name]=C-terminal of Alpha Tropomyosin (Rat) [PDB ID]=1mv4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:12534273). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P04692 [UniProt boundaries chain A]=251-284 [UniProt coverage chain A]=11% [Name chain A]=Tropomyosin alpha-1 chain [UniProt sequence chain A]=MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P04692 [UniProt boundaries chain B]=251-284 [UniProt coverage chain B]=11% [Name chain B]=Tropomyosin alpha-1 chain [UniProt sequence chain B]=MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI [Source organism chain B]=Rattus norvegicus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Rattus norvegicus [Accession]=MF7000086 [Entry] [Entry number]=283 [Entry name]=NF-YB/NF-YC histone dimer [PDB ID]=1n1j [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) [Evidence level]=Direct evidence [Evidence text]=Histone dimerization (as well as the dimerization of histone-like domains) has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829,15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000087,MF7000088,MF7000089,MF7000090 [UniProt ID chain A]=P25208 [UniProt boundaries chain A]=57-143 [UniProt coverage chain A]=42% [Name chain A]=Nuclear transcription factor Y subunit beta [UniProt sequence chain A]=MTMDGDSSTTDASQLGISADYIGGSHYVIQPHDDTEDSMNDHEDTNGSKESFREQDIYLPIANVARIMKNAIPQTGKIAKDAKECVQECVSEFISFITSEASERCHQEKRKTINGEDILFAMSTLGFDSYVEPLKLYLQKFREAMKGEKGIGGAVTATDGLSEELTEEAFTNQLPAGLITTDGQQQNVMVYTTSYQQISGVQQIQFS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q13952 [UniProt boundaries chain B]=43-120 [UniProt coverage chain B]=17% [Name chain B]=Nuclear transcription factor Y subunit gamma [UniProt sequence chain B]=MSTEGGFGGTSSSDAQQSLQSFWPRVMEEIRNLTVKDFRVQELPLARIKKIMKLDEDVKMISAEAPVLFAKAAQIFITELTLRAWIHTEDNKRRTLQRNDIAMAITKFDQFDFLIDIVPRDELKPPKRQEEVRQSVTPAEPVQYYFTLAQQPTAVQVQGQQQGQQTTSSTTTIQPGQIIIAQPQQGQTTPVTMQVGEGQQVQIVQAQPQGQAQQAQSGTGQTMQVMQQIITNTGEIQQIPVQLNAGQLQYIRLAQPVSGTQVVQGQIQTLATNAQQGQRNASQGKPRRCLKETLQITQTEVQQGQQQFSQFTDGQRNSVQQARVSELTGEAEPREVKATGNSTPCTSSLPTTHPPSHRAGASCVCCSQPQQSSTSPPPSDALQWVVVEVSGTPNQLETHRELHAPLPGMTSLSPLHPSQQLYQIQQVTMPAGQDLAQPMFIQSANQPSDGQAPQVTGD [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.67 [Source organism]=Homo sapiens [Accession]=MF7000087 [Entry] [Entry number]=284 [Entry name]=L1L NF-YC3 histone-fold dimer [PDB ID]=5g49 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) [Evidence level]=Direct evidence [Evidence text]=Histone dimerization (as well as the dimerization of histone-like domains) has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829,15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000087,MF7000088,MF7000089,MF7000090 [UniProt ID chain A]=Q84W66 [UniProt boundaries chain A]=55-147 [UniProt coverage chain A]=39% [Name chain A]=Nuclear transcription factor Y subunit B-6 [UniProt sequence chain A]=MERGGFHGYRKLSVNNTTPSPPGLAANFLMAEGSMRPPEFNQPNKTSNGGEEECTVREQDRFMPIANVIRIMRRILPAHAKISDDSKETIQECVSEYISFITGEANERCQREQRKTITAEDVLWAMSKLGFDDYIEPLTLYLHRYRELEGERGVSCSAGSVSMTNGLVVKRPNGTMTEYGAYGPVPGIHMAQYHYRHQNGFVFSGNEPNSKMSGSSSGASGARVEVFPTQQHKY [Source organism chain A]=Arabidopsis thaliana [UniProt ID chain B]=Q9ZVL3 [UniProt boundaries chain B]=55-148 [UniProt coverage chain B]=43% [Name chain B]=Nuclear transcription factor Y subunit C-3 [UniProt sequence chain B]=MDQQGQSSAMNYGSNPYQTNAMTTTPTGSDHPAYHQIHQQQQQQLTQQLQSFWETQFKEIEKTTDFKNHSLPLARIKKIMKADEDVRMISAEAPVVFARACEMFILELTLRSWNHTEENKRRTLQKNDIAAAVTRTDIFDFLVDIVPREDLRDEVLGGVGAEAATAAGYPYGYLPPGTAPIGNPGMVMGNPGAYPPNPYMGQPMWQQPGPEQQDPDN [Source organism chain B]=Arabidopsis thaliana [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Arabidopsis thaliana [Accession]=MF7000088 [Entry] [Entry number]=285 [Entry name]=Histone fold domain of AtNF-YB2/NF-YC3 in I2 [PDB ID]=6r0n [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) [Evidence level]=Direct evidence [Evidence text]=Histone dimerization (as well as the dimerization of histone-like domains) has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829,15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000087,MF7000088,MF7000089,MF7000090 [UniProt ID chain A]=Q9FGJ3 [UniProt boundaries chain A]=26-116 [UniProt coverage chain A]=47% [Name chain A]=Nuclear transcription factor Y subunit B-2 [UniProt sequence chain A]=MGDSDRDSGGGQNGNNQNGQSSLSPREQDRFLPIANVSRIMKKALPANAKISKDAKETMQECVSEFISFVTGEASDKCQKEKRKTINGDDLLWAMTTLGFEDYVEPLKVYLQRFREIEGERTGLGRPQTGGEVGEHQRDAVGDGGGFYGGGGGMQYHQHHQFLHQQNHMYGATGGGSDSGGGAASGRTRT [Source organism chain A]=Arabidopsis thaliana [UniProt ID chain B]=Q9ZVL3 [UniProt boundaries chain B]=69-148 [UniProt coverage chain B]=36% [Name chain B]=Nuclear transcription factor Y subunit C-3 [UniProt sequence chain B]=MDQQGQSSAMNYGSNPYQTNAMTTTPTGSDHPAYHQIHQQQQQQLTQQLQSFWETQFKEIEKTTDFKNHSLPLARIKKIMKADEDVRMISAEAPVVFARACEMFILELTLRSWNHTEENKRRTLQKNDIAAAVTRTDIFDFLVDIVPREDLRDEVLGGVGAEAATAAGYPYGYLPPGTAPIGNPGMVMGNPGAYPPNPYMGQPMWQQPGPEQQDPDN [Source organism chain B]=Arabidopsis thaliana [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Arabidopsis thaliana [Accession]=MF7000089 [Entry] [Entry number]=286 [Entry name]=Histone fold domain of OsGhd8/NF-YC7 in I2 [PDB ID]=6r0l [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) [Evidence level]=Direct evidence [Evidence text]=Histone dimerization (as well as the dimerization of histone-like domains) has been experimentally characterized to be coupled to the structure formation of both interacting partners (PMID:12779337); this synergistic folding has been shown separately for various histone dimers (PMID:15588829,15096635). Histones containing various types of monomeric subunits can exhibit varying stability and folding kinetics; however, independent of composition and folding kinetics, all histones appear to fold in a cooperative fashion that is coupled to binding (PMID:11669650). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000087,MF7000088,MF7000089,MF7000090 [UniProt ID chain A]=Q0J7P4 [UniProt boundaries chain A]=60-147 [UniProt coverage chain A]=29% [Name chain A]=Nuclear transcription factor Y subunit B-11 [UniProt sequence chain A]=MKSRKSYGHLLSPVGSPPLDNESGEAAAAAAAGGGGCGSSAGYVVYGGGGGGDSPAKEQDRFLPIANVSRIMKRSLPANAKISKESKETVQECVSEFISFVTGEASDKCQREKRKTINGDDLLWAMTTLGFEAYVGPLKSYLNRYREAEGEKADVLGGAGGAAAARHGEGGCCGGGGGGADGVVIDGHYPLAGGLSHSHHGHQQQDGGGDVGLMMGGGDAGVGYNAGAGSTTTAFYAPAATAASGNKAYCGGDGSRVMEFEGIGGEEESGGGGGGGERGFAGHLHGVQWFRLKRNTN [Source organism chain A]=Oryza sativa subsp japonica [UniProt ID chain B]=Q9XE33 [UniProt boundaries chain B]=92-168 [UniProt coverage chain B]=37% [Name chain B]=Nuclear transcription factor Y subunit C-6 [UniProt sequence chain B]=MEPKSTTPPPPPPPPVLGAPVPYPPAGAYPPPVGPYAHAPPLYAPPPPAAAAASAAATAASQQAAAAQLQNFWAEQYREIEHTTDFKNHNLPLARIKKIMKADEDVRMIAAEAPVVFARACEMFILELTHRGWAHAEENKRRTLQKSDIAAAIARTEVFDFLVDIVPRDEAKDAEAAAAVAAGIPHPAAGLPATDPMAYYYVQPQ [Source organism chain B]=Oryza sativa subsp japonica [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Oryza sativa subsp japonica [Accession]=MF7000090 [Entry] [Entry number]=287 [Entry name]=Dimerization/docking domain of the type I alpha regulatory subunit of protein kinase A [PDB ID]=3im3 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=The RIα D/D dimer is comprised of an X-type anti-parallel, four-helix bundle with each monomer contributing two helices, α1 and α2, to the hydrophobic dimer interface. α0 at the N-terminus also contributes to the dimer interface through two intermolecular disulfide bonds between Cys16 and Cys37 (PMID:20159461). The relative interface is very large. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P00514 [UniProt boundaries chain A]=13-62 [UniProt coverage chain A]=13% [Name chain A]=cAMP-dependent protein kinase type I-alpha regulatory subunit [UniProt sequence chain A]=MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV [Source organism chain A]=Bos taurus [UniProt ID chain A-2]=P00514 [UniProt boundaries chain A-2]=13-62 [UniProt coverage chain A-2]=13% [Name chain A-2]=cAMP-dependent protein kinase type I-alpha regulatory subunit [UniProt sequence chain A-2]=MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV [Source organism chain A-2]=Bos taurus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Bos taurus [Accession]=MF7000092 [Entry] [Entry number]=288 [Entry name]=Rubrerythrin (Pyrococcus furiosus) [PDB ID]=1nnq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Rubrerythrin-like fold [Evidence level]=Direct evidence [Evidence text]=Domain-swapped rubrerythrin-like fold, the coiled coils from the two monomers form a four-helix bundle within the dimer. There is a strong dimer interface within the hybrid four-helix bundle between the monomers, and a weak interface between the two bundles (PMID:14529281, PMID:34757735). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000070,MF7000093,MF7000071,MF7000072,MF7000073,MF7000074,MF7000075,MF7000076,MF7000077,MF7000078,MF7000079,MF7000080,MF7000081 [UniProt ID chain A]=Q9UWP7 [UniProt boundaries chain A]=2-171 [UniProt coverage chain A]=99% [Name chain A]=Rubrerythrin [UniProt sequence chain A]=MVVKRTMTKKFLEEAFAGESMAHMRYLIFAEKAEQEGFPNIAKLFRAIAYAEFVHAKNHFIALGKLGKTPENLQMGIEGETFEVEEMYPVYNKAAEFQGEKEAVRTTHYALEAEKIHAELYRKAKEKAEKGEDIEIKKVYICPICGYTAVDEAPEYCPVCGAPKEKFVVFE [Source organism chain A]=Pyrococcus furiosus [UniProt ID chain B]=Q9UWP7 [UniProt boundaries chain B]=2-171 [UniProt coverage chain B]=99% [Name chain B]=Rubrerythrin [UniProt sequence chain B]=MVVKRTMTKKFLEEAFAGESMAHMRYLIFAEKAEQEGFPNIAKLFRAIAYAEFVHAKNHFIALGKLGKTPENLQMGIEGETFEVEEMYPVYNKAAEFQGEKEAVRTTHYALEAEKIHAELYRKAKEKAEKGEDIEIKKVYICPICGYTAVDEAPEYCPVCGAPKEKFVVFE [Source organism chain B]=Pyrococcus furiosus [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Pyrococcus furiosus [Accession]=MF7000093 [Entry] [Entry number]=289 [Entry name]=Dimerization motif of Sir4p [PDB ID]=1nyh [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Regulatory protein SIR4 coiled coil [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:12791253). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000094,MF7000095 [UniProt ID chain A]=P11978 [UniProt boundaries chain A]=1271-1346 [UniProt coverage chain A]=5% [Name chain A]=Regulatory protein SIR4 [UniProt sequence chain A]=MPNDNKTPNRSSTPKFTKKPVTPNDKIPEREEKSNEVKTPKIPLFTFAKSKNYSRPSTAIHTSPHQPSDVKPTSHKQLQQPKSSPLKKNNYNSFPHSNLEKISNSKLLSLLRSKTSAGRIESNNPSHDASRSLASFEQTAFSRHAQQQTSTFNSKPVRTIVPISTSQTNNSFLSGVKSLLSEEKIRDYSKEILGINLANEQPVLEKPLKKGSADIGASVISLTKDKSIRKDTVEEKKEEKLNIGKNFAHSDSLSVPKVSAGDSGISPEESKARSPGIAKPNAIQTEVYGINEESTNERLEINQEKPVKLDENSANSTVASALDTNGTSATTETLTSKKIVPSPKKVAIDQDKITLHDEKTLAPSKHQPITSEQKMKEDADLKRMEILKSPHLSKSPADRPQGRRNSRNFSTRDEETTKLAFLVEYEGQENNYNSTSRSTEKKNDMNTSAKNKNGENKKIGKRPPEIMSTEAHVNKVTEETTKQIQSVRIDGRKVLQKVQGESHIDSRNNTLNVTPSKRPQLGEIPNPMKKHKPNEGRTPNISNGTINIQKKLEPKEIVRDILHTKESSNEAKKTIQNPLNKSQNTALPSTHKVTQKKDIKIGTNDLFQVESAPKISSEIDRENVKSKDEPVSKAVESKSLLNLFSNVLKAPFIKSESKPFSSDALSKEKANFLETIASTEKPENKTDKVSLSQPVSASKHEYSDNFPVSLSQPSKKSFANHTEDEQIEKKKICRGRMNTIITHPGKMELVYVSDSDDSSSDNDSLTDLESLSSGESNEIKVTNDLDTSAEKDQIQAGKWFDPVLDWRKSDRELTKNILWRIADKTTYDKETITDLIEQGIPKHSYLSGNPLTSVTNDICSVENYETSSAFFYQQVHKKDRLQYLPLYAVSTFENTNNTEKNDVTNKNINIGKHSQEQNSSSAKPSQIPTVSSPLGFEETKLSTTPTKSNRRVSHSDTNSSKPKNTKENLSKSSWRQEWLANLKLISVSLVDEFPSELSDSDRQIINEKMQLLKDIFANNLKSAISNNFRESDIIILKGEIEDYPMSSEIKIYYNELQNKPDAKKARFWSFMKTQRFVSNMGFDIQKSCEPVSISTSVKPHVVEPEHMADAKIMPKDILQITKKPLMVKNVKPSSPPDVKSLVQLSTMETKTLPEKKQFDSIFNSNKAKIIPGNGKHASENISLSFSRPASYGYFSVGKRVPIVEDRRVKQLDDITDSNTTEILTSVDVLGTHSQTGTQQSNMYTSTQKTELEIDNKDSVTECSKDMKEDGLSFVDIVLSKAASALDEKEKQLAVANEIIRSLSDEVMRNEIRITSLQGDLTFTKKCLENARSQISEKDAKINKLMEKDFQVNKEIKPY [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=P11978 [UniProt boundaries chain A-2]=1271-1346 [UniProt coverage chain A-2]=5% [Name chain A-2]=Regulatory protein SIR4 [UniProt sequence chain A-2]=MPNDNKTPNRSSTPKFTKKPVTPNDKIPEREEKSNEVKTPKIPLFTFAKSKNYSRPSTAIHTSPHQPSDVKPTSHKQLQQPKSSPLKKNNYNSFPHSNLEKISNSKLLSLLRSKTSAGRIESNNPSHDASRSLASFEQTAFSRHAQQQTSTFNSKPVRTIVPISTSQTNNSFLSGVKSLLSEEKIRDYSKEILGINLANEQPVLEKPLKKGSADIGASVISLTKDKSIRKDTVEEKKEEKLNIGKNFAHSDSLSVPKVSAGDSGISPEESKARSPGIAKPNAIQTEVYGINEESTNERLEINQEKPVKLDENSANSTVASALDTNGTSATTETLTSKKIVPSPKKVAIDQDKITLHDEKTLAPSKHQPITSEQKMKEDADLKRMEILKSPHLSKSPADRPQGRRNSRNFSTRDEETTKLAFLVEYEGQENNYNSTSRSTEKKNDMNTSAKNKNGENKKIGKRPPEIMSTEAHVNKVTEETTKQIQSVRIDGRKVLQKVQGESHIDSRNNTLNVTPSKRPQLGEIPNPMKKHKPNEGRTPNISNGTINIQKKLEPKEIVRDILHTKESSNEAKKTIQNPLNKSQNTALPSTHKVTQKKDIKIGTNDLFQVESAPKISSEIDRENVKSKDEPVSKAVESKSLLNLFSNVLKAPFIKSESKPFSSDALSKEKANFLETIASTEKPENKTDKVSLSQPVSASKHEYSDNFPVSLSQPSKKSFANHTEDEQIEKKKICRGRMNTIITHPGKMELVYVSDSDDSSSDNDSLTDLESLSSGESNEIKVTNDLDTSAEKDQIQAGKWFDPVLDWRKSDRELTKNILWRIADKTTYDKETITDLIEQGIPKHSYLSGNPLTSVTNDICSVENYETSSAFFYQQVHKKDRLQYLPLYAVSTFENTNNTEKNDVTNKNINIGKHSQEQNSSSAKPSQIPTVSSPLGFEETKLSTTPTKSNRRVSHSDTNSSKPKNTKENLSKSSWRQEWLANLKLISVSLVDEFPSELSDSDRQIINEKMQLLKDIFANNLKSAISNNFRESDIIILKGEIEDYPMSSEIKIYYNELQNKPDAKKARFWSFMKTQRFVSNMGFDIQKSCEPVSISTSVKPHVVEPEHMADAKIMPKDILQITKKPLMVKNVKPSSPPDVKSLVQLSTMETKTLPEKKQFDSIFNSNKAKIIPGNGKHASENISLSFSRPASYGYFSVGKRVPIVEDRRVKQLDDITDSNTTEILTSVDVLGTHSQTGTQQSNMYTSTQKTELEIDNKDSVTECSKDMKEDGLSFVDIVLSKAASALDEKEKQLAVANEIIRSLSDEVMRNEIRITSLQGDLTFTKKCLENARSQISEKDAKINKLMEKDFQVNKEIKPY [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=3.10 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000094 [Entry] [Entry number]=290 [Entry name]=Coiled coil C-terminal of Sir4p [PDB ID]=1pl5 [Chains]=S,A [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Regulatory protein SIR4 coiled coil [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:14636601). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain S]=N/A [Similar structures]=MF7000094,MF7000095 [UniProt ID chain A]=P11978 [UniProt boundaries chain A]=1272-1346 [UniProt coverage chain A]=5% [Name chain A]=Regulatory protein SIR4 [UniProt sequence chain A]=MPNDNKTPNRSSTPKFTKKPVTPNDKIPEREEKSNEVKTPKIPLFTFAKSKNYSRPSTAIHTSPHQPSDVKPTSHKQLQQPKSSPLKKNNYNSFPHSNLEKISNSKLLSLLRSKTSAGRIESNNPSHDASRSLASFEQTAFSRHAQQQTSTFNSKPVRTIVPISTSQTNNSFLSGVKSLLSEEKIRDYSKEILGINLANEQPVLEKPLKKGSADIGASVISLTKDKSIRKDTVEEKKEEKLNIGKNFAHSDSLSVPKVSAGDSGISPEESKARSPGIAKPNAIQTEVYGINEESTNERLEINQEKPVKLDENSANSTVASALDTNGTSATTETLTSKKIVPSPKKVAIDQDKITLHDEKTLAPSKHQPITSEQKMKEDADLKRMEILKSPHLSKSPADRPQGRRNSRNFSTRDEETTKLAFLVEYEGQENNYNSTSRSTEKKNDMNTSAKNKNGENKKIGKRPPEIMSTEAHVNKVTEETTKQIQSVRIDGRKVLQKVQGESHIDSRNNTLNVTPSKRPQLGEIPNPMKKHKPNEGRTPNISNGTINIQKKLEPKEIVRDILHTKESSNEAKKTIQNPLNKSQNTALPSTHKVTQKKDIKIGTNDLFQVESAPKISSEIDRENVKSKDEPVSKAVESKSLLNLFSNVLKAPFIKSESKPFSSDALSKEKANFLETIASTEKPENKTDKVSLSQPVSASKHEYSDNFPVSLSQPSKKSFANHTEDEQIEKKKICRGRMNTIITHPGKMELVYVSDSDDSSSDNDSLTDLESLSSGESNEIKVTNDLDTSAEKDQIQAGKWFDPVLDWRKSDRELTKNILWRIADKTTYDKETITDLIEQGIPKHSYLSGNPLTSVTNDICSVENYETSSAFFYQQVHKKDRLQYLPLYAVSTFENTNNTEKNDVTNKNINIGKHSQEQNSSSAKPSQIPTVSSPLGFEETKLSTTPTKSNRRVSHSDTNSSKPKNTKENLSKSSWRQEWLANLKLISVSLVDEFPSELSDSDRQIINEKMQLLKDIFANNLKSAISNNFRESDIIILKGEIEDYPMSSEIKIYYNELQNKPDAKKARFWSFMKTQRFVSNMGFDIQKSCEPVSISTSVKPHVVEPEHMADAKIMPKDILQITKKPLMVKNVKPSSPPDVKSLVQLSTMETKTLPEKKQFDSIFNSNKAKIIPGNGKHASENISLSFSRPASYGYFSVGKRVPIVEDRRVKQLDDITDSNTTEILTSVDVLGTHSQTGTQQSNMYTSTQKTELEIDNKDSVTECSKDMKEDGLSFVDIVLSKAASALDEKEKQLAVANEIIRSLSDEVMRNEIRITSLQGDLTFTKKCLENARSQISEKDAKINKLMEKDFQVNKEIKPY [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain S]=P11978 [UniProt boundaries chain S]=1272-1347 [UniProt coverage chain S]=5% [Name chain S]=Regulatory protein SIR4 [UniProt sequence chain S]=MPNDNKTPNRSSTPKFTKKPVTPNDKIPEREEKSNEVKTPKIPLFTFAKSKNYSRPSTAIHTSPHQPSDVKPTSHKQLQQPKSSPLKKNNYNSFPHSNLEKISNSKLLSLLRSKTSAGRIESNNPSHDASRSLASFEQTAFSRHAQQQTSTFNSKPVRTIVPISTSQTNNSFLSGVKSLLSEEKIRDYSKEILGINLANEQPVLEKPLKKGSADIGASVISLTKDKSIRKDTVEEKKEEKLNIGKNFAHSDSLSVPKVSAGDSGISPEESKARSPGIAKPNAIQTEVYGINEESTNERLEINQEKPVKLDENSANSTVASALDTNGTSATTETLTSKKIVPSPKKVAIDQDKITLHDEKTLAPSKHQPITSEQKMKEDADLKRMEILKSPHLSKSPADRPQGRRNSRNFSTRDEETTKLAFLVEYEGQENNYNSTSRSTEKKNDMNTSAKNKNGENKKIGKRPPEIMSTEAHVNKVTEETTKQIQSVRIDGRKVLQKVQGESHIDSRNNTLNVTPSKRPQLGEIPNPMKKHKPNEGRTPNISNGTINIQKKLEPKEIVRDILHTKESSNEAKKTIQNPLNKSQNTALPSTHKVTQKKDIKIGTNDLFQVESAPKISSEIDRENVKSKDEPVSKAVESKSLLNLFSNVLKAPFIKSESKPFSSDALSKEKANFLETIASTEKPENKTDKVSLSQPVSASKHEYSDNFPVSLSQPSKKSFANHTEDEQIEKKKICRGRMNTIITHPGKMELVYVSDSDDSSSDNDSLTDLESLSSGESNEIKVTNDLDTSAEKDQIQAGKWFDPVLDWRKSDRELTKNILWRIADKTTYDKETITDLIEQGIPKHSYLSGNPLTSVTNDICSVENYETSSAFFYQQVHKKDRLQYLPLYAVSTFENTNNTEKNDVTNKNINIGKHSQEQNSSSAKPSQIPTVSSPLGFEETKLSTTPTKSNRRVSHSDTNSSKPKNTKENLSKSSWRQEWLANLKLISVSLVDEFPSELSDSDRQIINEKMQLLKDIFANNLKSAISNNFRESDIIILKGEIEDYPMSSEIKIYYNELQNKPDAKKARFWSFMKTQRFVSNMGFDIQKSCEPVSISTSVKPHVVEPEHMADAKIMPKDILQITKKPLMVKNVKPSSPPDVKSLVQLSTMETKTLPEKKQFDSIFNSNKAKIIPGNGKHASENISLSFSRPASYGYFSVGKRVPIVEDRRVKQLDDITDSNTTEILTSVDVLGTHSQTGTQQSNMYTSTQKTELEIDNKDSVTECSKDMKEDGLSFVDIVLSKAASALDEKEKQLAVANEIIRSLSDEVMRNEIRITSLQGDLTFTKKCLENARSQISEKDAKINKLMEKDFQVNKEIKPY [Source organism chain S]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000095 [Entry] [Entry number]=291 [Entry name]=Orphan protein (TM0875) [PDB ID]=1o22 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. Authors describe the dimeric structure as highly intertwined including a four-stranded antiparallel β-sheet formed by both monomers (PMID:15229892). Only the first and last segments contribute to dimerization through MSF, while there is a well-folded part in the middle of the monomers. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q9WZX8 [UniProt boundaries chain A]=6-154 [UniProt coverage chain A]=94% [Name chain A]=DUF3855 domain-containing protein [UniProt sequence chain A]=MRLMDILEILYYKKGKEFGILEKKMKEIFNETGVSLEPVNSELIGRIFLKISVLEEGEEVPSFAIKALTPKENAVDLPLGDWTDLKNVFVEEIDYLDSYGDMKILSEKNWYKIYVPYSSVKKKNRNELVEEFMKYFFESKGWNPGEYTFSVQEIDNLF [Source organism chain A]=/ MSB8) [UniProt ID chain A-2]=Q9WZX8 [UniProt boundaries chain A-2]=6-154 [UniProt coverage chain A-2]=94% [Name chain A-2]=DUF3855 domain-containing protein [UniProt sequence chain A-2]=MRLMDILEILYYKKGKEFGILEKKMKEIFNETGVSLEPVNSELIGRIFLKISVLEEGEEVPSFAIKALTPKENAVDLPLGDWTDLKNVFVEEIDYLDSYGDMKILSEKNWYKIYVPYSSVKKKNRNELVEEFMKYFFESKGWNPGEYTFSVQEIDNLF [Source organism chain A-2]=/ MSB8) [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=/ MSB8) [Accession]=MF7000096 [Entry] [Entry number]=292 [Entry name]=Nucleocapsid protein of PRRSV [PDB ID]=1p65 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Nucleocapsid proteins [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. However, there is beta sheet augmentation and helix packing interactions between the small monomers, they are most probably not stable on their own (PMID:14604534). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9YJI1 [UniProt boundaries chain A]=62-118 [UniProt coverage chain A]=46% [Name chain A]=Nucleoprotein [UniProt sequence chain A]=MPNNNGRQQKKKKGDGQPVNQLCQMLGKIIAQQNQSRGKGPGRKIKKKNPEKPHFPLETEDDVRHHFTPSERQLCLSSIQTAFNQGAGTCTLSDSGRISYTVEFSLPTHHTVRLIRVTASPSA [Source organism chain A]=Porcine reproductive and respiratory syndrome virus [UniProt ID chain B]=Q9YJI1 [UniProt boundaries chain B]=62-118 [UniProt coverage chain B]=46% [Name chain B]=Nucleoprotein [UniProt sequence chain B]=MPNNNGRQQKKKKGDGQPVNQLCQMLGKIIAQQNQSRGKGPGRKIKKKNPEKPHFPLETEDDVRHHFTPSERQLCLSSIQTAFNQGAGTCTLSDSGRISYTVEFSLPTHHTVRLIRVTASPSA [Source organism chain B]=Porcine reproductive and respiratory syndrome virus [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Porcine reproductive and respiratory syndrome virus [Accession]=MF7000097 [Entry] [Entry number]=293 [Entry name]=Human Glyoxalase I [PDB ID]=1qin [Chains]=A,B [Total number of chains]=2 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q04760 [UniProt boundaries chain A]=9-184 [UniProt coverage chain A]=95% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q04760 [UniProt boundaries chain B]=9-184 [UniProt coverage chain B]=95% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000098 [Entry] [Entry number]=295 [Entry name]=Binding domain of E2 of the pyruvate dehydrogenase complex [PDB ID]=8oqj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. Only dimeric form detected even at very low concentrations (PMID:38324697). Extensive helix packing between the two small monomers. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P06959 [UniProt boundaries chain A]=322-375 [UniProt coverage chain A]=8% [Name chain A]=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex [UniProt sequence chain A]=MAIEIKVPDIGADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTQTGALIMIFDSADGAADAAPAQAEEKKEAAPAAAPAAAAAKDVNVPDIGSDEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAGAAAPAAKQEAAPAAAPAPAAGVKEVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGVVKELKVNVGDKVKTGSLIMIFEVEGAAPAAAPAKQEAAAPAPAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKEAIKRAEAAPAATGGGIPGMLPWPKVDFSKFGEIEEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITELEAFRKQQNEEAAKRKLDVKITPVVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYINIGVAVDTPNGLVVPVFKDVNKKGIIELSRELMTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMLPISLSFDHRVIDGADGARFITIINNTLSDIRRLVM [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P06959 [UniProt boundaries chain B]=322-376 [UniProt coverage chain B]=8% [Name chain B]=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex [UniProt sequence chain B]=MAIEIKVPDIGADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTQTGALIMIFDSADGAADAAPAQAEEKKEAAPAAAPAAAAAKDVNVPDIGSDEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAGAAAPAAKQEAAPAAAPAPAAGVKEVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGVVKELKVNVGDKVKTGSLIMIFEVEGAAPAAAPAKQEAAAPAPAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKEAIKRAEAAPAATGGGIPGMLPWPKVDFSKFGEIEEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITELEAFRKQQNEEAAKRKLDVKITPVVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYINIGVAVDTPNGLVVPVFKDVNKKGIIELSRELMTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMLPISLSFDHRVIDGADGARFITIINNTLSDIRRLVM [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.64 [Source organism]=Escherichia coli [Accession]=MF7000100 [Entry] [Entry number]=296 [Entry name]=C-terminal of ProP [PDB ID]=1r48 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:14643666). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P0C0L7 [UniProt boundaries chain A]=468-497 [UniProt coverage chain A]=6% [Name chain A]=Proline/betaine transporter [UniProt sequence chain A]=MLKRKKVKPITLRDVTIIDDGKLRKAITAASLGNAMEWFDFGVYGFVAYALGKVFFPGADPSVQMVAALATFSVPFLIRPLGGLFFGMLGDKYGRQKILAITIVIMSISTFCIGLIPSYDTIGIWAPILLLICKMAQGFSVGGEYTGASIFVAEYSPDRKRGFMGSWLDFGSIAGFVLGAGVVVLISTIVGEANFLDWGWRIPFFIALPLGIIGLYLRHALEETPAFQQHVDKLEQGDREGLQDGPKVSFKEIATKYWRSLLTCIGLVIATNVTYYMLLTYMPSYLSHNLHYSEDHGVLIIIAIMIGMLFVQPVMGLLSDRFGRRPFVLLGSVALFVLAIPAFILINSNVIGLIFAGLLMLAVILNCFTGVMASTLPAMFPTHIRYSALAAAFNISVLVAGLTPTLAAWLVESSQNLMMPAYYLMVVAVVGLITGVTMKETANRPLKGATPAASDIQEAKEILVEHYDNIEQKIDDIDHEIADLQAKRTRLVQQHPRIDE [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0C0L7 [UniProt boundaries chain B]=468-497 [UniProt coverage chain B]=6% [Name chain B]=Proline/betaine transporter [UniProt sequence chain B]=MLKRKKVKPITLRDVTIIDDGKLRKAITAASLGNAMEWFDFGVYGFVAYALGKVFFPGADPSVQMVAALATFSVPFLIRPLGGLFFGMLGDKYGRQKILAITIVIMSISTFCIGLIPSYDTIGIWAPILLLICKMAQGFSVGGEYTGASIFVAEYSPDRKRGFMGSWLDFGSIAGFVLGAGVVVLISTIVGEANFLDWGWRIPFFIALPLGIIGLYLRHALEETPAFQQHVDKLEQGDREGLQDGPKVSFKEIATKYWRSLLTCIGLVIATNVTYYMLLTYMPSYLSHNLHYSEDHGVLIIIAIMIGMLFVQPVMGLLSDRFGRRPFVLLGSVALFVLAIPAFILINSNVIGLIFAGLLMLAVILNCFTGVMASTLPAMFPTHIRYSALAAAFNISVLVAGLTPTLAAWLVESSQNLMMPAYYLMVVAVVGLITGVTMKETANRPLKGATPAASDIQEAKEILVEHYDNIEQKIDDIDHEIADLQAKRTRLVQQHPRIDE [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF7000101 [Entry] [Entry number]=297 [Entry name]=FosX (Mesorhizobium Loti) [PDB ID]=1r9c [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q98GG1 [UniProt boundaries chain A]=1-130 [UniProt coverage chain A]=93% [Name chain A]=Fosfomycin resistance protein FosX [UniProt sequence chain A]=MIEGLSHMTFIVRDLERMTRILEGVFDAREVYASDTEQFSLSREKFFLIGDIWVAIMQGEKLAERSYNHIAFKIDDADFDRYAERVGKLGLDMRPPRPRVEGEGRSIYFYDDDNHMFELHTGTLTERLARKAKGLEAAQ [Source organism chain A]= [UniProt ID chain B]=Q98GG1 [UniProt boundaries chain B]=1-129 [UniProt coverage chain B]=92% [Name chain B]=Fosfomycin resistance protein FosX [UniProt sequence chain B]=MIEGLSHMTFIVRDLERMTRILEGVFDAREVYASDTEQFSLSREKFFLIGDIWVAIMQGEKLAERSYNHIAFKIDDADFDRYAERVGKLGLDMRPPRPRVEGEGRSIYFYDDDNHMFELHTGTLTERLARKAKGLEAAQ [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.83 [Source organism]= [Accession]=MF7000102 [Entry] [Entry number]=298 [Entry name]=FosX (Listeria monocytogenes, hexagonal form) [PDB ID]=2p7k [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q8Y6I2 [UniProt boundaries chain A]=1-128 [UniProt coverage chain A]=96% [Name chain A]=Fosfomycin resistance protein FosX [UniProt sequence chain A]=MISGLSHITLIVKDLNKTTTFLREIFNAEEIYSSGDQTFSLSKEKFFLIAGLWICIMEGDSLQEQTYNHIAFRIQSEEVDEYIERIKSLGVEIKPERPRVEGEGRSIYFYDFDNHLFELHAGTLEERLKRYHE [Source organism chain A]=Listeria monocytogenes serovar 1/2a [UniProt ID chain B]=Q8Y6I2 [UniProt boundaries chain B]=1-128 [UniProt coverage chain B]=96% [Name chain B]=Fosfomycin resistance protein FosX [UniProt sequence chain B]=MISGLSHITLIVKDLNKTTTFLREIFNAEEIYSSGDQTFSLSKEKFFLIAGLWICIMEGDSLQEQTYNHIAFRIQSEEVDEYIERIKSLGVEIKPERPRVEGEGRSIYFYDFDNHLFELHAGTLEERLKRYHE [Source organism chain B]=Listeria monocytogenes serovar 1/2a [ExpTech]=X-ray [Resolution]=3.30 [Source organism]=Listeria monocytogenes serovar 1/2a [Accession]=MF7000103 [Entry] [Entry number]=299 [Entry name]=FosX (Listeria monocytogenes, tetragonal form) [PDB ID]=2p7o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q8Y6I2 [UniProt boundaries chain A]=1-132 [UniProt coverage chain A]=99% [Name chain A]=Fosfomycin resistance protein FosX [UniProt sequence chain A]=MISGLSHITLIVKDLNKTTTFLREIFNAEEIYSSGDQTFSLSKEKFFLIAGLWICIMEGDSLQEQTYNHIAFRIQSEEVDEYIERIKSLGVEIKPERPRVEGEGRSIYFYDFDNHLFELHAGTLEERLKRYHE [Source organism chain A]=Listeria monocytogenes serovar 1/2a [UniProt ID chain B]=Q8Y6I2 [UniProt boundaries chain B]=1-131 [UniProt coverage chain B]=98% [Name chain B]=Fosfomycin resistance protein FosX [UniProt sequence chain B]=MISGLSHITLIVKDLNKTTTFLREIFNAEEIYSSGDQTFSLSKEKFFLIAGLWICIMEGDSLQEQTYNHIAFRIQSEEVDEYIERIKSLGVEIKPERPRVEGEGRSIYFYDFDNHLFELHAGTLEERLKRYHE [Source organism chain B]=Listeria monocytogenes serovar 1/2a [ExpTech]=X-ray [Resolution]=1.44 [Source organism]=Listeria monocytogenes serovar 1/2a [Accession]=MF7000104 [Entry] [Entry number]=300 [Entry name]=Dimerization domain of talin [PDB ID]=2qdq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:18157087). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P26039 [UniProt boundaries chain A]=2496-2529 [UniProt coverage chain A]=1% [Name chain A]=Talin-1 [UniProt sequence chain A]=MVALSLKISIGNVVKTMQFEPSTMVYDACRMIRERIPEALAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEYRKKQRPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDIILKKKKSKDHFGLEGDEESTMLEDSVSPKKSTVLQQQYNRVGKVEHGSVALPAIMRSGASGPENFQVGSMPPAQQQITSGQMHRGHMPPLTSAQQALTGTINSSMQAVQAAQATLDDFETLPPLGQDAASKAWRKNKMDESKHEIHSQVDAITAGTASVVNLTAGDPAETDYTAVGCAVTTISSNLTEMSRGVKLLAALLEDEGGNGRPLLQAAKGLAGAVSELLRSAQPASAEPRQNLLQAAGNVGQASGELLQQIGESDTDPHFQDVLMQLAKAVASAAAALVLKAKSVAQRTEDSGLQTQVIAAATQCALSTSQLVACTKVVAPTISSPVCQEQLVEAGRLVAKAVEGCVSASQAATEDGQLLRGVGAAATAVTQALNELLQHVKAHATGAGPAGRYDQATDTILTVTENIFSSMGDAGEMVRQARILAQATSDLVNAIKADAEGESDLENSRKLLSAAKILADATAKMVEAAKGAAAHPDSEEQQQRLREAAEGLRMATNAAAQNAIKKKLVQRLEHAAKQAAASATQTIAAAQHAASAPKASAGPQPLLVQSCKAVAEQIPLLVQGVRGSQAQPDSPSAQLALIAASQSFLQPGGKMVAAAKASVPTIQDQASAMQLSQCAKNLGTALAELRTAAQKAQEACGPLEMDSALSVVQNLEKDLQEIKAAARDGKLKPLPGETMEKCTQDLGNSTKAVSSAIAKLLGEIAQGNENYAGIAARDVAGGLRSLAQAARGVAALTSDPAVQAIVLDTASDVLDKASSLIEEAKKASGHPGDPESQQRLAQVAKAVTQALNRCVSCLPGQRDVDNALRAVGDASKRLLSDSLPPSTGTFQEAQSRLNEAAAGLNQAATELVQASRGTPQDLARASGRFGQDFSTFLEAGVEMAGQAPSQEDRAQVVSNLKGISMSSSKLLLAAKALSTDPASPNLKSQLAAAARAVTDSINQLITMCTQQAPGQKECDNALRQLETVRELLENPVQPINDMSYFGCLDSVMENSKVLGEAMTGISQNAKNGNLPEFGDAIATASKALCGFTEAAAQAAYLVGVSDPNSQAGQQGLVEPTQFARANQAIQMACQSLGEPGCTQAQVLSAATIVAKHTSALCNSCRLASARTANPTAKRQFVQSAKEVANSTANLVKTIKALDGDFTEENRAQCRAATAPLLEAVDNLSAFASNPEFSSVPAQISPEGRAAMEPIVISAKTMLESAGGLIQTARALAVNPRDPPRWSVLAGHSRTVSDSIKKLITSMRDKAPGQLECETAIAALNSCLRDLDQASLAAVSQQLAPREGISQEALHTQMLTAVQEISHLIEPLASAARAEASQLGHKVSQMAQYFEPLTLAAVGAASKTLSHPQQMALLDQTKTLAESALQLLYTAKEAGGNPKQAAHTQEALEEAVQMMTEAVEDLTTTLNEAASAAGVVGGMVDSITQAINQLDEGPMGDPEGSFVDYQTTMVRTAKAIAVTVQEMVTKSNTSPEELGPLANQLTSDYGRLASQAKPAAVAAENEEIGAHIKHRVQELGHGCSALVTKAGALQCSPSDVYTKKELIECARRVSEKVSHVLAALQAGNRGTQACITAASAVSGIIADLDTTIMFATAGTLNREGAETFADHREGILKTAKVLVEDTKVLVQNAAGSQEKLAQAAQSSVATITRLADVVKLGAASLGAEDPETQVVLINAVKDVAKALGDLISATKAAAGKVGDDPAVWQLKNSAKVMVTNVTSLLKTVKAVEDEATKGTRALEATTEHIRQELAVFCSPEPPAKTSTPEDFIRMTKGITMATAKAVAAGNSCRQEDVIATANLSRRAIADMLRACKEAAFHPEVAPDVRLRALHYGRECANGYLELLDHVLLTLQKPNPDLKQQLTGHSKRVAGSVTELIQAAEAMKGTEWVDPEDPTVIAENELLGAAAAIEAAAKKLEQLKPRAKPKEADESLNFEEQILEAAKSIAAATSALVKAASAAQRELVAQGKVGAIPANALDDGQWSQGLISAARMVAAATNNLCEAANAAVQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAVKRASDNLVKAAQKAAAFEDQENETVVVKEKMVGGIAQIIAAQEEMLRKERELEEARKKLAQIRQQQYKFLPSELRDEH [Source organism chain A]=Mus musculus [UniProt ID chain B]=P26039 [UniProt boundaries chain B]=2497-2529 [UniProt coverage chain B]=1% [Name chain B]=Talin-1 [UniProt sequence chain B]=MVALSLKISIGNVVKTMQFEPSTMVYDACRMIRERIPEALAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEYRKKQRPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDIILKKKKSKDHFGLEGDEESTMLEDSVSPKKSTVLQQQYNRVGKVEHGSVALPAIMRSGASGPENFQVGSMPPAQQQITSGQMHRGHMPPLTSAQQALTGTINSSMQAVQAAQATLDDFETLPPLGQDAASKAWRKNKMDESKHEIHSQVDAITAGTASVVNLTAGDPAETDYTAVGCAVTTISSNLTEMSRGVKLLAALLEDEGGNGRPLLQAAKGLAGAVSELLRSAQPASAEPRQNLLQAAGNVGQASGELLQQIGESDTDPHFQDVLMQLAKAVASAAAALVLKAKSVAQRTEDSGLQTQVIAAATQCALSTSQLVACTKVVAPTISSPVCQEQLVEAGRLVAKAVEGCVSASQAATEDGQLLRGVGAAATAVTQALNELLQHVKAHATGAGPAGRYDQATDTILTVTENIFSSMGDAGEMVRQARILAQATSDLVNAIKADAEGESDLENSRKLLSAAKILADATAKMVEAAKGAAAHPDSEEQQQRLREAAEGLRMATNAAAQNAIKKKLVQRLEHAAKQAAASATQTIAAAQHAASAPKASAGPQPLLVQSCKAVAEQIPLLVQGVRGSQAQPDSPSAQLALIAASQSFLQPGGKMVAAAKASVPTIQDQASAMQLSQCAKNLGTALAELRTAAQKAQEACGPLEMDSALSVVQNLEKDLQEIKAAARDGKLKPLPGETMEKCTQDLGNSTKAVSSAIAKLLGEIAQGNENYAGIAARDVAGGLRSLAQAARGVAALTSDPAVQAIVLDTASDVLDKASSLIEEAKKASGHPGDPESQQRLAQVAKAVTQALNRCVSCLPGQRDVDNALRAVGDASKRLLSDSLPPSTGTFQEAQSRLNEAAAGLNQAATELVQASRGTPQDLARASGRFGQDFSTFLEAGVEMAGQAPSQEDRAQVVSNLKGISMSSSKLLLAAKALSTDPASPNLKSQLAAAARAVTDSINQLITMCTQQAPGQKECDNALRQLETVRELLENPVQPINDMSYFGCLDSVMENSKVLGEAMTGISQNAKNGNLPEFGDAIATASKALCGFTEAAAQAAYLVGVSDPNSQAGQQGLVEPTQFARANQAIQMACQSLGEPGCTQAQVLSAATIVAKHTSALCNSCRLASARTANPTAKRQFVQSAKEVANSTANLVKTIKALDGDFTEENRAQCRAATAPLLEAVDNLSAFASNPEFSSVPAQISPEGRAAMEPIVISAKTMLESAGGLIQTARALAVNPRDPPRWSVLAGHSRTVSDSIKKLITSMRDKAPGQLECETAIAALNSCLRDLDQASLAAVSQQLAPREGISQEALHTQMLTAVQEISHLIEPLASAARAEASQLGHKVSQMAQYFEPLTLAAVGAASKTLSHPQQMALLDQTKTLAESALQLLYTAKEAGGNPKQAAHTQEALEEAVQMMTEAVEDLTTTLNEAASAAGVVGGMVDSITQAINQLDEGPMGDPEGSFVDYQTTMVRTAKAIAVTVQEMVTKSNTSPEELGPLANQLTSDYGRLASQAKPAAVAAENEEIGAHIKHRVQELGHGCSALVTKAGALQCSPSDVYTKKELIECARRVSEKVSHVLAALQAGNRGTQACITAASAVSGIIADLDTTIMFATAGTLNREGAETFADHREGILKTAKVLVEDTKVLVQNAAGSQEKLAQAAQSSVATITRLADVVKLGAASLGAEDPETQVVLINAVKDVAKALGDLISATKAAAGKVGDDPAVWQLKNSAKVMVTNVTSLLKTVKAVEDEATKGTRALEATTEHIRQELAVFCSPEPPAKTSTPEDFIRMTKGITMATAKAVAAGNSCRQEDVIATANLSRRAIADMLRACKEAAFHPEVAPDVRLRALHYGRECANGYLELLDHVLLTLQKPNPDLKQQLTGHSKRVAGSVTELIQAAEAMKGTEWVDPEDPTVIAENELLGAAAAIEAAAKKLEQLKPRAKPKEADESLNFEEQILEAAKSIAAATSALVKAASAAQRELVAQGKVGAIPANALDDGQWSQGLISAARMVAAATNNLCEAANAAVQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAVKRASDNLVKAAQKAAAFEDQENETVVVKEKMVGGIAQIIAAQEEMLRKERELEEARKKLAQIRQQQYKFLPSELRDEH [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Mus musculus [Accession]=MF7000105 [Entry] [Entry number]=301 [Entry name]=Dimerization domain of SARS [PDB ID]=2gib [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Nucleocapsid proteins [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is beta sheet augmentation between the monomers. It is likely that the N protein is not stable in the monomeric form and that higher oligomerization of the polypeptide is necessary to produce a stable conformation (PMID:16627473). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P59595 [UniProt boundaries chain A]=270-366 [UniProt coverage chain A]=22% [Name chain A]=Nucleoprotein [UniProt sequence chain A]=MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSGPDDQIGYYRRATRRVRGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNQLESKVSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAADMDDFSRQLQNSMSGASADSTQA [Source organism chain A]=Severe acute respiratory syndrome coronavirus [UniProt ID chain B]=P59595 [UniProt boundaries chain B]=274-369 [UniProt coverage chain B]=22% [Name chain B]=Nucleoprotein [UniProt sequence chain B]=MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSGPDDQIGYYRRATRRVRGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNQLESKVSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAADMDDFSRQLQNSMSGASADSTQA [Source organism chain B]=Severe acute respiratory syndrome coronavirus [ExpTech]=X-ray [Resolution]=1.75 [Source organism]=Severe acute respiratory syndrome coronavirus [Accession]=MF7000106 [Entry] [Entry number]=302 [Entry name]=C-terminal dimerization domain of SARS [PDB ID]=2jw8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Nucleocapsid proteins [Sequence domain]=Coronavirus nucleocapsid [Evidence level]=Direct evidence [Evidence text]=The CTD of nucleocapsid proteins forms a tightly intertwined dimer with an intermolecular four-stranded central β-sheet platform flanked by α-helices that buries a large surface. It is a dimer in solution even at very low concentrations (PMID:16775348, PMID:28331093). Thermal transition of the CTD was fully reversible and cooperative, with a van't Hoff enthalpy/calorimetric enthalpy ratio of 1.03, which implies two-state folding (PMID:25700263). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000946,MF7000107,MF7000947 [UniProt ID chain A]=P59595 [UniProt boundaries chain A]=248-365 [UniProt coverage chain A]=27% [Name chain A]=Nucleoprotein [UniProt sequence chain A]=MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSGPDDQIGYYRRATRRVRGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNQLESKVSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAADMDDFSRQLQNSMSGASADSTQA [Source organism chain A]=Severe acute respiratory syndrome coronavirus [UniProt ID chain B]=P59595 [UniProt boundaries chain B]=248-365 [UniProt coverage chain B]=27% [Name chain B]=Nucleoprotein [UniProt sequence chain B]=MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSGPDDQIGYYRRATRRVRGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNQLESKVSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAADMDDFSRQLQNSMSGASADSTQA [Source organism chain B]=Severe acute respiratory syndrome coronavirus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Severe acute respiratory syndrome coronavirus [Accession]=MF7000107 [Entry] [Entry number]=303 [Entry name]=Mitofusin domain of HR2 V686M/I708M mutant [PDB ID]=1t3j [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:15297672). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q811U4 [UniProt boundaries chain A]=674-735 [UniProt coverage chain A]=8% [Name chain A]=Mitofusin-1 [UniProt sequence chain A]=MAETVSPLKHFVLAKKAITAIFGQLLEFVTEGSHFVEATYRNPELDRIASEDDLVEIQGYRNKLAVIGEVLSRRHMKVAFFGRTSSGKSSVINAMLWDKVLPSGIGHTTNCFLSVEGTDGDKAYLMTEGSDEKKSVKTVNQLAHALHMDKDLKAGCLVHVFWPKAKCALLRDDLVLVDSPGTDVTTELDIWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERLSKPNIFILNNRWDASASEPEYMEDVRRQHMERCLHFLVEELKVVSPSEARNRIFFVSAKEVLNSRKHKAQGMPEGGGALAEGFQARLQEFQNFEQTFEECISQSAVKTKFEQHTIRAKQILDTVKNILDSVNVAAAEKRVYSMEEREDQIDRLDFIRNQMNLLTLDVKKKIKEVTEEVANKVSCAMTDEICRLSVLVDEFCSEFHPTPSVLKVYKSELNKHIEDGMGRNLADRCTNEVNASILQSQQEIIENLKPLLPAGIQNKLHTLIPCKKFDLSYDLNCHKLCSDFQEDIVFRFSLGWSSLVHRFLGSTNAQRVLLGLSEPIFQVPRSLASTPTAPSNPAAPDNAAQEELMITLITGLASLTSRTSMGIIVVGGVIWKTVGWKLISVTLSMYGALYLYERLTWTTRAKERAFKQQFVNYATEKLQMIVSFTSANCSHQVQQEMATTFARLCQQVDVTQKHLEEEIARLSKEIDQLEKIQNNSKLLRNKAVQLESELENFSKQFLHPSSGES [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=Q811U4 [UniProt boundaries chain A-2]=674-735 [UniProt coverage chain A-2]=8% [Name chain A-2]=Mitofusin-1 [UniProt sequence chain A-2]=MAETVSPLKHFVLAKKAITAIFGQLLEFVTEGSHFVEATYRNPELDRIASEDDLVEIQGYRNKLAVIGEVLSRRHMKVAFFGRTSSGKSSVINAMLWDKVLPSGIGHTTNCFLSVEGTDGDKAYLMTEGSDEKKSVKTVNQLAHALHMDKDLKAGCLVHVFWPKAKCALLRDDLVLVDSPGTDVTTELDIWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERLSKPNIFILNNRWDASASEPEYMEDVRRQHMERCLHFLVEELKVVSPSEARNRIFFVSAKEVLNSRKHKAQGMPEGGGALAEGFQARLQEFQNFEQTFEECISQSAVKTKFEQHTIRAKQILDTVKNILDSVNVAAAEKRVYSMEEREDQIDRLDFIRNQMNLLTLDVKKKIKEVTEEVANKVSCAMTDEICRLSVLVDEFCSEFHPTPSVLKVYKSELNKHIEDGMGRNLADRCTNEVNASILQSQQEIIENLKPLLPAGIQNKLHTLIPCKKFDLSYDLNCHKLCSDFQEDIVFRFSLGWSSLVHRFLGSTNAQRVLLGLSEPIFQVPRSLASTPTAPSNPAAPDNAAQEELMITLITGLASLTSRTSMGIIVVGGVIWKTVGWKLISVTLSMYGALYLYERLTWTTRAKERAFKQQFVNYATEKLQMIVSFTSANCSHQVQQEMATTFARLCQQVDVTQKHLEEEIARLSKEIDQLEKIQNNSKLLRNKAVQLESELENFSKQFLHPSSGES [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Mus musculus [Accession]=MF7000108 [Entry] [Entry number]=304 [Entry name]=Dimerization motif of Geminin [PDB ID]=1t6f [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:15313623). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O75496 [UniProt boundaries chain A]=109-145 [UniProt coverage chain A]=17% [Name chain A]=Geminin [UniProt sequence chain A]=MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O75496 [UniProt boundaries chain B]=109-145 [UniProt coverage chain B]=17% [Name chain B]=Geminin [UniProt sequence chain B]=MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.47 [Source organism]=Homo sapiens [Accession]=MF7000109 [Entry] [Entry number]=305 [Entry name]=SSV1 (F-93 form) [PDB ID]=1tbx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Winged helix-like DNA-binding domain and helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=Only dimeric form detected in solution according to SEC and chemical cross-linking (PMID:15479795). It belongs to the HTH subfamily of winged-helix DNA binding proteins (like SlyA and MarR). It has a coiled-coil-like dimerization region, like other similar transcriptional regulators (PMID:15479795). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P20222 [UniProt boundaries chain A]=3-93 [UniProt coverage chain A]=97% [Name chain A]=Protein F-93 [UniProt sequence chain A]=MKSTPFFYPEAIVLAYLYDNEGIATYDLYKKVNAEFPMSTATFYDAKKFLIQEGFVKERQERGEKRLYLTEKGKLFAISLKTAIETYKQIKKR [Source organism chain A]=Sulfolobus spindle-shape virus 1 [UniProt ID chain B]=P20222 [UniProt boundaries chain B]=2-91 [UniProt coverage chain B]=96% [Name chain B]=Protein F-93 [UniProt sequence chain B]=MKSTPFFYPEAIVLAYLYDNEGIATYDLYKKVNAEFPMSTATFYDAKKFLIQEGFVKERQERGEKRLYLTEKGKLFAISLKTAIETYKQIKKR [Source organism chain B]=Sulfolobus spindle-shape virus 1 [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Sulfolobus spindle-shape virus 1 [Accession]=MF7000110 [Entry] [Entry number]=306 [Entry name]=Coat protein from the GA bacteriophage [PDB ID]=1una [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Bacteriophage capsid proteins [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The dimers are stabilized by a large number of interactions. The dimer can therefore be regarded as the basic unit in the coat protein folding as well as of subunit packing at the assembly of the viral shell (PMID:8254664). The homologous coat protein dimer (CP2) is an obligate dimer (PMID:34339197). CP2 folds similarly to single-domain proteins populating only the folded and the unfolded ensembles, separated by a prominent folding free energy barrier. Several intramonomer contacts form early, but the CP2 folding barrier is crossed only when the intermonomer contacts are made (PMID:34339197). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P07234 [UniProt boundaries chain A]=2-130 [UniProt coverage chain A]=99% [Name chain A]=Capsid protein [UniProt sequence chain A]=MATLRSFVLVDNGGTGNVTVVPVSNANGVAEWLSNNSRSQAYRVTASYRASGADKRKYAIKLEVPKIVTQVVNGVELPGSAWKAYASIDLTIPIFAATDDVTVISKSLAGLFKVGNPIAEAISSQSGFYA [Source organism chain A]=Enterobacteria phage GA [UniProt ID chain B]=P07234 [UniProt boundaries chain B]=2-130 [UniProt coverage chain B]=99% [Name chain B]=Capsid protein [UniProt sequence chain B]=MATLRSFVLVDNGGTGNVTVVPVSNANGVAEWLSNNSRSQAYRVTASYRASGADKRKYAIKLEVPKIVTQVVNGVELPGSAWKAYASIDLTIPIFAATDDVTVISKSLAGLFKVGNPIAEAISSQSGFYA [Source organism chain B]=Enterobacteria phage GA [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Enterobacteria phage GA [Accession]=MF7000111 [Entry] [Entry number]=307 [Entry name]=C-terminal domain of the end-binding protein 1 (EB1) [PDB ID]=6evi [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=EB1-like C-terminal motif [Evidence level]=Direct evidence [Evidence text]=EB1 is a stable dimer with a parallel coiled coil and show that dimerization is essential for the formation of its C-terminal domain (EB1-C) (PMID:15616574). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100017,MF7000115,MF7000116,MF7000112,MF7000113 [UniProt ID chain A]=Q61166 [UniProt boundaries chain A]=191-260 [UniProt coverage chain A]=26% [Name chain A]=Microtubule-associated protein RP/EB family member 1 [UniProt sequence chain A]=MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKEYDPVAARQGQETAVAPSLVAPALSKPKKPLGSSTAAPQRPIATQRTTAAPKAGPGMVRKNPGVGNGDDEAAELMQQVKVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q61166 [UniProt boundaries chain B]=191-260 [UniProt coverage chain B]=26% [Name chain B]=Microtubule-associated protein RP/EB family member 1 [UniProt sequence chain B]=MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKEYDPVAARQGQETAVAPSLVAPALSKPKKPLGSSTAAPQRPIATQRTTAAPKAGPGMVRKNPGVGNGDDEAAELMQQVKVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY [Source organism chain B]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus [Accession]=MF7000112 [Entry] [Entry number]=308 [Entry name]=C-terminal domain of the end-binding protein 1 (EB1) [PDB ID]=6evq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=EB1-like C-terminal motif [Evidence level]=Direct evidence [Evidence text]=EB1 is a stable dimer with a parallel coiled coil and show that dimerization is essential for the formation of its C-terminal domain (EB1-C) (PMID:15616574). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100017,MF7000115,MF7000116,MF7000112,MF7000113 [UniProt ID chain A]=Q61166 [UniProt boundaries chain A]=191-260 [UniProt coverage chain A]=26% [Name chain A]=Microtubule-associated protein RP/EB family member 1 [UniProt sequence chain A]=MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKEYDPVAARQGQETAVAPSLVAPALSKPKKPLGSSTAAPQRPIATQRTTAAPKAGPGMVRKNPGVGNGDDEAAELMQQVKVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q61166 [UniProt boundaries chain B]=191-260 [UniProt coverage chain B]=26% [Name chain B]=Microtubule-associated protein RP/EB family member 1 [UniProt sequence chain B]=MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKEYDPVAARQGQETAVAPSLVAPALSKPKKPLGSSTAAPQRPIATQRTTAAPKAGPGMVRKNPGVGNGDDEAAELMQQVKVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY [Source organism chain B]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus [Accession]=MF7000113 [Entry] [Entry number]=309 [Entry name]=EB1-like motif of Bim1p [PDB ID]=4e61 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=EB1-like C-terminal motif [Evidence level]=Direct evidence [Evidence text]=EB1 is a stable dimer with a parallel coiled coil and show that dimerization is essential for the formation of its C-terminal domain (EB1-C) (PMID:15616574). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100017,MF7000115,MF7000116,MF7000112,MF7000113 [UniProt ID chain A]=P40013 [UniProt boundaries chain A]=182-281 [UniProt coverage chain A]=29% [Name chain A]=Protein BIM1 [UniProt sequence chain A]=MSAGIGESRTELLTWLNGLLNLNYKKIEECGTGAAYCQIMDSIYGDLPMNRVKFNATAEYEFQTNYKILQSCFSRHGIEKTVYVDKLIRCKFQDNLEFLQWLKKHWIRHKDESVYDPDARRKYRPIITNNSATKPRTVSNPTTAKRSSSTGTGSAMSGGLATRHSSLGINGSRKTSVTQGQLVAIQAELTKSQETIGSLNEEIEQYKGTVSTLEIEREFYFNKLRDIEILVHTTQDLINEGVYKFNDETITGHGNGNGGALLRFVKKVESILYATAEGFEMNDGEDELNDKNLGEHGTVPNQGGYANSNGEVNGNEGSNHDVIMQNDEGEVGVSNNLIIDEETF [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P40013 [UniProt boundaries chain B]=182-276 [UniProt coverage chain B]=27% [Name chain B]=Protein BIM1 [UniProt sequence chain B]=MSAGIGESRTELLTWLNGLLNLNYKKIEECGTGAAYCQIMDSIYGDLPMNRVKFNATAEYEFQTNYKILQSCFSRHGIEKTVYVDKLIRCKFQDNLEFLQWLKKHWIRHKDESVYDPDARRKYRPIITNNSATKPRTVSNPTTAKRSSSTGTGSAMSGGLATRHSSLGINGSRKTSVTQGQLVAIQAELTKSQETIGSLNEEIEQYKGTVSTLEIEREFYFNKLRDIEILVHTTQDLINEGVYKFNDETITGHGNGNGGALLRFVKKVESILYATAEGFEMNDGEDELNDKNLGEHGTVPNQGGYANSNGEVNGNEGSNHDVIMQNDEGEVGVSNNLIIDEETF [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.45 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000115 [Entry] [Entry number]=310 [Entry name]=EB1-like domain of Mal3 [PDB ID]=5m97 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=EB1-like C-terminal motif [Evidence level]=Direct evidence [Evidence text]=EB1 is a stable dimer with a parallel coiled coil and show that dimerization is essential for the formation of its C-terminal domain (EB1-C) (PMID:15616574). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF2100017,MF7000115,MF7000116,MF7000112,MF7000113 [UniProt ID chain B]=Q10113 [UniProt boundaries chain B]=176-242 [UniProt coverage chain B]=21% [Name chain B]=Microtubule integrity protein mal3 [UniProt sequence chain B]=MSESRQELLAWINQVTSLGLTRIEDCGKGYAMIQIFDSIYQDIPLKKVNFECNNEYQYINNWKVLQQVFLKKGIDKVVDPERLSRCKMQDNLEFVQWAKRFWDQYYPGGDYDALARRGNRGPANTRVMNSSAGATGPSRRRQVSSGSSTPSMTKSSANNNNVSSTANTAAVLRAKQAQQQITSLETQLYEVNETMFGLERERDFYFNKLREIEILVQTHLTTSPMSMENMLERIQAILYSTEDGFELPPDQPADLTTALTDHDTNNVAEEAQMTDLKDSETQRVPSAPDFVHARLQSLEVDDDENITF [Source organism chain B]=Schizosaccharomyces pombe [UniProt ID chain A]=Q10113 [UniProt boundaries chain A]=176-240 [UniProt coverage chain A]=21% [Name chain A]=Microtubule integrity protein mal3 [UniProt sequence chain A]=MSESRQELLAWINQVTSLGLTRIEDCGKGYAMIQIFDSIYQDIPLKKVNFECNNEYQYINNWKVLQQVFLKKGIDKVVDPERLSRCKMQDNLEFVQWAKRFWDQYYPGGDYDALARRGNRGPANTRVMNSSAGATGPSRRRQVSSGSSTPSMTKSSANNNNVSSTANTAAVLRAKQAQQQITSLETQLYEVNETMFGLERERDFYFNKLREIEILVQTHLTTSPMSMENMLERIQAILYSTEDGFELPPDQPADLTTALTDHDTNNVAEEAQMTDLKDSETQRVPSAPDFVHARLQSLEVDDDENITF [Source organism chain A]=Schizosaccharomyces pombe [ExpTech]=X-ray [Resolution]=1.33 [Source organism]=Schizosaccharomyces pombe [Accession]=MF7000116 [Entry] [Entry number]=311 [Entry name]=Kinase recruitment domain of RsbU [PDB ID]=1w53 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=KaiA/RbsU domain [Sequence domain]=KaiA/RbsU domain [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The crystal structure of the N-terminal domain of RsbU reveals that only a dimeric form of RsbU can form what we believe to be an RsbT-binding surface. Deletion of the N-terminal part of rsbU or mutation in the dimer interface, has deleterious effects on he stress response of B. subtilis, presumably because the dimer form of RsbU is destroyed (PMID:15263010). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000117,MF7000118,MF7000119 [UniProt ID chain A]=P40399 [UniProt boundaries chain A]=1-84 [UniProt coverage chain A]=25% [Name chain A]=Phosphoserine phosphatase RsbU [UniProt sequence chain A]=MDFREVIEQRYHQLLSRYIAELTETSLYQAQKFSRKTIEHQIPPEEIISIHRKVLKELYPSLPEDVFHSLDFLIEVMIGYGMAYQEHQTLRGIQQEIKSEIEIAANVQQTLLGTKVPQEEALDIGAISVPAKQMSGDYYHFVKDKESINIAIADVIGKGIPAALCMSMIKYAMDSLPETGIHPSQVLKNLNRVVEQNVDASMFITMFYANYNMDKHQFTYASAGHEPGFYYSQKDNTFYDLEAKGLVLGISQDYDYKQFDQHLEKGDMIVLFSDGVTECRTENGFLERPDLQKLIEEHMCSSAQEMVKNIYDSLLKLQDFQLHDDFTLIVLRRKV [Source organism chain A]=Bacillus subtilis [UniProt ID chain A-2]=P40399 [UniProt boundaries chain A-2]=1-84 [UniProt coverage chain A-2]=25% [Name chain A-2]=Phosphoserine phosphatase RsbU [UniProt sequence chain A-2]=MDFREVIEQRYHQLLSRYIAELTETSLYQAQKFSRKTIEHQIPPEEIISIHRKVLKELYPSLPEDVFHSLDFLIEVMIGYGMAYQEHQTLRGIQQEIKSEIEIAANVQQTLLGTKVPQEEALDIGAISVPAKQMSGDYYHFVKDKESINIAIADVIGKGIPAALCMSMIKYAMDSLPETGIHPSQVLKNLNRVVEQNVDASMFITMFYANYNMDKHQFTYASAGHEPGFYYSQKDNTFYDLEAKGLVLGISQDYDYKQFDQHLEKGDMIVLFSDGVTECRTENGFLERPDLQKLIEEHMCSSAQEMVKNIYDSLLKLQDFQLHDDFTLIVLRRKV [Source organism chain A-2]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Bacillus subtilis [Accession]=MF7000117 [Entry] [Entry number]=312 [Entry name]=Phosphoserine phosphatase RsbU [PDB ID]=2j6z [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=KaiA/RbsU domain [Sequence domain]=KaiA/RbsU domain [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The crystal structure of the N-terminal domain of RsbU reveals that only a dimeric form of RsbU can form what we believe to be an RsbT-binding surface. Deletion of the N-terminal part of rsbU or mutation in the dimer interface, has deleterious effects on he stress response of B. subtilis, presumably because the dimer form of RsbU is destroyed (PMID:15263010). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000117,MF7000118,MF7000119 [UniProt ID chain A]=P40399 [UniProt boundaries chain A]=1-86 [UniProt coverage chain A]=25% [Name chain A]=Phosphoserine phosphatase RsbU [UniProt sequence chain A]=MDFREVIEQRYHQLLSRYIAELTETSLYQAQKFSRKTIEHQIPPEEIISIHRKVLKELYPSLPEDVFHSLDFLIEVMIGYGMAYQEHQTLRGIQQEIKSEIEIAANVQQTLLGTKVPQEEALDIGAISVPAKQMSGDYYHFVKDKESINIAIADVIGKGIPAALCMSMIKYAMDSLPETGIHPSQVLKNLNRVVEQNVDASMFITMFYANYNMDKHQFTYASAGHEPGFYYSQKDNTFYDLEAKGLVLGISQDYDYKQFDQHLEKGDMIVLFSDGVTECRTENGFLERPDLQKLIEEHMCSSAQEMVKNIYDSLLKLQDFQLHDDFTLIVLRRKV [Source organism chain A]=Bacillus subtilis [UniProt ID chain A-2]=P40399 [UniProt boundaries chain A-2]=1-86 [UniProt coverage chain A-2]=25% [Name chain A-2]=Phosphoserine phosphatase RsbU [UniProt sequence chain A-2]=MDFREVIEQRYHQLLSRYIAELTETSLYQAQKFSRKTIEHQIPPEEIISIHRKVLKELYPSLPEDVFHSLDFLIEVMIGYGMAYQEHQTLRGIQQEIKSEIEIAANVQQTLLGTKVPQEEALDIGAISVPAKQMSGDYYHFVKDKESINIAIADVIGKGIPAALCMSMIKYAMDSLPETGIHPSQVLKNLNRVVEQNVDASMFITMFYANYNMDKHQFTYASAGHEPGFYYSQKDNTFYDLEAKGLVLGISQDYDYKQFDQHLEKGDMIVLFSDGVTECRTENGFLERPDLQKLIEEHMCSSAQEMVKNIYDSLLKLQDFQLHDDFTLIVLRRKV [Source organism chain A-2]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Bacillus subtilis [Accession]=MF7000118 [Entry] [Entry number]=313 [Entry name]=Phosphoserine phosphatase RsbU [PDB ID]=2j70 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=KaiA/RbsU domain [Sequence domain]=KaiA/RbsU domain [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The crystal structure of the N-terminal domain of RsbU reveals that only a dimeric form of RsbU can form what we believe to be an RsbT-binding surface. Deletion of the N-terminal part of rsbU or mutation in the dimer interface, has deleterious effects on he stress response of B. subtilis, presumably because the dimer form of RsbU is destroyed (PMID:15263010). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000117,MF7000118,MF7000119 [UniProt ID chain A]=P40399 [UniProt boundaries chain A]=1-83 [UniProt coverage chain A]=24% [Name chain A]=Phosphoserine phosphatase RsbU [UniProt sequence chain A]=MDFREVIEQRYHQLLSRYIAELTETSLYQAQKFSRKTIEHQIPPEEIISIHRKVLKELYPSLPEDVFHSLDFLIEVMIGYGMAYQEHQTLRGIQQEIKSEIEIAANVQQTLLGTKVPQEEALDIGAISVPAKQMSGDYYHFVKDKESINIAIADVIGKGIPAALCMSMIKYAMDSLPETGIHPSQVLKNLNRVVEQNVDASMFITMFYANYNMDKHQFTYASAGHEPGFYYSQKDNTFYDLEAKGLVLGISQDYDYKQFDQHLEKGDMIVLFSDGVTECRTENGFLERPDLQKLIEEHMCSSAQEMVKNIYDSLLKLQDFQLHDDFTLIVLRRKV [Source organism chain A]=Bacillus subtilis [UniProt ID chain A-2]=P40399 [UniProt boundaries chain A-2]=1-83 [UniProt coverage chain A-2]=24% [Name chain A-2]=Phosphoserine phosphatase RsbU [UniProt sequence chain A-2]=MDFREVIEQRYHQLLSRYIAELTETSLYQAQKFSRKTIEHQIPPEEIISIHRKVLKELYPSLPEDVFHSLDFLIEVMIGYGMAYQEHQTLRGIQQEIKSEIEIAANVQQTLLGTKVPQEEALDIGAISVPAKQMSGDYYHFVKDKESINIAIADVIGKGIPAALCMSMIKYAMDSLPETGIHPSQVLKNLNRVVEQNVDASMFITMFYANYNMDKHQFTYASAGHEPGFYYSQKDNTFYDLEAKGLVLGISQDYDYKQFDQHLEKGDMIVLFSDGVTECRTENGFLERPDLQKLIEEHMCSSAQEMVKNIYDSLLKLQDFQLHDDFTLIVLRRKV [Source organism chain A-2]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Bacillus subtilis [Accession]=MF7000119 [Entry] [Entry number]=314 [Entry name]=CFP-10/ESAT-6 complex [PDB ID]=1wa8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Proteins of 100 residues with WXG [Evidence level]=Direct evidence [Evidence text]=Predicted coiled coil and validated disordered segments make up more than 50% of the structure. Antiparallel coiled-coil monomers form a four-helix bundle. Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815). The well-defined core of the CFP-10·ESAT-6 complex consists of two similar helix–turn–helix hairpin structures formed from the individual proteins, which have an extensive hydrophobic contact surface and lie antiparallel to each other to form a four-helix bundle (PMID:15973432). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000120,MF7000928,MF7000929 [UniProt ID chain A]=P0A567 [UniProt boundaries chain A]=2-100 [UniProt coverage chain A]=99% [Name chain A]=ESAT-6-like protein EsxB [UniProt sequence chain A]=MAEMKTDAATLAQEAGNFERISGDLKTQIDQVESTAGSLQGQWRGAAGTAAQAAVVRFQEAANKQKQELDEISTNIRQAGVQYSRADEEQQQALSSQMGF [Source organism chain A]=Mycobacterium bovis [UniProt ID chain B]=P9WNK7 [UniProt boundaries chain B]=1-95 [UniProt coverage chain B]=100% [Name chain B]=6 kDa early secretory antigenic target [UniProt sequence chain B]=MTEQQWNFAGIEAAASAIQGNVTSIHSLLDEGKQSLTKLAAAWGGSGSEAYQGVQQKWDATATELNNALQNLARTISEAGQAMASTEGNVTGMFA [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mycobacterium tuberculosis ;Mycobacterium bovis [Accession]=MF7000120 [Entry] [Entry number]=315 [Entry name]=Growth and Differentiation Factor 5 mutant R399E [PDB ID]=7zjf [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P43026 [UniProt boundaries chain A]=397-501 [UniProt coverage chain A]=20% [Name chain A]=Growth/differentiation factor 5 [UniProt sequence chain A]=MRLPKLLTFLLWYLAWLDLEFICTVLGAPDLGQRPQGTRPGLAKAEAKERPPLARNVFRPGGHSYGGGATNANARAKGGTGQTGGLTQPKKDEPKKLPPRPGGPEPKPGHPPQTRQATARTVTPKGQLPGGKAPPKAGSVPSSFLLKKAREPGPPREPKEPFRPPPITPHEYMLSLYRTLSDADRKGGNSSVKLEAGLANTITSFIDKGQDDRGPVVRKQRYVFDISALEKDGLLGAELRILRKKPSDTAKPAAPGGGRAAQLKLSSCPSGRQPAALLDVRSVPGLDGSGWEVFDIWKLFRNFKNSAQLCLELEAWERGRAVDLRGLGFDRAARQVHEKALFLVFGRTKKRDLFFNEIKARSGQDDKTVYEYLFSQRRKRRAPLATRQGKRPSKNLKARCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVPTRLSPISILFIDSANNVVYKQYEDMVVESCGCR [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P43026 [UniProt boundaries chain B]=383-501 [UniProt coverage chain B]=23% [Name chain B]=Growth/differentiation factor 5 [UniProt sequence chain B]=MRLPKLLTFLLWYLAWLDLEFICTVLGAPDLGQRPQGTRPGLAKAEAKERPPLARNVFRPGGHSYGGGATNANARAKGGTGQTGGLTQPKKDEPKKLPPRPGGPEPKPGHPPQTRQATARTVTPKGQLPGGKAPPKAGSVPSSFLLKKAREPGPPREPKEPFRPPPITPHEYMLSLYRTLSDADRKGGNSSVKLEAGLANTITSFIDKGQDDRGPVVRKQRYVFDISALEKDGLLGAELRILRKKPSDTAKPAAPGGGRAAQLKLSSCPSGRQPAALLDVRSVPGLDGSGWEVFDIWKLFRNFKNSAQLCLELEAWERGRAVDLRGLGFDRAARQVHEKALFLVFGRTKKRDLFFNEIKARSGQDDKTVYEYLFSQRRKRRAPLATRQGKRPSKNLKARCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVPTRLSPISILFIDSANNVVYKQYEDMVVESCGCR [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.30 [Source organism]=Homo sapiens [Accession]=MF7000121 [Entry] [Entry number]=316 [Entry name]=Growth and differentiation factor 15 [PDB ID]=5vt2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=Q99988 [UniProt boundaries chain A]=201-308 [UniProt coverage chain A]=35% [Name chain A]=Growth/differentiation factor 15 [UniProt sequence chain A]=MPGQELRTVNGSQMLLVLLVLSWLPHGGALSLAEASRASFPGPSELHSEDSRFRELRKRYEDLLTRLRANQSWEDSNTDLVPAPAVRILTPEVRLGSGGHLHLRISRAALPEGLPEASRLHRALFRLSPTASRSWDVTRPLRRQLSLARPQAPALHLRLSPPPSQSDQLLAESSSARPQLELHLRPQAARGRRRARARNGDHCPLGPGRCCRLHTVRASLEDLGWADWVLSPREVQVTMCIGACPSQFRAANMHAQIKTSLHRLKPDTVPAPCCVPASYNPMVLIQKTDTGVSLQTYDDLLAKDCHCI [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q99988 [UniProt boundaries chain B]=201-308 [UniProt coverage chain B]=35% [Name chain B]=Growth/differentiation factor 15 [UniProt sequence chain B]=MPGQELRTVNGSQMLLVLLVLSWLPHGGALSLAEASRASFPGPSELHSEDSRFRELRKRYEDLLTRLRANQSWEDSNTDLVPAPAVRILTPEVRLGSGGHLHLRISRAALPEGLPEASRLHRALFRLSPTASRSWDVTRPLRRQLSLARPQAPALHLRLSPPPSQSDQLLAESSSARPQLELHLRPQAARGRRRARARNGDHCPLGPGRCCRLHTVRASLEDLGWADWVLSPREVQVTMCIGACPSQFRAANMHAQIKTSLHRLKPDTVPAPCCVPASYNPMVLIQKTDTGVSLQTYDDLLAKDCHCI [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Homo sapiens [Accession]=MF7000122 [Entry] [Entry number]=317 [Entry name]=Growth and differentiation factor 15 [PDB ID]=5vz3 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=Q99988 [UniProt boundaries chain A]=201-308 [UniProt coverage chain A]=35% [Name chain A]=Growth/differentiation factor 15 [UniProt sequence chain A]=MPGQELRTVNGSQMLLVLLVLSWLPHGGALSLAEASRASFPGPSELHSEDSRFRELRKRYEDLLTRLRANQSWEDSNTDLVPAPAVRILTPEVRLGSGGHLHLRISRAALPEGLPEASRLHRALFRLSPTASRSWDVTRPLRRQLSLARPQAPALHLRLSPPPSQSDQLLAESSSARPQLELHLRPQAARGRRRARARNGDHCPLGPGRCCRLHTVRASLEDLGWADWVLSPREVQVTMCIGACPSQFRAANMHAQIKTSLHRLKPDTVPAPCCVPASYNPMVLIQKTDTGVSLQTYDDLLAKDCHCI [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q99988 [UniProt boundaries chain A-2]=201-308 [UniProt coverage chain A-2]=35% [Name chain A-2]=Growth/differentiation factor 15 [UniProt sequence chain A-2]=MPGQELRTVNGSQMLLVLLVLSWLPHGGALSLAEASRASFPGPSELHSEDSRFRELRKRYEDLLTRLRANQSWEDSNTDLVPAPAVRILTPEVRLGSGGHLHLRISRAALPEGLPEASRLHRALFRLSPTASRSWDVTRPLRRQLSLARPQAPALHLRLSPPPSQSDQLLAESSSARPQLELHLRPQAARGRRRARARNGDHCPLGPGRCCRLHTVRASLEDLGWADWVLSPREVQVTMCIGACPSQFRAANMHAQIKTSLHRLKPDTVPAPCCVPASYNPMVLIQKTDTGVSLQTYDDLLAKDCHCI [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.97 [Source organism]=Homo sapiens [Accession]=MF7000123 [Entry] [Entry number]=318 [Entry name]=Endophilin A1 BAR domain (rat) [PDB ID]=2c08 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=N-BAR domain [Sequence domain]=N-BAR domain [Evidence level]=Direct evidence [Evidence text]=The human AmphyphisinII/Bin1 and Endophilin BAR domains (N-BARs) display two-state equilibrium unfolding from the dimeric to unfolded monomeric forms (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000916,MF7000125,MF7000126,MF7000124 [UniProt ID chain A]=O35179 [UniProt boundaries chain A]=25-247 [UniProt coverage chain A]=63% [Name chain A]=Endophilin-A1 [UniProt sequence chain A]=MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDGTQPNGGLSHTGTPKPAGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH [Source organism chain A]=Rattus norvegicus [UniProt ID chain A-2]=O35179 [UniProt boundaries chain A-2]=25-247 [UniProt coverage chain A-2]=63% [Name chain A-2]=Endophilin-A1 [UniProt sequence chain A-2]=MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDGTQPNGGLSHTGTPKPAGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH [Source organism chain A-2]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=2.90 [Source organism]=Rattus norvegicus [Accession]=MF7000124 [Entry] [Entry number]=319 [Entry name]=Endophilin-A1 BAR domain (mouse) [PDB ID]=1zww [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=N-BAR domain [Sequence domain]=N-BAR domain [Evidence level]=Direct evidence [Evidence text]=The human AmphyphisinII/Bin1 and Endophilin BAR domains (N-BARs) display two-state equilibrium unfolding from the dimeric to unfolded monomeric forms (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000916,MF7000125,MF7000126,MF7000124 [UniProt ID chain A]=Q62420 [UniProt boundaries chain A]=27-246 [UniProt coverage chain A]=62% [Name chain A]=Endophilin-A1 [UniProt sequence chain A]=MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDSTQPNGGLSHTGTPKPPGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q62420 [UniProt boundaries chain B]=28-247 [UniProt coverage chain B]=62% [Name chain B]=Endophilin-A1 [UniProt sequence chain B]=MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDSTQPNGGLSHTGTPKPPGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Mus musculus [Accession]=MF7000125 [Entry] [Entry number]=320 [Entry name]=Endophilin BAR domain (human) [PDB ID]=1x03 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=N-BAR domain [Sequence domain]=N-BAR domain [Evidence level]=Direct evidence [Evidence text]=The human AmphyphisinII/Bin1 and Endophilin BAR domains (N-BARs) display two-state equilibrium unfolding from the dimeric to unfolded monomeric forms (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000916,MF7000125,MF7000126,MF7000124 [UniProt ID chain A]=Q99962 [UniProt boundaries chain A]=26-247 [UniProt coverage chain A]=63% [Name chain A]=Endophilin-A1 [UniProt sequence chain A]=MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFPTGDSTQPNGGLSHTGTPKPSGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGHSGFFPINYVEILVALPH [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q99962 [UniProt boundaries chain A-2]=26-247 [UniProt coverage chain A-2]=63% [Name chain A-2]=Endophilin-A1 [UniProt sequence chain A-2]=MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFPTGDSTQPNGGLSHTGTPKPSGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGHSGFFPINYVEILVALPH [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.10 [Source organism]=Homo sapiens [Accession]=MF7000126 [Entry] [Entry number]=321 [Entry name]=Histone H3/ING3 complex [PDB ID]=8cok [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Inhibitor of growth proteins N-terminal histone-binding [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:37148949). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100005,MF7000127 [UniProt ID chain A]=Q9NXR8 [UniProt boundaries chain A]=1-97 [UniProt coverage chain A]=23% [Name chain A]=Inhibitor of growth protein 3 [UniProt sequence chain A]=MLYLEDYLEMIEQLPMDLRDRFTEMREMDLQVQNAMDQLEQRVSEFFMNAKKNKPEWREEQMASIKKDYYKALEDADEKVQLANQIYDLVDRHLRKLDQELAKFKMELEADNAGITEILERRSLELDTPSQPVNNHHAHSHTPVEKRKYNPTSHHTTTDHIPEKKFKSEALLSTLTSDASKENTLGCRNNNSTASSNNAYNVNSSQPLGSYNIGSLSSGTGAGAITMAAAQAVQATAQMKEGRRTSSLKASYEAFKNNDFQLGKEFSMARETVGYSSSSALMTTLTQNASSSAADSRSGRKSKNNNKSSSQQSSSSSSSSSLSSCSSSSTVVQEISQQTTVVPESDSNSQVDWTYDPNEPRYCICNQVSYGEMVGCDNQDCPIEWFHYGCVGLTEAPKGKWYCPQCTAAMKRRGSRHK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9NXR8 [UniProt boundaries chain B]=1-100 [UniProt coverage chain B]=23% [Name chain B]=Inhibitor of growth protein 3 [UniProt sequence chain B]=MLYLEDYLEMIEQLPMDLRDRFTEMREMDLQVQNAMDQLEQRVSEFFMNAKKNKPEWREEQMASIKKDYYKALEDADEKVQLANQIYDLVDRHLRKLDQELAKFKMELEADNAGITEILERRSLELDTPSQPVNNHHAHSHTPVEKRKYNPTSHHTTTDHIPEKKFKSEALLSTLTSDASKENTLGCRNNNSTASSNNAYNVNSSQPLGSYNIGSLSSGTGAGAITMAAAQAVQATAQMKEGRRTSSLKASYEAFKNNDFQLGKEFSMARETVGYSSSSALMTTLTQNASSSAADSRSGRKSKNNNKSSSQQSSSSSSSSSLSSCSSSSTVVQEISQQTTVVPESDSNSQVDWTYDPNEPRYCICNQVSYGEMVGCDNQDCPIEWFHYGCVGLTEAPKGKWYCPQCTAAMKRRGSRHK [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.91 [Source organism]=Homo sapiens [Accession]=MF7000127 [Entry] [Entry number]=322 [Entry name]=ZNF174 SCAN domain [PDB ID]=1y7q [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=SCAN domain [Sequence domain]=SCAN domain [Evidence level]=Direct evidence [Evidence text]=The SCAN domain is a domain-swapped dimer that encompasses an independently folding protein module of 10 helices with five helical segments coming from each monomer. Thermal denaturation studies of ZNF174 showed that the SCAN domain exhibits two-state folding behavior in which folded dimer appears to be in equilibrium with unfolded monomer (PMID:16950398, PMID:11741982). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000128,MF7000129,MF7000130 [UniProt ID chain A]=Q15697 [UniProt boundaries chain A]=37-132 [UniProt coverage chain A]=23% [Name chain A]=Zinc finger protein 174 [UniProt sequence chain A]=MAAKMEITLSSNTEASSKQERHIIAKLEEKRGPPLQKNCPDPELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLVEDFHRASKKPKQWVAVCMQGQKVLLEKTGSQLGEQELPDFQPQTPRRDLRESSPAEPSQAGAYDRLSPHHWEKSPLLQEPTPKLAGTEAPRMRSDNKENPQQEGAKGAKPCAVSAGRSKGNGLQNPEPRGANMSEPRLSRRQVSSPNAQKPFAHYQRHCRVEYISSPLKSHPLRELKKSKGGKRSLSNRLQHLGHQPTRSAKKPYKCDDCGKSFTWNSELKRHKRVHTGERPYTCGECGNCFGRQSTLKLHQRIHTGEKPYQCGQCGKSFRQSSNLHQHHRLHHGD [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q15697 [UniProt boundaries chain B]=37-132 [UniProt coverage chain B]=23% [Name chain B]=Zinc finger protein 174 [UniProt sequence chain B]=MAAKMEITLSSNTEASSKQERHIIAKLEEKRGPPLQKNCPDPELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLVEDFHRASKKPKQWVAVCMQGQKVLLEKTGSQLGEQELPDFQPQTPRRDLRESSPAEPSQAGAYDRLSPHHWEKSPLLQEPTPKLAGTEAPRMRSDNKENPQQEGAKGAKPCAVSAGRSKGNGLQNPEPRGANMSEPRLSRRQVSSPNAQKPFAHYQRHCRVEYISSPLKSHPLRELKKSKGGKRSLSNRLQHLGHQPTRSAKKPYKCDDCGKSFTWNSELKRHKRVHTGERPYTCGECGNCFGRQSTLKLHQRIHTGEKPYQCGQCGKSFRQSSNLHQHHRLHHGD [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000128 [Entry] [Entry number]=323 [Entry name]=MZF1 SCAN domain [PDB ID]=2fi2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=SCAN domain [Sequence domain]=SCAN domain [Evidence level]=Direct evidence [Evidence text]=The SCAN domain is a domain-swapped dimer that encompasses an independently folding protein module of 10 helices with five helical segments coming from each monomer. Thermal denaturation studies of ZNF174 showed that the SCAN domain exhibits two-state folding behavior in which folded dimer appears to be in equilibrium with unfolded monomer (PMID:16950398, PMID:11741982). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000128,MF7000129,MF7000130 [UniProt ID chain A]=P28698 [UniProt boundaries chain A]=37-128 [UniProt coverage chain A]=12% [Name chain A]=Myeloid zinc finger 1 [UniProt sequence chain A]=MRPAVLGSPDRAPPEDEGPVMVKLEDSEEEGEAALWDPGPEAARLRFRCFRYEEATGPQEALAQLRELCRQWLRPEVRSKEQMLELLVLEQFLGALPPEIQARVQGQRPGSPEEAAALVDGLRREPGGPRRWVTVQVQGQEVLSEKMEPSSFQPLPETEPPTPEPGPKTPPRTMQESPLGLQVKEESEVTEDSDFLESGPLAATQESVPTLLPEEAQRCGTVLDQIFPHSKTGPEGPSWREHPRALWHEEAGGIFSPGFALQLGSISAGPGSVSPHLHVPWDLGMAGLSGQIQSPSREGGFAHALLLPSDLRSEQDPTDEDPCRGVGPALITTRWRSPRGRSRGRPSTGGGVVRGGRCDVCGKVFSQRSNLLRHQKIHTGERPFVCSECGRSFSRSSHLLRHQLTHTEERPFVCGDCGQGFVRSARLEEHRRVHTGEQPFRCAECGQSFRQRSNLLQHQRIHGDPPGPGAKPPAPPGAPEPPGPFPCSECRESFARRAVLLEHQAVHTGDKSFGCVECGERFGRRSVLLQHRRVHSGERPFACAECGQSFRQRSNLTQHRRIHTGERPFACAECGKAFRQRPTLTQHLRVHTGEKPFACPECGQRFSQRLKLTRHQRTHTGEKPYHCGECGLGFTQVSRLTEHQRIHTGERPFACPECGQSFRQHANLTQHRRIHTGERPYACPECGKAFRQRPTLTQHLRTHRREKPFACQDCGRRFHQSTKLIQHQRVHSAE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P28698 [UniProt boundaries chain B]=37-128 [UniProt coverage chain B]=12% [Name chain B]=Myeloid zinc finger 1 [UniProt sequence chain B]=MRPAVLGSPDRAPPEDEGPVMVKLEDSEEEGEAALWDPGPEAARLRFRCFRYEEATGPQEALAQLRELCRQWLRPEVRSKEQMLELLVLEQFLGALPPEIQARVQGQRPGSPEEAAALVDGLRREPGGPRRWVTVQVQGQEVLSEKMEPSSFQPLPETEPPTPEPGPKTPPRTMQESPLGLQVKEESEVTEDSDFLESGPLAATQESVPTLLPEEAQRCGTVLDQIFPHSKTGPEGPSWREHPRALWHEEAGGIFSPGFALQLGSISAGPGSVSPHLHVPWDLGMAGLSGQIQSPSREGGFAHALLLPSDLRSEQDPTDEDPCRGVGPALITTRWRSPRGRSRGRPSTGGGVVRGGRCDVCGKVFSQRSNLLRHQKIHTGERPFVCSECGRSFSRSSHLLRHQLTHTEERPFVCGDCGQGFVRSARLEEHRRVHTGEQPFRCAECGQSFRQRSNLLQHQRIHGDPPGPGAKPPAPPGAPEPPGPFPCSECRESFARRAVLLEHQAVHTGDKSFGCVECGERFGRRSVLLQHRRVHSGERPFACAECGQSFRQRSNLTQHRRIHTGERPFACAECGKAFRQRPTLTQHLRVHTGEKPFACPECGQRFSQRLKLTRHQRTHTGEKPYHCGECGLGFTQVSRLTEHQRIHTGERPFACPECGQSFRQHANLTQHRRIHTGERPYACPECGKAFRQRPTLTQHLRTHRREKPFACQDCGRRFHQSTKLIQHQRVHSAE [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000129 [Entry] [Entry number]=324 [Entry name]=Zfp206 SCAN domain [PDB ID]=4e6s [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=SCAN domain [Sequence domain]=SCAN domain [Evidence level]=Direct evidence [Evidence text]=The SCAN domain is a domain-swapped dimer that encompasses an independently folding protein module of 10 helices with five helical segments coming from each monomer. Thermal denaturation studies of ZNF174 showed that the SCAN domain exhibits two-state folding behavior in which folded dimer appears to be in equilibrium with unfolded monomer (PMID:16950398, PMID:11741982). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000128,MF7000129,MF7000130 [UniProt ID chain A]=Q3URR7 [UniProt boundaries chain A]=35-120 [UniProt coverage chain A]=10% [Name chain A]=Zinc finger and SCAN domain-containing protein 10 [UniProt sequence chain A]=MLAEPVPDALEQEHPGAVKLEEDEVGEEDPRLAESRPRPEVAHQLFRCFQYQEDMGPRASLGRLRELCNHWLRPALHTKKQILELLVLEQFLSVLPPHVLSRLHGQPLRDGEEVVQLLEGVPRDISHMGPLDFSFSAGKNAPADIISEEQNSPSQVPSHSPQTELPSEEIPALHPLNELPPPQPAPIRPAEPEEWRLAPSSNWPMSPEPQEILQDPRESNPSQGPSWLEENSRDQELAAVLESLTFEDTSEKRAWPANPLGFGSRMPDNEELKVEEPKVTTWPVVIGAESQTEKPEVAGEPLTQTVGQETSSTGWGGTPADGSEVVKVRGASDAPEPQGEMQFICTYCGVNFPEMSHLQAHQLQSHPNLQPHPSSRSFRCLWCGKTFGRSSILKLHMRTHTDERPHACHLCNRRFRQSSHLTKHLLTHSSEPAFRCAECNQGFQRRSSLMQHLLAHAQGKNLTPNPEGKTKVPEMAAVLCSHCGQTFKRRSSLKRHLRNHAKDKDHLSSEDPGSLSSSQESNPYVCSDCGKAFRQSEQLMIHTRRVHTRERPFSCQVCGRCFTQNSQLISHQQIHTGEKPHACPQCSKRFVRRAGLARHLLTHGSLRPYHCAQCGKSFRQMRDLTRHVRCHTGEKPCRCNECGEGFTQNAHLARHQRIHTGEKPHACDICGHRFRNSSNLARHRRSHTGERPYSCPTCGRSFRRNAHLQRHLITHTGSKQEKEVPQECPECGKSFNRSCNLLRHLLVHTGARPYSCALCGRSFSRNSHLLRHLRTHARESLY [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=Q3URR7 [UniProt boundaries chain A-2]=35-120 [UniProt coverage chain A-2]=10% [Name chain A-2]=Zinc finger and SCAN domain-containing protein 10 [UniProt sequence chain A-2]=MLAEPVPDALEQEHPGAVKLEEDEVGEEDPRLAESRPRPEVAHQLFRCFQYQEDMGPRASLGRLRELCNHWLRPALHTKKQILELLVLEQFLSVLPPHVLSRLHGQPLRDGEEVVQLLEGVPRDISHMGPLDFSFSAGKNAPADIISEEQNSPSQVPSHSPQTELPSEEIPALHPLNELPPPQPAPIRPAEPEEWRLAPSSNWPMSPEPQEILQDPRESNPSQGPSWLEENSRDQELAAVLESLTFEDTSEKRAWPANPLGFGSRMPDNEELKVEEPKVTTWPVVIGAESQTEKPEVAGEPLTQTVGQETSSTGWGGTPADGSEVVKVRGASDAPEPQGEMQFICTYCGVNFPEMSHLQAHQLQSHPNLQPHPSSRSFRCLWCGKTFGRSSILKLHMRTHTDERPHACHLCNRRFRQSSHLTKHLLTHSSEPAFRCAECNQGFQRRSSLMQHLLAHAQGKNLTPNPEGKTKVPEMAAVLCSHCGQTFKRRSSLKRHLRNHAKDKDHLSSEDPGSLSSSQESNPYVCSDCGKAFRQSEQLMIHTRRVHTRERPFSCQVCGRCFTQNSQLISHQQIHTGEKPHACPQCSKRFVRRAGLARHLLTHGSLRPYHCAQCGKSFRQMRDLTRHVRCHTGEKPCRCNECGEGFTQNAHLARHQRIHTGEKPHACDICGHRFRNSSNLARHRRSHTGERPYSCPTCGRSFRRNAHLQRHLITHTGSKQEKEVPQECPECGKSFNRSCNLLRHLLVHTGARPYSCALCGRSFSRNSHLLRHLRTHARESLY [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=1.85 [Source organism]=Mus musculus [Accession]=MF7000130 [Entry] [Entry number]=325 [Entry name]=CaiB (Type III CoA transferase in carnitine metabolism) [PDB ID]=1xa3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=CoA-transferase family III [Evidence level]=Indirect evidence [Evidence text]=The structure of CaiB reveals a spectacular fold where two monomers are interlaced to form an interlocked dimer with large interface (PMID:15518548). The folding path of CaiB and other proteins of this fold must be quite complex because the dimer cannot be formed by the individually folded monomers, partial unfolding would have to take place to break the CaiB dimer, thus it is most probably very stable (PMID:15518548). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000131,MF7000132,MF7000133,MF7000134,MF7000135,MF7000871 [UniProt ID chain A]=P31572 [UniProt boundaries chain A]=4-403 [UniProt coverage chain A]=98% [Name chain A]=L-carnitine CoA-transferase [UniProt sequence chain A]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P31572 [UniProt boundaries chain B]=4-403 [UniProt coverage chain B]=98% [Name chain B]=L-carnitine CoA-transferase [UniProt sequence chain B]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.85 [Source organism]=Escherichia coli [Accession]=MF7000131 [Entry] [Entry number]=326 [Entry name]=CaiB (Type III CoA transferase in carnitine metabolism) [PDB ID]=1xa4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=CoA-transferase family III [Evidence level]=Indirect evidence [Evidence text]=The structure of CaiB reveals a spectacular fold where two monomers are interlaced to form an interlocked dimer with large interface (PMID:15518548). The folding path of CaiB and other proteins of this fold must be quite complex because the dimer cannot be formed by the individually folded monomers, partial unfolding would have to take place to break the CaiB dimer, thus it is most probably very stable (PMID:15518548). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000131,MF7000132,MF7000133,MF7000134,MF7000135,MF7000871 [UniProt ID chain A]=P31572 [UniProt boundaries chain A]=4-403 [UniProt coverage chain A]=98% [Name chain A]=L-carnitine CoA-transferase [UniProt sequence chain A]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P31572 [UniProt boundaries chain B]=4-403 [UniProt coverage chain B]=98% [Name chain B]=L-carnitine CoA-transferase [UniProt sequence chain B]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Escherichia coli [Accession]=MF7000132 [Entry] [Entry number]=327 [Entry name]=CaiB (Type III CoA transferase in carnitine metabolism)/CoA complex [PDB ID]=1xvt [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=CoA-transferase family III [Evidence level]=Indirect evidence [Evidence text]=The structure of CaiB reveals a spectacular fold where two monomers are interlaced to form an interlocked dimer with large interface (PMID:15518548). The folding path of CaiB and other proteins of this fold must be quite complex because the dimer cannot be formed by the individually folded monomers, partial unfolding would have to take place to break the CaiB dimer, thus it is most probably very stable (PMID:15518548). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000131,MF7000132,MF7000133,MF7000134,MF7000135,MF7000871 [UniProt ID chain A]=P31572 [UniProt boundaries chain A]=4-405 [UniProt coverage chain A]=99% [Name chain A]=L-carnitine CoA-transferase [UniProt sequence chain A]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P31572 [UniProt boundaries chain A-2]=4-405 [UniProt coverage chain A-2]=99% [Name chain A-2]=L-carnitine CoA-transferase [UniProt sequence chain A-2]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Escherichia coli [Accession]=MF7000133 [Entry] [Entry number]=328 [Entry name]=CaiB (Type III CoA transferase in carnitine metabolism), D169A mutant /CoA complex [PDB ID]=1xvu [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=CoA-transferase family III [Evidence level]=Indirect evidence [Evidence text]=The structure of CaiB reveals a spectacular fold where two monomers are interlaced to form an interlocked dimer with large interface (PMID:15518548). The folding path of CaiB and other proteins of this fold must be quite complex because the dimer cannot be formed by the individually folded monomers, partial unfolding would have to take place to break the CaiB dimer, thus it is most probably very stable (PMID:15518548). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000131,MF7000132,MF7000133,MF7000134,MF7000135,MF7000871 [UniProt ID chain A]=P31572 [UniProt boundaries chain A]=4-405 [UniProt coverage chain A]=99% [Name chain A]=L-carnitine CoA-transferase [UniProt sequence chain A]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P31572 [UniProt boundaries chain A-2]=4-405 [UniProt coverage chain A-2]=99% [Name chain A-2]=L-carnitine CoA-transferase [UniProt sequence chain A-2]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Escherichia coli [Accession]=MF7000134 [Entry] [Entry number]=329 [Entry name]=CaiB (Type III CoA transferase in carnitine metabolism),D169A mutant /carnitinyl-CoA complex [PDB ID]=1xvv [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=CoA-transferase family III [Evidence level]=Indirect evidence [Evidence text]=The structure of CaiB reveals a spectacular fold where two monomers are interlaced to form an interlocked dimer with large interface (PMID:15518548). The folding path of CaiB and other proteins of this fold must be quite complex because the dimer cannot be formed by the individually folded monomers, partial unfolding would have to take place to break the CaiB dimer, thus it is most probably very stable (PMID:15518548). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000131,MF7000132,MF7000133,MF7000134,MF7000135,MF7000871 [UniProt ID chain A]=P31572 [UniProt boundaries chain A]=4-405 [UniProt coverage chain A]=99% [Name chain A]=L-carnitine CoA-transferase [UniProt sequence chain A]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P31572 [UniProt boundaries chain A-2]=4-405 [UniProt coverage chain A-2]=99% [Name chain A-2]=L-carnitine CoA-transferase [UniProt sequence chain A-2]=MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Escherichia coli [Accession]=MF7000135 [Entry] [Entry number]=330 [Entry name]=Dynein light chain TcTex-1 [PDB ID]=1xdx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Tctex-1 family [Evidence level]=Direct evidence [Evidence text]=The equilibrium unfolding transition of the dynein light chain TcTex-1 dimer was monitored by intrinsic fluorescence intensity, fluorescence anisotropy, and circular dichroism and was modeled as a two-state mechanism where a folded dimer dissociates to two unfolded monomers without populating thermodynamically stable monomeric or dimeric intermediates (PMID:16734416). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000137,MF2110016 [UniProt ID chain A]=O64980 [UniProt boundaries chain A]=1-114 [UniProt coverage chain A]=100% [Name chain A]=Dynein light chain Tctex1 [UniProt sequence chain A]=MEGVDPAVEEAAFVADDVSNIIKESIDAVLQNQQYSEAKVSQWTSSCLEHCIKRLTALNKPFKYVVTCIIMQKNGAGLHTAASCWWDSTTDGSRTVRWENKSMYCICTVFGLAI [Source organism chain A]=Chlamydomonas reinhardtii [UniProt ID chain B]=O64980 [UniProt boundaries chain B]=1-114 [UniProt coverage chain B]=100% [Name chain B]=Dynein light chain Tctex1 [UniProt sequence chain B]=MEGVDPAVEEAAFVADDVSNIIKESIDAVLQNQQYSEAKVSQWTSSCLEHCIKRLTALNKPFKYVVTCIIMQKNGAGLHTAASCWWDSTTDGSRTVRWENKSMYCICTVFGLAI [Source organism chain B]=Chlamydomonas reinhardtii [ExpTech]=NMR [Resolution]=N/A [Source organism]=Chlamydomonas reinhardtii [Accession]=MF7000137 [Entry] [Entry number]=331 [Entry name]=N-terminal of CTIP (human) [PDB ID]=7bgf [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:34129781). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q99708 [UniProt boundaries chain A]=31-141 [UniProt coverage chain A]=12% [Name chain A]=DNA endonuclease RBBP8 [UniProt sequence chain A]=MNISGSSCGSPNSADTSSDFKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSLGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEEESEHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNPCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q99708 [UniProt boundaries chain B]=31-138 [UniProt coverage chain B]=12% [Name chain B]=DNA endonuclease RBBP8 [UniProt sequence chain B]=MNISGSSCGSPNSADTSSDFKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSLGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEEESEHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNPCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Homo sapiens [Accession]=MF7000138 [Entry] [Entry number]=332 [Entry name]=AphA (Vibrio cholerae) [PDB ID]=1yg2 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q9X399 [UniProt boundaries chain A]=2-179 [UniProt coverage chain A]=99% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MSLPHVILTVLSTRDATGYDITKEFSASIGYFWKASHQQVYRELNKMGEQGLVTCVLEPQEGKPDRKVYSITQAGRSALGEWFDQPTAHPTVRDEFSAKLMACSVQSAEPYRLQLAELVEESRKLVAHYQEIEAAYYANPAVLDKQQRLERLTLRRNLLVRQAWIQWADEVLAELNAMA [Source organism chain A]=Vibrio cholerae [UniProt ID chain A-2]=Q9X399 [UniProt boundaries chain A-2]=2-179 [UniProt coverage chain A-2]=99% [Name chain A-2]=Transcriptional regulator [UniProt sequence chain A-2]=MSLPHVILTVLSTRDATGYDITKEFSASIGYFWKASHQQVYRELNKMGEQGLVTCVLEPQEGKPDRKVYSITQAGRSALGEWFDQPTAHPTVRDEFSAKLMACSVQSAEPYRLQLAELVEESRKLVAHYQEIEAAYYANPAVLDKQQRLERLTLRRNLLVRQAWIQWADEVLAELNAMA [Source organism chain A-2]=Vibrio cholerae [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Vibrio cholerae [Accession]=MF7000139 [Entry] [Entry number]=333 [Entry name]=MED7/MED21 (Med7/Srb7) heterodimer [PDB ID]=1ykh [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=MED7 and MED21 form a continuous hydrophobic interface, which explains why subunits that are individually expressed in E. coli are structurally unstable and either poorly soluble or easily degraded (PMID:15710619). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q08278 [UniProt boundaries chain A]=111-205 [UniProt coverage chain A]=42% [Name chain A]=Mediator of RNA polymerase II transcription subunit 7 [UniProt sequence chain A]=MSNDPGNEVSSLYPPPPPYVKFFTQSNLEKLPKYKEKKAASAKQTAPNNSNGGSEEEITCALDYLIPPPMPKNQQYRAFGSIWQVKDQLPDLESMGLTQLYKKSTENESTNYQYKIQELRKLLKSLLLNYLELIGVLSINPDMYERKVENIRTILVNIHHLLNEYRPHQSRESLIMLLEEQLEYKRGEIREIEQVCKQVHDKLTSIQDTLRTGSQSPPSSSQ [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P47822 [UniProt boundaries chain B]=2-130 [UniProt coverage chain B]=92% [Name chain B]=Mediator of RNA polymerase II transcription subunit 21 [UniProt sequence chain B]=MTDRLTQLQICLDQMTEQFCATLNYIDKNHGFERLTVNEPQMSDKHATVVPPEEFSNTIDELSTDIILKTRQINKLIDSLPGVDVSAEEQLRKIDMLQKKLVEVEDEKIEAIKKKEKLLRHVDSLIEDFVDGIANSKKST [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000140 [Entry] [Entry number]=334 [Entry name]=Coiled coil domain of cGMP-dependent Protein Kinase Ia [PDB ID]=1zxa [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:16131665). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q13976 [UniProt boundaries chain A]=9-44 [UniProt coverage chain A]=5% [Name chain A]=cGMP-dependent protein kinase 1 [UniProt sequence chain A]=MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDNDEPPPDDNSGWDIDF [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q13976 [UniProt boundaries chain B]=9-44 [UniProt coverage chain B]=5% [Name chain B]=cGMP-dependent protein kinase 1 [UniProt sequence chain B]=MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGTVNVTREDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDNDEPPPDDNSGWDIDF [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000141 [Entry] [Entry number]=335 [Entry name]=Heterodimer GABA(B) receptor (human) [PDB ID]=4pas [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:24778228). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9UBS5 [UniProt boundaries chain A]=884-918 [UniProt coverage chain A]=3% [Name chain A]=Gamma-aminobutyric acid type B receptor subunit 1 [UniProt sequence chain A]=MLLLLLLAPLFLRPPGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKIYDPSINCTVDEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRNQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSRKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQLRSRRHPPTPPEPSGGLPRGPPEPPDRLSCDGSRVHLLYK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O75899 [UniProt boundaries chain B]=779-817 [UniProt coverage chain B]=4% [Name chain B]=Gamma-aminobutyric acid type B receptor subunit 2 [UniProt sequence chain B]=MASPRSSGQPGPPPPPPPPPARLLLLLLLPLLLPLAPGAWGWARGAPRPPPSSPPLSIMGLMPLTKEVAKGSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDIEISDTESFSNDPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYEPSWWEQVHTEANSSRCLRKNLLAAMEGYIGVDFEPLSSKQIKTISGKTPQQYEREYNNKRSGVGPSKFHGYAYDGIWVIAKTLQRAMETLHASSRHQRIQDFNYTDHTLGRIILNAMNETNFFGVTGQVVFRNGERMGTIKFTQFQDSREVKVGEYNAVADTLEIINDTIRFQGSEPPKDKTIILEQLRKISLPLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSEKTFETLCTVRTWILTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVEKYSMEPDPAGRDISIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNVQFCIVALVIIFCSTITLCLVFVPKLITLRTNPDAATQNRRFQFTQNQKKEDSKTSTSVTSVNQASTSRLEGLQSENHRLRMKITELDKDLEEVTMQLQDTPEKTTYIKQNHYQELNDILNLGNFTESTDGGKAILKNHLDQNPQLQWNTTEPSRTCKDPIEDINSPEHIQRRLSLQLPILHHAYLPSIGGVDASCVSPCVSPTASPRHRHVPPSFRVMVSGL [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.62 [Source organism]=Homo sapiens [Accession]=MF7000142 [Entry] [Entry number]=336 [Entry name]=GCN2 protein kinase C-terminal domain (yeast) [PDB ID]=4otm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Histidyl tRNA synthetase-related domain [Evidence level]=Indirect evidence [Evidence text]=Both yeast and mammalian CTDs share a core subunit structure and an unusual interdigitated dimeric form (PMID:24719324). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000143,MF7000144 [UniProt ID chain A]=P15442 [UniProt boundaries chain A]=1537-1659 [UniProt coverage chain A]=7% [Name chain A]=eIF-2-alpha kinase GCN2 [UniProt sequence chain A]=MSLSHLTLDQYYEIQCNELEAIRSIYMDDFTDLTKRKSSWDKQPQIIFEITLRSVDKEPVESSITLHFAMTPMYPYTAPEIEFKNVQNVMDSQLQMLKSEFKKIHNTSRGQEIIFEITSFTQEKLDEFQNVVNTQSLEDDRLQRIKETKEQLEKEEREKQQETIKKRSDEQRRIDEIVQRELEKRQDDDDDLLFNRTTQLDLQPPSEWVASGEAIVFSKTIKAKLPNNSMFKFKAVVNPKPIKLTSDIFSFSKQFLVKPYIPPESPLADFLMSSEMMENFYYLLSEIELDNSYFNTSNGKKEIANLEKELETVLKAKHDNVNRLFGYTVERMGRNNATFVWKIRLLTEYCNYYPLGDLIQSVGFVNLATARIWMIRLLEGLEAIHKLGIVHKCINLETVILVKDADFGSTIPKLVHSTYGYTVLNMLSRYPNKNGSSVELSPSTWIAPELLKFNNAKPQRLTDIWQLGVLFIQIISGSDIVMNFETPQEFLDSTSMDETLYDLLSKMLNNDPKKRLGTLELLPMKFLRTNIDSTINRFNLVSESVNSNSLELTPGDTITVRGNGGRTLSQSSIRRRSFNVGSRFSSINPATRSRYASDFEEIAVLGQGAFGQVVKARNALDSRYYAIKKIRHTEEKLSTILSEVMLLASLNHQYVVRYYAAWLEEDSMDENVFESTDEESDLSESSSDFEENDLLDQSSIFKNRTNHDLDNSNWDFISGSGYPDIVFENSSRDDENEDLDHDTSSTSSSESQDDTDKESKSIQNVPRRRNFVKPMTAVKKKSTLFIQMEYCENRTLYDLIHSENLNQQRDEYWRLFRQILEALSYIHSQGIIHRDLKPMNIFIDESRNVKIGDFGLAKNVHRSLDILKLDSQNLPGSSDNLTSAIGTAMYVATEVLDGTGHYNEKIDMYSLGIIFFEMIYPFSTGMERVNILKKLRSVSIEFPPDFDDNKMKVEKKIIRLLIDHDPNKRPGARTLLNSGWLPVKHQDEVIKEALKSLSNPSSPWQQQVRESLFNQSYSLTNDILFDNSVPTSTPFANILRSQMTEEVVKIFRKHGGIENNAPPRIFPKAPIYGTQNVYEVLDKGGTVLQLQYDLTYPMARYLSKNPSLISKQYRMQHVYRPPDHSRSSLEPRKFGEIDFDIISKSSSESGFYDAESLKIIDEILTVFPVFEKTNTFFILNHADILESVFNFTNIDKAQRPLVSRMLSQVGFARSFKEVKNELKAQLNISSTALNDLELFDFRLDFEAAKKRLYKLMIDSPHLKKIEDSLSHISKVLSYLKPLEVARNVVISPLSNYNSAFYKGGIMFHAVYDDGSSRNMIAAGGRYDTLISFFARPSGKKSSNTRKAVGFNLAWETIFGIAQNYFKLASGNRIKKRNRFLKDTAVDWKPSRCDVLISSFSNSLLDTIGVTILNTLWKQNIKADMLRDCSSVDDVVTGAQQDGIDWILLIKQQAYPLTNHKRKYKPLKIKKLSTNVDIDLDLDEFLTLYQQETGNKSLINDSLTLGDKADEFKRWDENSSAGSSQEGDIDDVVAGSTNNQKVIYVPNMATRSKKANKREKWVYEDAARNSSNMILHNLSNAPIITVDALRDETLEIISITSLAQKEEWLRKVFGSGNNSTPRSFATSIYNNLSKEAHKGNRWAILYCHKTGKSSVIDLQR [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P15442 [UniProt boundaries chain B]=1538-1659 [UniProt coverage chain B]=7% [Name chain B]=eIF-2-alpha kinase GCN2 [UniProt sequence chain B]=MSLSHLTLDQYYEIQCNELEAIRSIYMDDFTDLTKRKSSWDKQPQIIFEITLRSVDKEPVESSITLHFAMTPMYPYTAPEIEFKNVQNVMDSQLQMLKSEFKKIHNTSRGQEIIFEITSFTQEKLDEFQNVVNTQSLEDDRLQRIKETKEQLEKEEREKQQETIKKRSDEQRRIDEIVQRELEKRQDDDDDLLFNRTTQLDLQPPSEWVASGEAIVFSKTIKAKLPNNSMFKFKAVVNPKPIKLTSDIFSFSKQFLVKPYIPPESPLADFLMSSEMMENFYYLLSEIELDNSYFNTSNGKKEIANLEKELETVLKAKHDNVNRLFGYTVERMGRNNATFVWKIRLLTEYCNYYPLGDLIQSVGFVNLATARIWMIRLLEGLEAIHKLGIVHKCINLETVILVKDADFGSTIPKLVHSTYGYTVLNMLSRYPNKNGSSVELSPSTWIAPELLKFNNAKPQRLTDIWQLGVLFIQIISGSDIVMNFETPQEFLDSTSMDETLYDLLSKMLNNDPKKRLGTLELLPMKFLRTNIDSTINRFNLVSESVNSNSLELTPGDTITVRGNGGRTLSQSSIRRRSFNVGSRFSSINPATRSRYASDFEEIAVLGQGAFGQVVKARNALDSRYYAIKKIRHTEEKLSTILSEVMLLASLNHQYVVRYYAAWLEEDSMDENVFESTDEESDLSESSSDFEENDLLDQSSIFKNRTNHDLDNSNWDFISGSGYPDIVFENSSRDDENEDLDHDTSSTSSSESQDDTDKESKSIQNVPRRRNFVKPMTAVKKKSTLFIQMEYCENRTLYDLIHSENLNQQRDEYWRLFRQILEALSYIHSQGIIHRDLKPMNIFIDESRNVKIGDFGLAKNVHRSLDILKLDSQNLPGSSDNLTSAIGTAMYVATEVLDGTGHYNEKIDMYSLGIIFFEMIYPFSTGMERVNILKKLRSVSIEFPPDFDDNKMKVEKKIIRLLIDHDPNKRPGARTLLNSGWLPVKHQDEVIKEALKSLSNPSSPWQQQVRESLFNQSYSLTNDILFDNSVPTSTPFANILRSQMTEEVVKIFRKHGGIENNAPPRIFPKAPIYGTQNVYEVLDKGGTVLQLQYDLTYPMARYLSKNPSLISKQYRMQHVYRPPDHSRSSLEPRKFGEIDFDIISKSSSESGFYDAESLKIIDEILTVFPVFEKTNTFFILNHADILESVFNFTNIDKAQRPLVSRMLSQVGFARSFKEVKNELKAQLNISSTALNDLELFDFRLDFEAAKKRLYKLMIDSPHLKKIEDSLSHISKVLSYLKPLEVARNVVISPLSNYNSAFYKGGIMFHAVYDDGSSRNMIAAGGRYDTLISFFARPSGKKSSNTRKAVGFNLAWETIFGIAQNYFKLASGNRIKKRNRFLKDTAVDWKPSRCDVLISSFSNSLLDTIGVTILNTLWKQNIKADMLRDCSSVDDVVTGAQQDGIDWILLIKQQAYPLTNHKRKYKPLKIKKLSTNVDIDLDLDEFLTLYQQETGNKSLINDSLTLGDKADEFKRWDENSSAGSSQEGDIDDVVAGSTNNQKVIYVPNMATRSKKANKREKWVYEDAARNSSNMILHNLSNAPIITVDALRDETLEIISITSLAQKEEWLRKVFGSGNNSTPRSFATSIYNNLSKEAHKGNRWAILYCHKTGKSSVIDLQR [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000143 [Entry] [Entry number]=337 [Entry name]=GCN2 protein kinase C-terminal domain (mouse) [PDB ID]=4otn [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Histidyl tRNA synthetase-related domain [Evidence level]=Indirect evidence [Evidence text]=Both yeast and mammalian CTDs share a core subunit structure and an unusual interdigitated dimeric form (PMID:24719324). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000143,MF7000144 [UniProt ID chain A]=Q9QZ05 [UniProt boundaries chain A]=1526-1648 [UniProt coverage chain A]=7% [Name chain A]=eIF-2-alpha kinase GCN2 [UniProt sequence chain A]=MAGGRGASGRGRAEPQESYSQRQDHELQALEAIYGSDFQDLRPDARGRVREPPEINLVLYPQGLAGEEVYVQVELQVKCPPTYPDVVPEIELKNAKGLSNESVNLLKSHLEELAKKQCGEVMIFELAHHVQSFLSEHNKPPPKSFHEEMLERQAQEKQQRLLEARRKEEQEQREILHEIQRRKEEIKEEKKRKEMAKQERLEITSLTNQDYASKRDPAGHRAAAILHGGSPDFVGNGKARTYSSGRSRRERQYSVCSGEPSPGSCDILHFSVGSPDQLMVHKGRCVGSDEQLGKVVYNALETATGSFVLLHEWVLQWQKMGPCLTSQEKEKIDKCKRQIQGAETEFSSLVKLSHPNIVRYFAMNSREEEDSIVIDILAEHVSGISLATHLSHSGPVPAHQLRKYTAQLLAGLDYLHSNSVVHKVLSASSVLVDAEGTVKITDYSISKRLADICKEDVFEQARVRFSDSALPYKTGKKGDVWRLGLLLLSLSQGQECGEYPVTIPSDLPADFQDFLKKCVCLDDKERWSPQQLLKHSFINPQPKLPLVEQSPEDSGGQDYIETVIPSNQLPSAAFFSETQKQFSRYFIEFEELQLLGKGAFGAVIKVQNKLDGCCYAVKRIPINPASRHFRRIKGEVTLLSRLHHENIVRYYNAWIERHERPAVPGTPPPDCTPQAQDSPATCGKTSGDTEELGSVEAAAPPPILSSSVEWSTSAERSTSTRFPVTGQDSSSDEEDEDERDGVFSQSFLPASDSDSDIIFDNEDENSKSQNQDEDCNQKDGSHEIEPSVTAEAVHYLYIQMEYCEKSTLRDTIDQGLFRDTSRLWRLFREILDGLAYIHEKGMIHRDLKPVNIFLDSDDHVKIGDFGLATDHLAFTAEGKQDDQAGDGVIKSDPSGHLTGMVGTALYVSPEVQGSTKSAYNQKVDLFSLGIIFFEMSYHPMVTASERIFVLNQLRDPTSPKFPDDFDDGEHTKQKSVISWLLNHDPAKRPTAMELLKSELLPPPQMEESELHEVLHHTLANIDGKAYRTMMSQIFCQHISPAIDYTYDSDILKGNFLIRTAKIQQLVCETIVRVFKRHGAVQLCTPLLLPRNRQIYEHNEAALFMDHSGMLVMLPFDLRVPFARYVARNNILNLKRYCIERVFRPRKLDRFHPKELLECAFDIVTSTTNSSLPTAETIYTIYEIIQEFPALQERNYSIYLNHTMLLKAILLHCGIPEDKLSQVYVILYDAVTEKLTRREVEAKFCNLSLSSNSLCRLYKFIEQKGDLQDLTPTINSLIKQKTGVAQLVKYSLKDLEDVVGLLKKLGVKLQVSINLGLVYKVQQHTGIIFQFLAFSKRRQRVVPEILAAGGRYDLLIPKFRGPQTVGPVPTAVGVSIAIDKIFAAVLNMEEPVTVSSCDLLVVSVGQMSMSRAINLTQKLWTAGITAEIMYDWSQSQEELQEYCRHHEITYVALVSDKEGSHVKVKSFEKERQTEKRVLESDLVDHVMQKLRTKVGDERNFRDASDNLAVQTLKGSFSNASGLFEIHGTTVVPNVIVLAPEKLSASTRRRHEIQVQTRLQTTLANLHQKSSEIEILAVDLPKETILQFLSLEWDADEQAFNTTVKQLLSRLPKQRYLKLVCDEIYNIKVEKKVSVLFLYSYRDDYYRILF [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9QZ05 [UniProt boundaries chain B]=1530-1648 [UniProt coverage chain B]=7% [Name chain B]=eIF-2-alpha kinase GCN2 [UniProt sequence chain B]=MAGGRGASGRGRAEPQESYSQRQDHELQALEAIYGSDFQDLRPDARGRVREPPEINLVLYPQGLAGEEVYVQVELQVKCPPTYPDVVPEIELKNAKGLSNESVNLLKSHLEELAKKQCGEVMIFELAHHVQSFLSEHNKPPPKSFHEEMLERQAQEKQQRLLEARRKEEQEQREILHEIQRRKEEIKEEKKRKEMAKQERLEITSLTNQDYASKRDPAGHRAAAILHGGSPDFVGNGKARTYSSGRSRRERQYSVCSGEPSPGSCDILHFSVGSPDQLMVHKGRCVGSDEQLGKVVYNALETATGSFVLLHEWVLQWQKMGPCLTSQEKEKIDKCKRQIQGAETEFSSLVKLSHPNIVRYFAMNSREEEDSIVIDILAEHVSGISLATHLSHSGPVPAHQLRKYTAQLLAGLDYLHSNSVVHKVLSASSVLVDAEGTVKITDYSISKRLADICKEDVFEQARVRFSDSALPYKTGKKGDVWRLGLLLLSLSQGQECGEYPVTIPSDLPADFQDFLKKCVCLDDKERWSPQQLLKHSFINPQPKLPLVEQSPEDSGGQDYIETVIPSNQLPSAAFFSETQKQFSRYFIEFEELQLLGKGAFGAVIKVQNKLDGCCYAVKRIPINPASRHFRRIKGEVTLLSRLHHENIVRYYNAWIERHERPAVPGTPPPDCTPQAQDSPATCGKTSGDTEELGSVEAAAPPPILSSSVEWSTSAERSTSTRFPVTGQDSSSDEEDEDERDGVFSQSFLPASDSDSDIIFDNEDENSKSQNQDEDCNQKDGSHEIEPSVTAEAVHYLYIQMEYCEKSTLRDTIDQGLFRDTSRLWRLFREILDGLAYIHEKGMIHRDLKPVNIFLDSDDHVKIGDFGLATDHLAFTAEGKQDDQAGDGVIKSDPSGHLTGMVGTALYVSPEVQGSTKSAYNQKVDLFSLGIIFFEMSYHPMVTASERIFVLNQLRDPTSPKFPDDFDDGEHTKQKSVISWLLNHDPAKRPTAMELLKSELLPPPQMEESELHEVLHHTLANIDGKAYRTMMSQIFCQHISPAIDYTYDSDILKGNFLIRTAKIQQLVCETIVRVFKRHGAVQLCTPLLLPRNRQIYEHNEAALFMDHSGMLVMLPFDLRVPFARYVARNNILNLKRYCIERVFRPRKLDRFHPKELLECAFDIVTSTTNSSLPTAETIYTIYEIIQEFPALQERNYSIYLNHTMLLKAILLHCGIPEDKLSQVYVILYDAVTEKLTRREVEAKFCNLSLSSNSLCRLYKFIEQKGDLQDLTPTINSLIKQKTGVAQLVKYSLKDLEDVVGLLKKLGVKLQVSINLGLVYKVQQHTGIIFQFLAFSKRRQRVVPEILAAGGRYDLLIPKFRGPQTVGPVPTAVGVSIAIDKIFAAVLNMEEPVTVSSCDLLVVSVGQMSMSRAINLTQKLWTAGITAEIMYDWSQSQEELQEYCRHHEITYVALVSDKEGSHVKVKSFEKERQTEKRVLESDLVDHVMQKLRTKVGDERNFRDASDNLAVQTLKGSFSNASGLFEIHGTTVVPNVIVLAPEKLSASTRRRHEIQVQTRLQTTLANLHQKSSEIEILAVDLPKETILQFLSLEWDADEQAFNTTVKQLLSRLPKQRYLKLVCDEIYNIKVEKKVSVLFLYSYRDDYYRILF [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Mus musculus [Accession]=MF7000144 [Entry] [Entry number]=338 [Entry name]=Dimerization domain of Quaking Qua1 (mouse) [PDB ID]=4dnn [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Homodimerisation region of STAR domain protein [Evidence level]=Direct evidence [Evidence text]=The homodimer stability of the set of QkI Qua1 mutants was determined by thermal melting monitored by CD spectroscopy. The resulting curves show a single transition implying that QkI Qua1 forms obligate dimers in which dimer dissociation and unfolding of the monomer secondary structure occur simultaneously and a folded monomeric Qua1 domain likely does not exist (PMID:22982292). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000145,MF7000146 [UniProt ID chain A]=Q9QYS9 [UniProt boundaries chain A]=14-61 [UniProt coverage chain A]=14% [Name chain A]=KH domain-containing RNA-binding protein QKI [UniProt sequence chain A]=MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9QYS9 [UniProt boundaries chain B]=14-62 [UniProt coverage chain B]=14% [Name chain B]=KH domain-containing RNA-binding protein QKI [UniProt sequence chain B]=MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Mus musculus [Accession]=MF7000145 [Entry] [Entry number]=339 [Entry name]=Dimerization domain of Quaking Qua1 (pXqua) [PDB ID]=2ymj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Homodimerisation region of STAR domain protein [Evidence level]=Direct evidence [Evidence text]=The homodimer stability of the set of QkI Qua1 mutants was determined by thermal melting monitored by CD spectroscopy. The resulting curves show a single transition implying that QkI Qua1 forms obligate dimers in which dimer dissociation and unfolding of the monomer secondary structure occur simultaneously and a folded monomeric Qua1 domain likely does not exist (PMID:22982292). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000145,MF7000146 [UniProt ID chain A]=Q32NN2 [UniProt boundaries chain A]=8-57 [UniProt coverage chain A]=14% [Name chain A]=KH domain-containing RNA-binding protein qki.S [UniProt sequence chain A]=MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFTHLERLLDEEISRVRKDMYNDTMNSSSNEKRTSELPDGIGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAELKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANLKSPALAFSLAATGQAPRIITGPAPVLSPAALRTPTPAGHTLMPLIRQIQTAVMPNGTPHPTATLMQQAPEGGLIYTPYEYPYTLAPATSILEYPIEASGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN [Source organism chain A]=Xenopus laevis [UniProt ID chain B]=Q32NN2 [UniProt boundaries chain B]=8-57 [UniProt coverage chain B]=14% [Name chain B]=KH domain-containing RNA-binding protein qki.S [UniProt sequence chain B]=MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFTHLERLLDEEISRVRKDMYNDTMNSSSNEKRTSELPDGIGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAELKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANLKSPALAFSLAATGQAPRIITGPAPVLSPAALRTPTPAGHTLMPLIRQIQTAVMPNGTPHPTATLMQQAPEGGLIYTPYEYPYTLAPATSILEYPIEASGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN [Source organism chain B]=Xenopus laevis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Xenopus laevis [Accession]=MF7000146 [Entry] [Entry number]=340 [Entry name]=Cytoplasmic domain of a bacterial chemoreceptor (Thermotoga maritima) [PDB ID]=2ch7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Methyl-accepting chemotaxis protein (MCP) signalling domain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:16622408). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000917,MF7000147,MF7000263,MF7000264 [UniProt ID chain A]=Q9X0M7 [UniProt boundaries chain A]=222-529 [UniProt coverage chain A]=58% [Name chain A]=Methyl-accepting chemotaxis protein 2 [UniProt sequence chain A]=MSLKGKTLLVSTITLAAVVLVALLGGSVFLKAGQNVRKAFEEYELAVEALDKLGELETKVALFVNNAAKIEEVSSLFNELKKVADKIPSLKEHMDALERNISEIISGKTEVVSRIQSSVDQVKEDIMANLDRTRENLDKEISYSSELIRNVLFIVLPIVAVASGVFLFVMISRSLRLLKPVMEASRSLRNNDLTINIQEAKGKDEISTLLNEFKASIEYLRNNLKDVQTETFSVAESIEEISKANEEITNQLLGISKEMDNISTRIESISASVQETTAGSEEISSATKNIADSAQQAASFADQSTQLAKEAGDALKKVIEVTRMISNSAKDVERVVESFQKGAEEITSFVETINAIAEQTNLLALNAAIEAARAGEAGRGFAVVADEIRKLAEESQQASENVRRVVNEIRSIAEDAGKVSSEITARVEEGTKLADEADEKLNSIVGAVERINEMLQNIAAAIEEQTAAVDEITTAMTENAKNAEEITNSVKEVNARLQEISASTEEVTSRVQTIRENVQMLKEIVARYKI [Source organism chain A]=/ MSB8) [UniProt ID chain B]=Q9X0M7 [UniProt boundaries chain B]=222-529 [UniProt coverage chain B]=58% [Name chain B]=Methyl-accepting chemotaxis protein 2 [UniProt sequence chain B]=MSLKGKTLLVSTITLAAVVLVALLGGSVFLKAGQNVRKAFEEYELAVEALDKLGELETKVALFVNNAAKIEEVSSLFNELKKVADKIPSLKEHMDALERNISEIISGKTEVVSRIQSSVDQVKEDIMANLDRTRENLDKEISYSSELIRNVLFIVLPIVAVASGVFLFVMISRSLRLLKPVMEASRSLRNNDLTINIQEAKGKDEISTLLNEFKASIEYLRNNLKDVQTETFSVAESIEEISKANEEITNQLLGISKEMDNISTRIESISASVQETTAGSEEISSATKNIADSAQQAASFADQSTQLAKEAGDALKKVIEVTRMISNSAKDVERVVESFQKGAEEITSFVETINAIAEQTNLLALNAAIEAARAGEAGRGFAVVADEIRKLAEESQQASENVRRVVNEIRSIAEDAGKVSSEITARVEEGTKLADEADEKLNSIVGAVERINEMLQNIAAAIEEQTAAVDEITTAMTENAKNAEEITNSVKEVNARLQEISASTEEVTSRVQTIRENVQMLKEIVARYKI [Source organism chain B]=/ MSB8) [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=/ MSB8) [Accession]=MF7000147 [Entry] [Entry number]=341 [Entry name]=FGFR1OP N-terminal domain (human) [PDB ID]=2d68 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The N-terminal fragment of FOP forms a dimer in which each chain is composed of five a-helices connected by irregular loops. In the dimer, the monomer/monomer interface has a hydrophobic character maintained by residues that form helices a1, a2 and a3. The surface between the chains is tightly packed with Leu, Val, and Phe residues, forming a hydrophobic core. The second region of FOP responsible for homodimerization is located at the C-terminal part of the chain. The wild-type construct migrated as a dimer and mutations disturbung dimerization resulted in unstable, aggregating monomers (PMID:16690081). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O95684 [UniProt boundaries chain A]=58-135 [UniProt coverage chain A]=19% [Name chain A]=Centrosomal protein 43 [UniProt sequence chain A]=MAATAAAVVAEEDTELRDLLVQTLENSGVLNRIKAELRAAVFLALEEQEKVENKTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTLQGLEGRENLARDLGIIEAEGTVGGPLLLEVIRRCQQKEKGPTTGEGALDLSDVHSPPKSPEGKTSAQTTPSKIPRYKGQGKKKTSGQKAGDKKANDEANQSDTSVSLSEPKSKSSLHLLSHETKIGSFLSNRTLDGKDKAGLCPDEDDMEGDSFFDDPIPKPEKTYGLRKEPRKQAGSLASLSDAPPLKSGLSSLAGAPSLKDSESKRGNTVLKDLKLISDKIGSLGLGTGEDDDYVDDFNSTSHRSEKSEISIGEEIEEDLSVEIDDINTSDKLDDLTQDLTVSQLSDVADYLEDVA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O95684 [UniProt boundaries chain B]=59-135 [UniProt coverage chain B]=19% [Name chain B]=Centrosomal protein 43 [UniProt sequence chain B]=MAATAAAVVAEEDTELRDLLVQTLENSGVLNRIKAELRAAVFLALEEQEKVENKTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTLQGLEGRENLARDLGIIEAEGTVGGPLLLEVIRRCQQKEKGPTTGEGALDLSDVHSPPKSPEGKTSAQTTPSKIPRYKGQGKKKTSGQKAGDKKANDEANQSDTSVSLSEPKSKSSLHLLSHETKIGSFLSNRTLDGKDKAGLCPDEDDMEGDSFFDDPIPKPEKTYGLRKEPRKQAGSLASLSDAPPLKSGLSSLAGAPSLKDSESKRGNTVLKDLKLISDKIGSLGLGTGEDDDYVDDFNSTSHRSEKSEISIGEEIEEDLSVEIDDINTSDKLDDLTQDLTVSQLSDVADYLEDVA [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Homo sapiens [Accession]=MF7000148 [Entry] [Entry number]=343 [Entry name]=Orange domain of HES1 [PDB ID]=7c4o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Orange domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=The HES1 protein orange domain exists as a dimer in solution, and the monomer consists of two helices separated by a small linker forming a U-shaped structure. The dimer has an extensive buried surface area with 6 hydrogen bonds and 12 salt bridges, rendering the Orange domain highly stable. This region is responsible for the stability and dimerization of the full-length HES1 protein (PMID:35640677). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q14469 [UniProt boundaries chain A]=103-150 [UniProt coverage chain A]=17% [Name chain A]=Transcription factor HES-1 [UniProt sequence chain A]=MPADIMEKNSSSPVAATPASVNTTPDKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQMTAALSTDPSVLGKYRAGFSECMNEVTRFLSTCEGVNTEVRTRLLGHLANCMTQINAMTYPGQPHPALQAPPPPPPGPGGPQHAPFAPPPPLVPIPGGAAPPPGGAPCKLGSQAGEAAKVFGGFQVVPAPDGQFAFLIPNGAFAHSGPVIPVYTSNSGTSVGPNAVSPSSGPSLTADSMWRPWRN [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q14469 [UniProt boundaries chain B]=103-150 [UniProt coverage chain B]=17% [Name chain B]=Transcription factor HES-1 [UniProt sequence chain B]=MPADIMEKNSSSPVAATPASVNTTPDKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQMTAALSTDPSVLGKYRAGFSECMNEVTRFLSTCEGVNTEVRTRLLGHLANCMTQINAMTYPGQPHPALQAPPPPPPGPGGPQHAPFAPPPPLVPIPGGAAPPPGGAPCKLGSQAGEAAKVFGGFQVVPAPDGQFAFLIPNGAFAHSGPVIPVYTSNSGTSVGPNAVSPSSGPSLTADSMWRPWRN [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000150 [Entry] [Entry number]=344 [Entry name]=Putative transcriptional regulator SCO5550 (Streptomyces coelicolor A3(2)) [PDB ID]=2dg6 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The dimerization domain of SCO5550 is an all-helical domain, and the helices of two monomers wrap around each other. Among these helices, a9 and a11 stretch to the neighboring monomer and form a stable dimer. The helix a9 associates with a9' by hydrophobic interaction in an antiparallel orientation. The helix a11 is surrounded by an a helical barrel formed by a5', a6', a7', a8', a9', and a10' of the other monomer, suggesting that a11 is a key for dimerization of SCO5550. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=O86531 [UniProt boundaries chain A]=1-214 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MRLADLSKRSGVSTATIKYYLREGLLPPGRQVNATTAEYDEDHLRRLRLVRALIQVGKVPVATAREVLGHVDDDSLGRTVRLGAALWALPQDAEPDEADPAVAAARVEVDRLLELLGWETSRELAPLSPVHRSLVVAVAALRRLDYPWDAELMAPYGELMMEVARRDLDFMETHASEAEKVEMAVAAAVLFQPVLRALHRLAQEEESARRYGIE [Source organism chain A]=Streptomyces coelicolor [UniProt ID chain A-2]=O86531 [UniProt boundaries chain A-2]=1-214 [UniProt coverage chain A-2]=100% [Name chain A-2]=Transcriptional regulator [UniProt sequence chain A-2]=MRLADLSKRSGVSTATIKYYLREGLLPPGRQVNATTAEYDEDHLRRLRLVRALIQVGKVPVATAREVLGHVDDDSLGRTVRLGAALWALPQDAEPDEADPAVAAARVEVDRLLELLGWETSRELAPLSPVHRSLVVAVAALRRLDYPWDAELMAPYGELMMEVARRDLDFMETHASEAEKVEMAVAAAVLFQPVLRALHRLAQEEESARRYGIE [Source organism chain A-2]=Streptomyces coelicolor [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Streptomyces coelicolor [Accession]=MF7000151 [Entry] [Entry number]=345 [Entry name]=Transcription factor CGL2947 from Corynebacterium glutamicum [PDB ID]=2du9 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Bacterial regulatory proteins, gntR family [Evidence level]=Indirect evidence [Evidence text]=The Cgl2947 monomer is composed of a DNA-binding domain containing a winged HTH motif in the N terminus and two helices (α4 and α5) with a fishhook-shaped arrangement in the C terminus. C-terminal helices α4 and α5 of the two monomers intertwine together to form a novel homodimer assembly through MSF (PMID:17766384). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000152,MF7000960 [UniProt ID chain A]=Q8NLJ5 [UniProt boundaries chain A]=3-118 [UniProt coverage chain A]=95% [Name chain A]=Predicted transcriptional regulators [UniProt sequence chain A]=MTVPLYKQIASLIEDSIVDGTLSIDQRVPSTNELAAFHRINPATARNGLTLLVEAGILYKKRGIGMFVSAQAPALIRERRDAAFAATYVAPLIDESIHLGFTRARIHALLDQVAESRGLYK [Source organism chain A]=534) [UniProt ID chain A-2]=Q8NLJ5 [UniProt boundaries chain A-2]=3-118 [UniProt coverage chain A-2]=95% [Name chain A-2]=Predicted transcriptional regulators [UniProt sequence chain A-2]=MTVPLYKQIASLIEDSIVDGTLSIDQRVPSTNELAAFHRINPATARNGLTLLVEAGILYKKRGIGMFVSAQAPALIRERRDAAFAATYVAPLIDESIHLGFTRARIHALLDQVAESRGLYK [Source organism chain A-2]=534) [ExpTech]=X-ray [Resolution]=2.28 [Source organism]=534) [Accession]=MF7000152 [Entry] [Entry number]=346 [Entry name]=Atg16 (Saccharomyces cerevisiae) [PDB ID]=3a7p [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Autophagy protein 16 (ATG16) [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:19889643). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110005,MF7000153 [UniProt ID chain A]=Q03818 [UniProt boundaries chain A]=55-142 [UniProt coverage chain A]=58% [Name chain A]=Autophagy protein 16 [UniProt sequence chain A]=MGNFIITERKKAKEERSNPQTDSMDDLLIRRLTDRNDKEAHLNELFQDNSGAIGGNIVSHDDALLNTLAILQKELKSKEQEIRRLKEVIALKNKNTERLNDELISGTIENNVLQQKLSDLKKEHSQLVARWLKKTEKETEAMNSEIDGTK [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=Q03818 [UniProt boundaries chain B]=58-133 [UniProt coverage chain B]=50% [Name chain B]=Autophagy protein 16 [UniProt sequence chain B]=MGNFIITERKKAKEERSNPQTDSMDDLLIRRLTDRNDKEAHLNELFQDNSGAIGGNIVSHDDALLNTLAILQKELKSKEQEIRRLKEVIALKNKNTERLNDELISGTIENNVLQQKLSDLKKEHSQLVARWLKKTEKETEAMNSEIDGTK [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000153 [Entry] [Entry number]=347 [Entry name]=BAR domain of APPL1 [PDB ID]=2q12 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=APPL BAR domain [Sequence domain]=APPL BAR domain [Evidence level]=Direct evidence [Evidence text]=The two BAR domains form a tightly packed dimer with a crescent-like shape, a hallmark of BAR domain dimers. The helix α1 forms an antiparallel helix bundle with its symmetry counterpart because it packs against α3 of the other protomer on the convex side of the dimer. A huge solvent accessible surface (SAS) area gets buried in the dimer interface. The addition of each α4 helix to the canonical BAR motif results in a large increase in buried SAS on the two protomers, corresponding to over 40% of the total buried SAS. Other BAR domains (N-BARs) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). In some structures of the family an independently folded PH domain is also included in the structure, so only a part of the structure undergoes MSF. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000905,MF7000906,MF7000154,MF7000907 [UniProt ID chain A]=Q9UKG1 [UniProt boundaries chain A]=13-259 [UniProt coverage chain A]=34% [Name chain A]=DCC-interacting protein 13-alpha [UniProt sequence chain A]=MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNEQLEEFLANIGTSVQNVRREMDSDIETMQQTIEDLEVASDPLYVPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPAAGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQENKRLFGFVLRTSSGRSESNLSSVCYIFESNNEGEKICDSVGLAKQIALHAELDRRASEKQKEIERVKEKQQKELNKQKQIEKDLEEQSRLIAASSRPNQASSEGQFVVLSSSQSEESDLGEGGKKRESEA [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q9UKG1 [UniProt boundaries chain A-2]=13-259 [UniProt coverage chain A-2]=34% [Name chain A-2]=DCC-interacting protein 13-alpha [UniProt sequence chain A-2]=MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNEQLEEFLANIGTSVQNVRREMDSDIETMQQTIEDLEVASDPLYVPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPAAGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQENKRLFGFVLRTSSGRSESNLSSVCYIFESNNEGEKICDSVGLAKQIALHAELDRRASEKQKEIERVKEKQQKELNKQKQIEKDLEEQSRLIAASSRPNQASSEGQFVVLSSSQSEESDLGEGGKKRESEA [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.79 [Source organism]=Homo sapiens [Accession]=MF7000154 [Entry] [Entry number]=349 [Entry name]=Multiple antibiotic-resistance repressor (MarR) from Xanthomonas campestris [PDB ID]=2fa5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=Q8PDA5 [UniProt boundaries chain A]=12-159 [UniProt coverage chain A]=91% [Name chain A]=Transcriptional regulator marR/emrR family [UniProt sequence chain A]=MSDLDTPTPSPHPVLLNLEQFLPYRLSVLSNRISGNIAKVYGDRYGMAIPEWRVITILALYPGSSASEVSDRTAMDKVAVSRAVARLLERGFIRRETHGDDRRRSMLALSPAGRQVYETVAPLVNEMEQRLMSVFSAEEQQTLERLIDRLAKDGLPRMASKD [Source organism chain A]=528 / LMG 568 / P 25) [UniProt ID chain B]=Q8PDA5 [UniProt boundaries chain B]=10-159 [UniProt coverage chain B]=92% [Name chain B]=Transcriptional regulator marR/emrR family [UniProt sequence chain B]=MSDLDTPTPSPHPVLLNLEQFLPYRLSVLSNRISGNIAKVYGDRYGMAIPEWRVITILALYPGSSASEVSDRTAMDKVAVSRAVARLLERGFIRRETHGDDRRRSMLALSPAGRQVYETVAPLVNEMEQRLMSVFSAEEQQTLERLIDRLAKDGLPRMASKD [Source organism chain B]=528 / LMG 568 / P 25) [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=528 / LMG 568 / P 25) [Accession]=MF7000156 [Entry] [Entry number]=350 [Entry name]=NadR [PDB ID]=5aip [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=Q7DD70 [UniProt boundaries chain A]=1-141 [UniProt coverage chain A]=96% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MPTQSKHASINIGLIQAREALMTQFRPILNQANITDQQWRIIRLLAENGTLDFQDLANQACILRPSLTGILTRLEKAGLVVRLKPSNDQRRVFLKLTAEGEKLYEEIGEEVDERYDAIEEVLGREKMLLLKDLLAELAKIEDALNS [Source organism chain A]=Neisseria meningitidis serogroup B [UniProt ID chain B]=Q7DD70 [UniProt boundaries chain B]=9-145 [UniProt coverage chain B]=93% [Name chain B]=Transcriptional regulator, MarR family [UniProt sequence chain B]=MPTQSKHASINIGLIQAREALMTQFRPILNQANITDQQWRIIRLLAENGTLDFQDLANQACILRPSLTGILTRLEKAGLVVRLKPSNDQRRVFLKLTAEGEKLYEEIGEEVDERYDAIEEVLGREKMLLLKDLLAELAKIEDALNS [Source organism chain B]=Neisseria meningitidis serogroup B [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Neisseria meningitidis serogroup B [Accession]=MF7000157 [Entry] [Entry number]=351 [Entry name]=Yeast kinetochore Spc24/Spc25 [PDB ID]=2fv4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Spc24G and Spc25G associate very stably, even without the long coiled coil regions at the N-terminal ends of the two intact proteins. The small dimer has an unusually large buried surface area, thus, it is reasonable to think of the two subunits as folded together into a single globular domain. Its HSQC spectrum indicates that Spc25G alone is partially unfolded (PMID:16765893). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P40014 [UniProt boundaries chain A]=133-221 [UniProt coverage chain A]=40% [Name chain A]=Kinetochore protein SPC25 [UniProt sequence chain A]=MASIDAFSDLERRMDGFQKDVAQVLARQQNHARQQLQQFQAEMRQLHNQHQHLIDELQRLATQRTALQQQIHAAQQATNTTREQWRSYHERESELSRRQSTLAAQSRELDSLLQQRGKECVQLRARWAAQSGNDAAEVALYERLLQLRVLPGASDVHDVRFVFGDDSRCWIEVAMHGDHVIGNSHPALDPKSRATLEHVLTVQGDLAAFLVVARDMLLASL [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=Q04477 [UniProt boundaries chain B]=156-213 [UniProt coverage chain B]=27% [Name chain B]=Kinetochore protein SPC24 [UniProt sequence chain B]=MSQKDNLLDNPVEFLKEVRESFDIQQDVDAMKRIRHDLDVIKEESEARISKEHSKVSESNKKLNAERINVAKLEGDLEYTNEESNEFGSKDELVKLLKDLDGLERNIVSLRSELDEKMKLYLKDSEIISTPNGSKIKAKVIEPELEEQSAVTPEANENILKLKLYRSLGVILDLENDQVLINRKNDGNIDILPLDNNLSDFYKTKYIWERLGK [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000158 [Entry] [Entry number]=352 [Entry name]=10S myosin II (smooth muscle) [PDB ID]=2fxm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:17095604). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P12883 [UniProt boundaries chain A]=838-963 [UniProt coverage chain A]=6% [Name chain A]=Myosin-7 [UniProt sequence chain A]=MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P12883 [UniProt boundaries chain B]=850-961 [UniProt coverage chain B]=5% [Name chain B]=Myosin-7 [UniProt sequence chain B]=MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Homo sapiens [Accession]=MF7000159 [Entry] [Entry number]=353 [Entry name]=Cyclin T-binding domain of Hexim1 [PDB ID]=2gd7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:17724342). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O94992 [UniProt boundaries chain A]=255-359 [UniProt coverage chain A]=29% [Name chain A]=Protein HEXIM1 [UniProt sequence chain A]=MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O94992 [UniProt boundaries chain B]=255-359 [UniProt coverage chain B]=29% [Name chain B]=Protein HEXIM1 [UniProt sequence chain B]=MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000160 [Entry] [Entry number]=354 [Entry name]=Coiled coil domain of Hexim1 [PDB ID]=3s9g [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:22033481). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O94992 [UniProt boundaries chain A]=266-350 [UniProt coverage chain A]=23% [Name chain A]=Protein HEXIM1 [UniProt sequence chain A]=MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O94992 [UniProt boundaries chain B]=272-350 [UniProt coverage chain B]=22% [Name chain B]=Protein HEXIM1 [UniProt sequence chain B]=MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Homo sapiens [Accession]=MF7000161 [Entry] [Entry number]=355 [Entry name]=Isochorismate-pyruvate lyase (Pseudomonas aeruginosa) [PDB ID]=2h9c [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Chorismate mutase type II [Evidence level]=Indirect evidence [Evidence text]=The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000162,MF7000212,MF7000163,MF7000211,MF7000164,MF7000165,MF7000209,MF7000210 [UniProt ID chain A]=Q51507 [UniProt boundaries chain A]=1-96 [UniProt coverage chain A]=95% [Name chain A]=Isochorismate pyruvate lyase [UniProt sequence chain A]=MKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q51507 [UniProt boundaries chain B]=1-92 [UniProt coverage chain B]=91% [Name chain B]=Isochorismate pyruvate lyase [UniProt sequence chain B]=MKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000162 [Entry] [Entry number]=356 [Entry name]=Isochorismate-pyruvate lyase, K42A mutant (Pseudomonas aeruginosa) [PDB ID]=3hgx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Chorismate mutase type II [Evidence level]=Indirect evidence [Evidence text]=The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000162,MF7000212,MF7000163,MF7000211,MF7000164,MF7000165,MF7000209,MF7000210 [UniProt ID chain A]=Q51507 [UniProt boundaries chain A]=1-99 [UniProt coverage chain A]=98% [Name chain A]=Isochorismate pyruvate lyase [UniProt sequence chain A]=MKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q51507 [UniProt boundaries chain B]=1-99 [UniProt coverage chain B]=98% [Name chain B]=Isochorismate pyruvate lyase [UniProt sequence chain B]=MKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000163 [Entry] [Entry number]=357 [Entry name]=Isochorismate-pyruvate lyase (Pseudomonas aeruginosa) [PDB ID]=3rem [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Chorismate mutase type II [Evidence level]=Indirect evidence [Evidence text]=The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000162,MF7000212,MF7000163,MF7000211,MF7000164,MF7000165,MF7000209,MF7000210 [UniProt ID chain A]=Q51507 [UniProt boundaries chain A]=2-98 [UniProt coverage chain A]=96% [Name chain A]=Isochorismate pyruvate lyase [UniProt sequence chain A]=MKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q51507 [UniProt boundaries chain B]=2-98 [UniProt coverage chain B]=96% [Name chain B]=Isochorismate pyruvate lyase [UniProt sequence chain B]=MKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000164 [Entry] [Entry number]=358 [Entry name]=Isochorismate-pyruvate lyase, K42E mutant (Pseudomonas aeruginosa) [PDB ID]=3ret [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Chorismate mutase type II [Evidence level]=Indirect evidence [Evidence text]=The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000162,MF7000212,MF7000163,MF7000211,MF7000164,MF7000165,MF7000209,MF7000210 [UniProt ID chain A]=Q51507 [UniProt boundaries chain A]=1-97 [UniProt coverage chain A]=96% [Name chain A]=Isochorismate pyruvate lyase [UniProt sequence chain A]=MKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q51507 [UniProt boundaries chain B]=1-97 [UniProt coverage chain B]=96% [Name chain B]=Isochorismate pyruvate lyase [UniProt sequence chain B]=MKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=1.79 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000165 [Entry] [Entry number]=359 [Entry name]=Copper-specific repressor (CsoR) (Mycobacterium tuberculosis) [PDB ID]=2hh7 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Copper-loaded CsoR has a homodimeric antiparallel four-helix bundle architecture. A helical hairpin of the a1 and a2 helices is packed against a hairpin of a1'- a2' from the other protomer to form a standard antiparallel four-helix bundle (PMID:17143269). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P9WP49 [UniProt boundaries chain A]=4-88 [UniProt coverage chain A]=71% [Name chain A]=Copper-sensing transcriptional repressor CsoR [UniProt sequence chain A]=MSKELTAKKRAALNRLKTVRGHLDGIVRMLESDAYCVDVMKQISAVQSSLERANRVMLHNHLETCFSTAVLDGHGQAAIEELIDAVKFTPALTGPHARLGGAAVGESATEEPMPDASNM [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=P9WP49 [UniProt boundaries chain A-2]=4-88 [UniProt coverage chain A-2]=71% [Name chain A-2]=Copper-sensing transcriptional repressor CsoR [UniProt sequence chain A-2]=MSKELTAKKRAALNRLKTVRGHLDGIVRMLESDAYCVDVMKQISAVQSSLERANRVMLHNHLETCFSTAVLDGHGQAAIEELIDAVKFTPALTGPHARLGGAAVGESATEEPMPDASNM [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.55 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000166 [Entry] [Entry number]=360 [Entry name]=Histoplasma capsulatum CBP Homodimer [PDB ID]=2jv7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Highly intertwined homodimer that is formed by a head-to-tail interaction of the two monomers involving all four helices (PMID:19298372). Disruption of the dimer would expose at least 12 of these residues to the solvent, suggesting that the dimer is the energetically favorable form. This correlates well with previous unfolding data that indicated that an isolated monomeric form of CBP is unstable (Beck et al., 2008). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O42720 [UniProt boundaries chain A]=33-110 [UniProt coverage chain A]=70% [Name chain A]=Calcium-binding protein [UniProt sequence chain A]=MLFSKVIAPAFILLGAASAAPGGLAPENASKRDQPSVGDAFDKYNEAVRVFTQLSSAANCDWAACLSSLSASSAACIAAVGELGLDVPLDLACAATATSSATEACKGCLW [Source organism chain A]= [UniProt ID chain B]=O42720 [UniProt boundaries chain B]=33-110 [UniProt coverage chain B]=70% [Name chain B]=Calcium-binding protein [UniProt sequence chain B]=MLFSKVIAPAFILLGAASAAPGGLAPENASKRDQPSVGDAFDKYNEAVRVFTQLSSAANCDWAACLSSLSASSAACIAAVGELGLDVPLDLACAATATSSATEACKGCLW [Source organism chain B]= [ExpTech]=NMR [Resolution]=N/A [Source organism]= [Accession]=MF7000167 [Entry] [Entry number]=362 [Entry name]=GIT1 [PDB ID]=2w6a [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:19136011). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9Z272 [UniProt boundaries chain A]=427-483 [UniProt coverage chain A]=7% [Name chain A]=ARF GTPase-activating protein GIT1 [UniProt sequence chain A]=MSRKGPRAEVCADCSAPDPGWASISRGVLVCDECCSVHRSLGRHISIVKHLRHSAWPPTLLQMVHTLASNGANSIWEHSLLDPAQVQSGRRKANPQDKVHPIKSEFIRAKYQMLAFVHKLPCRDDDGVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGTTPLHVAAKAGQTLQAELLVVYGADPGSPDVNGRTPIDYARQAGHHELAERLVECQYELTDRLAFYLCGRKPDHKNGHYIIPQMADRSRQKCMSQSLDLSELAKAAKKKLQALSNRLFEELAMDVYDEVDRRENDAVWLATQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSEAKRRQQGKSLSSPTDNLELSARNQSDLDDQHDYDSVASDEDTDQEPLPSAGATRNNRARSMDSSDLSDGAVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRKLQREIHKLQAENLQLRQPPGPVPVPSLPSERAEHTLMGPGGSTHRRDRQAFSMYEPGSALKPFGGAPGDELATRLQPFHSTELEDDAIYSVHVPAGLYRIRKGVSASSVTFTPSSPLLSSSQEGSRHASKLSRHGSGAESDYENTQSGEPLLGLEGKRFLELSKEDELHAELESLDGDPDPGLPSTEDVILKTEQVTKNIQELLRAAQEFKHDSFVPCSEKIHLAVTEMASLFPKRPALEPVRSSLRLLNASAYRLQSECRKTVPPEPGAPVDFQLLTQQVIQCAYDIAKAAKQLVTITTREKKQ [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=Q9Z272 [UniProt boundaries chain B]=427-482 [UniProt coverage chain B]=7% [Name chain B]=ARF GTPase-activating protein GIT1 [UniProt sequence chain B]=MSRKGPRAEVCADCSAPDPGWASISRGVLVCDECCSVHRSLGRHISIVKHLRHSAWPPTLLQMVHTLASNGANSIWEHSLLDPAQVQSGRRKANPQDKVHPIKSEFIRAKYQMLAFVHKLPCRDDDGVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGTTPLHVAAKAGQTLQAELLVVYGADPGSPDVNGRTPIDYARQAGHHELAERLVECQYELTDRLAFYLCGRKPDHKNGHYIIPQMADRSRQKCMSQSLDLSELAKAAKKKLQALSNRLFEELAMDVYDEVDRRENDAVWLATQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSEAKRRQQGKSLSSPTDNLELSARNQSDLDDQHDYDSVASDEDTDQEPLPSAGATRNNRARSMDSSDLSDGAVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRKLQREIHKLQAENLQLRQPPGPVPVPSLPSERAEHTLMGPGGSTHRRDRQAFSMYEPGSALKPFGGAPGDELATRLQPFHSTELEDDAIYSVHVPAGLYRIRKGVSASSVTFTPSSPLLSSSQEGSRHASKLSRHGSGAESDYENTQSGEPLLGLEGKRFLELSKEDELHAELESLDGDPDPGLPSTEDVILKTEQVTKNIQELLRAAQEFKHDSFVPCSEKIHLAVTEMASLFPKRPALEPVRSSLRLLNASAYRLQSECRKTVPPEPGAPVDFQLLTQQVIQCAYDIAKAAKQLVTITTREKKQ [Source organism chain B]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Rattus norvegicus [Accession]=MF7000169 [Entry] [Entry number]=363 [Entry name]=Proline utilization A (PutA) DNA-binding domain (Pseudomonas putida) [PDB ID]=2jxg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=PutA, RHH domain [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:18767154). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2120033,MF7000170,MF7000171 [UniProt ID chain A]=Q9R9T7 [UniProt boundaries chain A]=1-45 [UniProt coverage chain A]=3% [Name chain A]=Bifunctional protein PutA [UniProt sequence chain A]=MATTTLGVKLDDPTRERLKAAAQSIDRTPHWLIKQAIFNYLEKLEGGATLTELNGHASNPADDAGEVQADHSHQCFLEFAESILPQSVLRSAITAAYRRPEQEVVPMLLEQARLSAPLADATNKLAASIAEKLRNQKSVGGRAGIVQGLLQEFSLSSQERRGVCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNETGLTSSLTRIIGKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANASRFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWNGIGFVIQAYQKRCPYLINYFFDLAKRTPHRLIIRLLKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYVACARKLLAVPEAIYPQFATHNAHTLSAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKIADGKLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADHSISIQELVADRWPASIAWVPRKGSIGLPHPRIPLPRDLYGTERAKLAGIEMANEHRLGLLSCAMVATAHKQWEAAPLLACAARESAAAPVLNPADHRNVVGHVQEATVAKFDNAIHCALNPAPIWQATPPAERAAILERTADLMEAEIHPLMGLLIREAGKTFPNAIAELREAVDFLRYYAVQALNDFSNDAHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNVAGRLDNQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGCPDRLAVDIGPVIDAEAKAGIEKHIQGMREKGRPVYQVAIADAAEIKRGTFVMPTLIELDSFDELKREIFGPVLHVVRYNRRNLDQLIEQINNSGYGLTLGVHTRIDETIAKVVETATPATCRHRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPADAIGRHFQQQDGEGTPDRTLHEQLVKPLHGLKAWAENNQLADLAALCSQFASQSQSGIARLLPGPTGERNSYTILPREHVLCLADNETDLLAQFAAVLAVGSSAVWVDGEPGKALRARLPRELQAKVKLVADWNKDEVAFDAVIHHGDSDQLRGVCQQVAKRAGAIVGVHGLSSGDHQIALERLVIERAVSVNTAAAGGNASLMTIG [Source organism chain A]=Pseudomonas putida [UniProt ID chain B]=Q9R9T7 [UniProt boundaries chain B]=1-45 [UniProt coverage chain B]=3% [Name chain B]=Bifunctional protein PutA [UniProt sequence chain B]=MATTTLGVKLDDPTRERLKAAAQSIDRTPHWLIKQAIFNYLEKLEGGATLTELNGHASNPADDAGEVQADHSHQCFLEFAESILPQSVLRSAITAAYRRPEQEVVPMLLEQARLSAPLADATNKLAASIAEKLRNQKSVGGRAGIVQGLLQEFSLSSQERRGVCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNETGLTSSLTRIIGKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANASRFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWNGIGFVIQAYQKRCPYLINYFFDLAKRTPHRLIIRLLKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYVACARKLLAVPEAIYPQFATHNAHTLSAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKIADGKLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADHSISIQELVADRWPASIAWVPRKGSIGLPHPRIPLPRDLYGTERAKLAGIEMANEHRLGLLSCAMVATAHKQWEAAPLLACAARESAAAPVLNPADHRNVVGHVQEATVAKFDNAIHCALNPAPIWQATPPAERAAILERTADLMEAEIHPLMGLLIREAGKTFPNAIAELREAVDFLRYYAVQALNDFSNDAHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNVAGRLDNQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGCPDRLAVDIGPVIDAEAKAGIEKHIQGMREKGRPVYQVAIADAAEIKRGTFVMPTLIELDSFDELKREIFGPVLHVVRYNRRNLDQLIEQINNSGYGLTLGVHTRIDETIAKVVETATPATCRHRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPADAIGRHFQQQDGEGTPDRTLHEQLVKPLHGLKAWAENNQLADLAALCSQFASQSQSGIARLLPGPTGERNSYTILPREHVLCLADNETDLLAQFAAVLAVGSSAVWVDGEPGKALRARLPRELQAKVKLVADWNKDEVAFDAVIHHGDSDQLRGVCQQVAKRAGAIVGVHGLSSGDHQIALERLVIERAVSVNTAAAGGNASLMTIG [Source organism chain B]=Pseudomonas putida [ExpTech]=NMR [Resolution]=N/A [Source organism]=Pseudomonas putida [Accession]=MF7000170 [Entry] [Entry number]=364 [Entry name]=Proline utilization A (PutA) DNA-binding domain (Pseudomonas putida) [PDB ID]=2jxh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=PutA, RHH domain [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:18767154). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2120033,MF7000170,MF7000171 [UniProt ID chain A]=Q9R9T7 [UniProt boundaries chain A]=1-45 [UniProt coverage chain A]=3% [Name chain A]=Bifunctional protein PutA [UniProt sequence chain A]=MATTTLGVKLDDPTRERLKAAAQSIDRTPHWLIKQAIFNYLEKLEGGATLTELNGHASNPADDAGEVQADHSHQCFLEFAESILPQSVLRSAITAAYRRPEQEVVPMLLEQARLSAPLADATNKLAASIAEKLRNQKSVGGRAGIVQGLLQEFSLSSQERRGVCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNETGLTSSLTRIIGKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANASRFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWNGIGFVIQAYQKRCPYLINYFFDLAKRTPHRLIIRLLKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYVACARKLLAVPEAIYPQFATHNAHTLSAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKIADGKLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADHSISIQELVADRWPASIAWVPRKGSIGLPHPRIPLPRDLYGTERAKLAGIEMANEHRLGLLSCAMVATAHKQWEAAPLLACAARESAAAPVLNPADHRNVVGHVQEATVAKFDNAIHCALNPAPIWQATPPAERAAILERTADLMEAEIHPLMGLLIREAGKTFPNAIAELREAVDFLRYYAVQALNDFSNDAHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNVAGRLDNQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGCPDRLAVDIGPVIDAEAKAGIEKHIQGMREKGRPVYQVAIADAAEIKRGTFVMPTLIELDSFDELKREIFGPVLHVVRYNRRNLDQLIEQINNSGYGLTLGVHTRIDETIAKVVETATPATCRHRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPADAIGRHFQQQDGEGTPDRTLHEQLVKPLHGLKAWAENNQLADLAALCSQFASQSQSGIARLLPGPTGERNSYTILPREHVLCLADNETDLLAQFAAVLAVGSSAVWVDGEPGKALRARLPRELQAKVKLVADWNKDEVAFDAVIHHGDSDQLRGVCQQVAKRAGAIVGVHGLSSGDHQIALERLVIERAVSVNTAAAGGNASLMTIG [Source organism chain A]=Pseudomonas putida [UniProt ID chain B]=Q9R9T7 [UniProt boundaries chain B]=1-45 [UniProt coverage chain B]=3% [Name chain B]=Bifunctional protein PutA [UniProt sequence chain B]=MATTTLGVKLDDPTRERLKAAAQSIDRTPHWLIKQAIFNYLEKLEGGATLTELNGHASNPADDAGEVQADHSHQCFLEFAESILPQSVLRSAITAAYRRPEQEVVPMLLEQARLSAPLADATNKLAASIAEKLRNQKSVGGRAGIVQGLLQEFSLSSQERRGVCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNETGLTSSLTRIIGKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANASRFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWNGIGFVIQAYQKRCPYLINYFFDLAKRTPHRLIIRLLKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYVACARKLLAVPEAIYPQFATHNAHTLSAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKIADGKLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADHSISIQELVADRWPASIAWVPRKGSIGLPHPRIPLPRDLYGTERAKLAGIEMANEHRLGLLSCAMVATAHKQWEAAPLLACAARESAAAPVLNPADHRNVVGHVQEATVAKFDNAIHCALNPAPIWQATPPAERAAILERTADLMEAEIHPLMGLLIREAGKTFPNAIAELREAVDFLRYYAVQALNDFSNDAHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNVAGRLDNQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGCPDRLAVDIGPVIDAEAKAGIEKHIQGMREKGRPVYQVAIADAAEIKRGTFVMPTLIELDSFDELKREIFGPVLHVVRYNRRNLDQLIEQINNSGYGLTLGVHTRIDETIAKVVETATPATCRHRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPADAIGRHFQQQDGEGTPDRTLHEQLVKPLHGLKAWAENNQLADLAALCSQFASQSQSGIARLLPGPTGERNSYTILPREHVLCLADNETDLLAQFAAVLAVGSSAVWVDGEPGKALRARLPRELQAKVKLVADWNKDEVAFDAVIHHGDSDQLRGVCQQVAKRAGAIVGVHGLSSGDHQIALERLVIERAVSVNTAAAGGNASLMTIG [Source organism chain B]=Pseudomonas putida [ExpTech]=NMR [Resolution]=N/A [Source organism]=Pseudomonas putida [Accession]=MF7000171 [Entry] [Entry number]=365 [Entry name]=Plasmid copy control protein ORF56 (Sulfolobus islandicus) [PDB ID]=2k9i [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Arc-type ribbon-helix-helix [Evidence level]=Direct evidence [Evidence text]=The protein showed an extremely high stability in denaturant, heat, and pH-induced unfolding transitions, which can be well described by a two-state reaction between native dimers and unfolded monomers (PMID:14741218). The interacting chains form a ribbon-helix-helix (RHH) structure. These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000176,MF7000173 [UniProt ID chain A]=Q54323 [UniProt boundaries chain A]=2-56 [UniProt coverage chain A]=98% [Name chain A]=CopG domain protein DNA-binding domain protein [UniProt sequence chain A]=MGRPYKLLNGIKLGVYIPQEWHDRLMEIAKEKNLTLSDVCRLAIKEYLDNHDKQKK [Source organism chain A]=Sulfolobus islandicus [UniProt ID chain B]=Q54323 [UniProt boundaries chain B]=2-56 [UniProt coverage chain B]=98% [Name chain B]=CopG domain protein DNA-binding domain protein [UniProt sequence chain B]=MGRPYKLLNGIKLGVYIPQEWHDRLMEIAKEKNLTLSDVCRLAIKEYLDNHDKQKK [Source organism chain B]=Sulfolobus islandicus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Sulfolobus islandicus [Accession]=MF7000173 [Entry] [Entry number]=366 [Entry name]=Plasmid copy control protein ORF56 (Sulfolobus islandicus) [PDB ID]=3ft7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:19788170). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:9857196). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). Furthermore, CopG was directly shown to associate and fold cooperatively via a two state folding and binding process (PMID:9857196,PMID:15169951). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q54323 [UniProt boundaries chain A]=8-52 [UniProt coverage chain A]=80% [Name chain A]=CopG domain protein DNA-binding domain protein [UniProt sequence chain A]=MGRPYKLLNGIKLGVYIPQEWHDRLMEIAKEKNLTLSDVCRLAIKEYLDNHDKQKK [Source organism chain A]=Sulfolobus islandicus [UniProt ID chain B]=Q54323 [UniProt boundaries chain B]=7-52 [UniProt coverage chain B]=82% [Name chain B]=CopG domain protein DNA-binding domain protein [UniProt sequence chain B]=MGRPYKLLNGIKLGVYIPQEWHDRLMEIAKEKNLTLSDVCRLAIKEYLDNHDKQKK [Source organism chain B]=Sulfolobus islandicus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Sulfolobus islandicus [Accession]=MF7000174 [Entry] [Entry number]=367 [Entry name]=C-terminal dimerization domain of Borealin [PDB ID]=2kdd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=No monomer was observed in size-exclusion chromatography. Large changes occurred in the HSQC spectra of T230A, T230D, and T230K Borealin 207−280 fragments when compared to the wild type, consistent with a substantial loss of structure. The complexes containing Borealin T230D and T230A are monomeric in solution. The Circular Dichroism titration has three states (PMID:19530738) [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q53HL2 [UniProt boundaries chain A]=224-280 [UniProt coverage chain A]=20% [Name chain A]=Borealin [UniProt sequence chain A]=MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q53HL2 [UniProt boundaries chain B]=224-280 [UniProt coverage chain B]=20% [Name chain B]=Borealin [UniProt sequence chain B]=MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000175 [Entry] [Entry number]=368 [Entry name]=Archeal SvtR [PDB ID]=2kel [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Arc-type ribbon-helix-helix [Evidence level]=Direct evidence [Evidence text]=The protein showed an extremely high stability in denaturant, heat, and pH-induced unfolding transitions, which can be well described by a two-state reaction between native dimers and unfolded monomers (PMID:14741218). The interacting chains form a ribbon-helix-helix (RHH) structure. These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000176,MF7000173 [UniProt ID chain A]=Q8QL46 [UniProt boundaries chain A]=11-56 [UniProt coverage chain A]=82% [Name chain A]=Uncharacterized protein 56B [UniProt sequence chain A]=MQTQEQSQKKKQKAVFGIYMDKDLKTRLKVYCAKNNLQLTQAIEEAIKEYLQKRNG [Source organism chain A]=SIRV-1) [UniProt ID chain B]=Q8QL46 [UniProt boundaries chain B]=11-56 [UniProt coverage chain B]=82% [Name chain B]=Uncharacterized protein 56B [UniProt sequence chain B]=MQTQEQSQKKKQKAVFGIYMDKDLKTRLKVYCAKNNLQLTQAIEEAIKEYLQKRNG [Source organism chain B]=SIRV-1) [ExpTech]=NMR [Resolution]=N/A [Source organism]=SIRV-1) [Accession]=MF7000176 [Entry] [Entry number]=369 [Entry name]=Omega Transcriptional Repressor [PDB ID]=1irq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:11733997). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:9857196). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). Furthermore, CopG was directly shown to associate and fold cooperatively via a two state folding and binding process (PMID:9857196,PMID:15169951). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q57468 [UniProt boundaries chain A]=24-71 [UniProt coverage chain A]=67% [Name chain A]=Transcriptional repressor [UniProt sequence chain A]=MIVGNLGAQKAKRNDTPISAKKDIMGDKTVRVRADLHHIIKIETAKNGGNVKEVMDQALEEYIRKYLPDKL [Source organism chain A]=Streptococcus pyogenes [UniProt ID chain B]=Q57468 [UniProt boundaries chain B]=23-71 [UniProt coverage chain B]=69% [Name chain B]=Transcriptional repressor [UniProt sequence chain B]=MIVGNLGAQKAKRNDTPISAKKDIMGDKTVRVRADLHHIIKIETAKNGGNVKEVMDQALEEYIRKYLPDKL [Source organism chain B]=Streptococcus pyogenes [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Streptococcus pyogenes [Accession]=MF7000177 [Entry] [Entry number]=370 [Entry name]=C-terminal non-repetitive domain of ADF-3 [PDB ID]=2khm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Spidroin, C-terminal domain [Sequence domain]=Major ampullate spidroin 1 and 2 [Evidence level]=Direct evidence [Evidence text]=Circular dichroism of the C-terminal domain fits two-state unfolding model (PMID:23418525). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000178,MF7000179,MF7000180 [UniProt ID chain A]=Q16987 [UniProt boundaries chain A]=513-636 [UniProt coverage chain A]=19% [Name chain A]=Fibroin-3 [UniProt sequence chain A]=ARAGSGQQGPGQQGPGQQGPGQQGPYGPGASAAAAAAGGYGPGSGQQGPSQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQQGPGGQGPYGPGSSAAAAAAGGNGPGSGQQGAGQQGPGQQGPGASAAAAAAGGYGPGSGQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQQGPGQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGYGQQGPGQQGPGGQGPYGPGASAASAASGGYGPGSGQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQQGPGQQGPGQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGGQGAYGPGASAAAGAAGGYGPGSGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPYGPGASAAAAAAGGYGPGSGQQGPGQQGPGQQGPGGQGPYGPGAASAAVSVGGYGPQSSSVPVASAVASRLSSPAASSRVSSAVSSLVSSGPTKHAALSNTISSVVSQVSASNPGLSGCDVLVQALLEVVSALVSILGSSSIGQINYGASAQYTQMVGQSVAQALA [Source organism chain A]=Araneus diadematus [UniProt ID chain B]=Q16987 [UniProt boundaries chain B]=513-636 [UniProt coverage chain B]=19% [Name chain B]=Fibroin-3 [UniProt sequence chain B]=ARAGSGQQGPGQQGPGQQGPGQQGPYGPGASAAAAAAGGYGPGSGQQGPSQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQQGPGGQGPYGPGSSAAAAAAGGNGPGSGQQGAGQQGPGQQGPGASAAAAAAGGYGPGSGQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQQGPGQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGYGQQGPGQQGPGGQGPYGPGASAASAASGGYGPGSGQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQQGPGQQGPGQQGPGQQGPGGQGPYGPGASAAAAAAGGYGPGSGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGGQGAYGPGASAAAGAAGGYGPGSGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPGQQGPYGPGASAAAAAAGGYGPGSGQQGPGQQGPGQQGPGGQGPYGPGAASAAVSVGGYGPQSSSVPVASAVASRLSSPAASSRVSSAVSSLVSSGPTKHAALSNTISSVVSQVSASNPGLSGCDVLVQALLEVVSALVSILGSSSIGQINYGASAQYTQMVGQSVAQALA [Source organism chain B]=Araneus diadematus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Araneus diadematus [Accession]=MF7000178 [Entry] [Entry number]=371 [Entry name]=Spidroin domains of minor ampullate fibroin 1 [PDB ID]=2m0m [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Spidroin, C-terminal domain [Sequence domain]=Major ampullate spidroin 1 and 2 [Evidence level]=Direct evidence [Evidence text]=Circular dichroism of the C-terminal domain fits two-state unfolding model (PMID:23418525). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000178,MF7000179,MF7000180 [UniProt ID chain A]=Q2LC34 [UniProt boundaries chain A]=250-356 [UniProt coverage chain A]=30% [Name chain A]=Minor ampullate fibroin 1 [UniProt sequence chain A]=GAAASGAGAGGAGGYGRGAGAGAGAGAGSAAGNAFAQSLSSNLLSSGDFVQMISSTTSTDQAVSVATSVAQNVGNQLGLDANAMNSLLGAVSGYVSTLGNAISDASAYANAISSAIGNVLANSGSISESTASSAASSAASSVTTTLTSYGPAVFYAPTSSAGGYGGLVGYGAGAGAAAGAGAGAGGAGGYIGQGGYGAGAGAAAAAGAGAGATGGYGRGAGAGATNAGGYGGQGGYGAGARAFAGAGVGVGTTVASTTSRLSTAEASSRISTAASTLVSGGYLNTAALPSVIADLFAQVGASSPGVSDSEVLIQVLLEIVSSLIHILSSSSVGQVDFSSVGSSAAAVGQSMQVVMG [Source organism chain A]=Trichonephila antipodiana [UniProt ID chain B]=Q2LC34 [UniProt boundaries chain B]=250-356 [UniProt coverage chain B]=30% [Name chain B]=Minor ampullate fibroin 1 [UniProt sequence chain B]=GAAASGAGAGGAGGYGRGAGAGAGAGAGSAAGNAFAQSLSSNLLSSGDFVQMISSTTSTDQAVSVATSVAQNVGNQLGLDANAMNSLLGAVSGYVSTLGNAISDASAYANAISSAIGNVLANSGSISESTASSAASSAASSVTTTLTSYGPAVFYAPTSSAGGYGGLVGYGAGAGAAAGAGAGAGGAGGYIGQGGYGAGAGAAAAAGAGAGATGGYGRGAGAGATNAGGYGGQGGYGAGARAFAGAGVGVGTTVASTTSRLSTAEASSRISTAASTLVSGGYLNTAALPSVIADLFAQVGASSPGVSDSEVLIQVLLEIVSSLIHILSSSSVGQVDFSSVGSSAAAVGQSMQVVMG [Source organism chain B]=Trichonephila antipodiana [ExpTech]=NMR [Resolution]=N/A [Source organism]=Trichonephila antipodiana [Accession]=MF7000179 [Entry] [Entry number]=372 [Entry name]=C-terminal domain of minor ampullate spidroin (MiSp) [PDB ID]=2mfz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Spidroin, C-terminal domain [Sequence domain]=Major ampullate spidroin 1 and 2 [Evidence level]=Direct evidence [Evidence text]=Circular dichroism of the C-terminal domain fits two-state unfolding model (PMID:23418525). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000178,MF7000179,MF7000180 [UniProt ID chain A]=K4MTL7 [UniProt boundaries chain A]=1647-1766 [UniProt coverage chain A]=6% [Name chain A]=Minor ampullate spidroin [UniProt sequence chain A]=MQLPTRLSFFFLVLFIQGFLSQSQPIWTNPNAAMTMTNNLVQCASRSGVLTADQMDDMGMMADSVNSQMQKMGPNPPQHRLRAMNTAMAAEVAEVVATSPPQSYSAVLNTIGACLRESMMQATGSVDNAFTNEVMQLVKMLSADSANEVSTASASGASYATSTSSAVSSSQATGYSTAAGYGNAAGAGAGAAAAVSGGAGSAGGYGEGAGAGVRSGAGASAGAAGGYGRATGAGAGGAAAAGASGYGGSYGAGAGAGAAGAGGASAYGAGIGGGYGAGAADAYGGGASAGAGAGAGAGVSGGYGRAAGAGAAAAAGANGYGGSYDAGVGAGTAGAGAGAGASGGYGGGAGEGAGAAAAAGAGAGGAGGYGGGAGSGAGAVARAGAGGAGGYGSGIGGGYGSGAGAAAGAGAGGAGAYGGGYGTGAGAGARGADSAGAAAGYGGGVGTGTGSSAGYGRGAGAGAGAGAAAGSGAGAAGGYGGGYGAGAGAGAGAGGATGNRAGDAFAQVFSQNVINSGVITSTTVTKNSAQAAASSMVSTAAKSLGLDENTARSMANAMSSYAAAMAKSFRNSDEFIRNMSYQMGRMLSNAGAINESTASAAASSASSTVTETVRTYGPAAIFSGAGAGGAGGYAQGYGAGAGAGAGAGTGAGGAGGYGQGYGAGSGAGAGGAGGYGAGAGAGAGAGGASGYGQGYGDGAGAGAGAAAAAGAAAGARGAGGYGGGAGDGAGAGAGAGAAGGYGQGYGAGEGAGAGAGAGGAGGYGAGAGAGGAGGYGQSYGDGAAAAAGSGAGAGGSGGYGAGAGAGAGAGAGSGAGAAGGYGGGAGAGVGAGGAGGYDQGYGAGAGAGSGAGAGGAGGYGGGAGAGADAGAGGAGGYGGGAGAGAGARAGAGGVGGYGQSYGAGAGAGAGVGAGGAGAGGADGYGQGYGAGAGTGAGDAGGYGGGAGAGASAGAGGYGGGAGAGGVGVYGKGYGSGSGAGAAAAAGAGGATGNRAGDAFAQVFSQNVINSGVITSTTVTKNSAQAAASSMVSTAAKSLGLDENTARSMANAMSSYAAAMAKSFRNSDEFIRNMSYQMGRMLSNAGAINESTASAAASSASSTVTETVRTYGPAAIFSGAGAGGAGGYAQGYGAGAGAGAGAGTGAGGAGGYGQGYGAGSGAGAGGAGGYGAGAGAGAGAGDASGYGQGYGDGAGAGAGAAAAAGAAAGARGAGGYGGGAGAGAGAGAGAAGGYGQGYGAGAGEGAGAGAGAGAVAGAGAAAAAGAGAGAGGAEGYGAGAGAGGAGGYGQSYGDGAAAAAGSGAGAGGSGGYGAGAGAGSGAGAAGGYGGGAGAGVGAGGEGGYDQGYGAGAGAGSGGGAGGAGGYGGGAGAGSGGGAGGAGGYGGGAGAGAGAGAGGAGGYGGGAGAGTGARAGAGGVGGYGQSYGAGASAAAGAGVGAGGAGAGGAGGYGQGYGAGAGIGAGDAGGYGGGAGAGASAGAGGYGGGAGAGAGGVGGYGKGYGAGSGAGAAAAAGAGAGSAGGYGRGDGAGAGGASGYGQGYGAGAAAGAAATAGAGASVAGGYGGGAGAAAGAGAGGYGGGYGAVAGSGAGAAAAASSGAGGAAGYGRGYGAGSGAGAGAGTVAAYGGAGGVATSSSSATASGSRIVTSGGYGYGTSAAAGAGVAAGSYAGAVNRLSSAEAASRVSSNIAAIASGGASALPSVISNIYSGVVASGVSSNEALIQALLELLSALVHVLSSASIGNVSSVGVDSTLNVVQDSVGQYVG [Source organism chain A]=Araneus ventricosus [UniProt ID chain B]=K4MTL7 [UniProt boundaries chain B]=1647-1766 [UniProt coverage chain B]=6% [Name chain B]=Minor ampullate spidroin [UniProt sequence chain B]=MQLPTRLSFFFLVLFIQGFLSQSQPIWTNPNAAMTMTNNLVQCASRSGVLTADQMDDMGMMADSVNSQMQKMGPNPPQHRLRAMNTAMAAEVAEVVATSPPQSYSAVLNTIGACLRESMMQATGSVDNAFTNEVMQLVKMLSADSANEVSTASASGASYATSTSSAVSSSQATGYSTAAGYGNAAGAGAGAAAAVSGGAGSAGGYGEGAGAGVRSGAGASAGAAGGYGRATGAGAGGAAAAGASGYGGSYGAGAGAGAAGAGGASAYGAGIGGGYGAGAADAYGGGASAGAGAGAGAGVSGGYGRAAGAGAAAAAGANGYGGSYDAGVGAGTAGAGAGAGASGGYGGGAGEGAGAAAAAGAGAGGAGGYGGGAGSGAGAVARAGAGGAGGYGSGIGGGYGSGAGAAAGAGAGGAGAYGGGYGTGAGAGARGADSAGAAAGYGGGVGTGTGSSAGYGRGAGAGAGAGAAAGSGAGAAGGYGGGYGAGAGAGAGAGGATGNRAGDAFAQVFSQNVINSGVITSTTVTKNSAQAAASSMVSTAAKSLGLDENTARSMANAMSSYAAAMAKSFRNSDEFIRNMSYQMGRMLSNAGAINESTASAAASSASSTVTETVRTYGPAAIFSGAGAGGAGGYAQGYGAGAGAGAGAGTGAGGAGGYGQGYGAGSGAGAGGAGGYGAGAGAGAGAGGASGYGQGYGDGAGAGAGAAAAAGAAAGARGAGGYGGGAGDGAGAGAGAGAAGGYGQGYGAGEGAGAGAGAGGAGGYGAGAGAGGAGGYGQSYGDGAAAAAGSGAGAGGSGGYGAGAGAGAGAGAGSGAGAAGGYGGGAGAGVGAGGAGGYDQGYGAGAGAGSGAGAGGAGGYGGGAGAGADAGAGGAGGYGGGAGAGAGARAGAGGVGGYGQSYGAGAGAGAGVGAGGAGAGGADGYGQGYGAGAGTGAGDAGGYGGGAGAGASAGAGGYGGGAGAGGVGVYGKGYGSGSGAGAAAAAGAGGATGNRAGDAFAQVFSQNVINSGVITSTTVTKNSAQAAASSMVSTAAKSLGLDENTARSMANAMSSYAAAMAKSFRNSDEFIRNMSYQMGRMLSNAGAINESTASAAASSASSTVTETVRTYGPAAIFSGAGAGGAGGYAQGYGAGAGAGAGAGTGAGGAGGYGQGYGAGSGAGAGGAGGYGAGAGAGAGAGDASGYGQGYGDGAGAGAGAAAAAGAAAGARGAGGYGGGAGAGAGAGAGAAGGYGQGYGAGAGEGAGAGAGAGAVAGAGAAAAAGAGAGAGGAEGYGAGAGAGGAGGYGQSYGDGAAAAAGSGAGAGGSGGYGAGAGAGSGAGAAGGYGGGAGAGVGAGGEGGYDQGYGAGAGAGSGGGAGGAGGYGGGAGAGSGGGAGGAGGYGGGAGAGAGAGAGGAGGYGGGAGAGTGARAGAGGVGGYGQSYGAGASAAAGAGVGAGGAGAGGAGGYGQGYGAGAGIGAGDAGGYGGGAGAGASAGAGGYGGGAGAGAGGVGGYGKGYGAGSGAGAAAAAGAGAGSAGGYGRGDGAGAGGASGYGQGYGAGAAAGAAATAGAGASVAGGYGGGAGAAAGAGAGGYGGGYGAVAGSGAGAAAAASSGAGGAAGYGRGYGAGSGAGAGAGTVAAYGGAGGVATSSSSATASGSRIVTSGGYGYGTSAAAGAGVAAGSYAGAVNRLSSAEAASRVSSNIAAIASGGASALPSVISNIYSGVVASGVSSNEALIQALLELLSALVHVLSSASIGNVSSVGVDSTLNVVQDSVGQYVG [Source organism chain B]=Araneus ventricosus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Araneus ventricosus [Accession]=MF7000180 [Entry] [Entry number]=373 [Entry name]=Coiled coil domain of Rtt103p [PDB ID]=5m48 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:29073019). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q05543 [UniProt boundaries chain A]=141-246 [UniProt coverage chain A]=25% [Name chain A]=Regulator of Ty1 transposition protein 103 [UniProt sequence chain A]=MPFSSEQFTTKLNTLEDSQESISSASKWLLLQYRDAPKVAEMWKEYMLRPSVNTRRKLLGLYLMNHVVQQAKGQKIIQFQDSFGKVAAEVLGRINQEFPRDLKKKLSRVVNILKERNIFSKQVVNDIERSLKTESSPVEALVLPQKLKDFAKDYEKLVKMHHNVCAMKMRFDKSSDELDPSSSVYEENFKTISKIGNMAKDIINESILKRESGIHKLQSTLDDEKRHLDEEQNMLSEIEFVLSAKDPSRLNKNVDEDNIIPTYEVGDGDDDDDDGDNDDDDDDDDDDKNYDDRSNDSNYGVTNISTTDKKNEVVEKTDSEHKNSTHNPSDNQFGMKRTHDMIGHDDANDIPEKKVHLDSKTSEDGTFNSEDGHYELDIEGHVGAQTDEGVENSGGVSSSIQDLLSKLAN [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=Q05543 [UniProt boundaries chain A-2]=141-246 [UniProt coverage chain A-2]=25% [Name chain A-2]=Regulator of Ty1 transposition protein 103 [UniProt sequence chain A-2]=MPFSSEQFTTKLNTLEDSQESISSASKWLLLQYRDAPKVAEMWKEYMLRPSVNTRRKLLGLYLMNHVVQQAKGQKIIQFQDSFGKVAAEVLGRINQEFPRDLKKKLSRVVNILKERNIFSKQVVNDIERSLKTESSPVEALVLPQKLKDFAKDYEKLVKMHHNVCAMKMRFDKSSDELDPSSSVYEENFKTISKIGNMAKDIINESILKRESGIHKLQSTLDDEKRHLDEEQNMLSEIEFVLSAKDPSRLNKNVDEDNIIPTYEVGDGDDDDDDGDNDDDDDDDDDDKNYDDRSNDSNYGVTNISTTDKKNEVVEKTDSEHKNSTHNPSDNQFGMKRTHDMIGHDDANDIPEKKVHLDSKTSEDGTFNSEDGHYELDIEGHVGAQTDEGVENSGGVSSSIQDLLSKLAN [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.59 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000181 [Entry] [Entry number]=374 [Entry name]=Dimerization domain of Lsr2 (Mycobacterium tuberculosis) [PDB ID]=4e1p [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Lsr2 [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The structure shows an intimate dimer of two ß-ß-a motifs. No monomers were observed using SEC (PMID:22719899). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000182,MF7000183 [UniProt ID chain A]=P9WIP7 [UniProt boundaries chain A]=4-58 [UniProt coverage chain A]=49% [Name chain A]=Nucleoid-associated protein Lsr2 [UniProt sequence chain A]=MAKKVTVTLVDDFDGSGAADETVEFGLDGVTYEIDLSTKNATKLRGDLKQWVAAGRRVGGRRRGRSGSGRGRGAIDREQSAAIREWARRNGHNVSTRGRIPADVIDAYHAAT [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WIP7 [UniProt boundaries chain B]=4-59 [UniProt coverage chain B]=50% [Name chain B]=Nucleoid-associated protein Lsr2 [UniProt sequence chain B]=MAKKVTVTLVDDFDGSGAADETVEFGLDGVTYEIDLSTKNATKLRGDLKQWVAAGRRVGGRRRGRSGSGRGRGAIDREQSAAIREWARRNGHNVSTRGRIPADVIDAYHAAT [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.73 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000182 [Entry] [Entry number]=375 [Entry name]=Dimerization domain of Lsr2 (Mycobacterium tuberculosis) [PDB ID]=4e1r [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Lsr2 [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The structure shows an intimate dimer of two ß-ß-a motifs. No monomers were observed using SEC (PMID:22719899). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000182,MF7000183 [UniProt ID chain A]=P9WIP7 [UniProt boundaries chain A]=4-58 [UniProt coverage chain A]=49% [Name chain A]=Nucleoid-associated protein Lsr2 [UniProt sequence chain A]=MAKKVTVTLVDDFDGSGAADETVEFGLDGVTYEIDLSTKNATKLRGDLKQWVAAGRRVGGRRRGRSGSGRGRGAIDREQSAAIREWARRNGHNVSTRGRIPADVIDAYHAAT [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WIP7 [UniProt boundaries chain B]=4-59 [UniProt coverage chain B]=50% [Name chain B]=Nucleoid-associated protein Lsr2 [UniProt sequence chain B]=MAKKVTVTLVDDFDGSGAADETVEFGLDGVTYEIDLSTKNATKLRGDLKQWVAAGRRVGGRRRGRSGSGRGRGAIDREQSAAIREWARRNGHNVSTRGRIPADVIDAYHAAT [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.04 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000183 [Entry] [Entry number]=376 [Entry name]=Human lamin-B1 coil 2 [PDB ID]=3tyy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:22265972). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P20700 [UniProt boundaries chain A]=311-385 [UniProt coverage chain A]=12% [Name chain A]=Lamin-B1 [UniProt sequence chain A]=MATATPVPPRMGSRAGGPTTPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEAAGVVVEEELFHQQGTPRASNRSCAIM [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P20700 [UniProt boundaries chain B]=313-383 [UniProt coverage chain B]=12% [Name chain B]=Lamin-B1 [UniProt sequence chain B]=MATATPVPPRMGSRAGGPTTPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEAAGVVVEEELFHQQGTPRASNRSCAIM [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Homo sapiens [Accession]=MF7000184 [Entry] [Entry number]=377 [Entry name]=CDK2-associated protein 1 [PDB ID]=2kw6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The homodimeric structure of CDK2AP1 includes an intrinsically disordered 60-residue N-terminal region and a four-helix bundle dimeric structure. The four-helix bundle structure is predominantly stabilized by hydrophobic interactions involving numerous hydrophobic residues at the dimer interface. CDK2AP1 is a stable dimer in solution, even in the absence of interchain disulfide bond formation. No dimer dissociation was observed under reducing conditions and concentrations as low as 10 μM (PMID:22427660). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O14519 [UniProt boundaries chain A]=61-115 [UniProt coverage chain A]=47% [Name chain A]=Cyclin-dependent kinase 2-associated protein 1 [UniProt sequence chain A]=MSYKPNLAAHMPAAALNAAGSVHSPSTSMATSSQYRQLLSDYGPPSLGYTQGTGNSQVPQSKYAELLAIIEELGKEIRPTYAGSKSAMERLKRGIIHARGLVRECLAETERNARS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O14519 [UniProt boundaries chain B]=61-115 [UniProt coverage chain B]=47% [Name chain B]=Cyclin-dependent kinase 2-associated protein 1 [UniProt sequence chain B]=MSYKPNLAAHMPAAALNAAGSVHSPSTSMATSSQYRQLLSDYGPPSLGYTQGTGNSQVPQSKYAELLAIIEELGKEIRPTYAGSKSAMERLKRGIIHARGLVRECLAETERNARS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000185 [Entry] [Entry number]=378 [Entry name]=S100A16 (apo form) [PDB ID]=2l50 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q96FQ6 [UniProt boundaries chain A]=2-103 [UniProt coverage chain A]=99% [Name chain A]=Protein S100-A16 [UniProt sequence chain A]=MSDCYTELEKAVIVLVENFYKYVSKYSLVKNKISKSSFREMLQKELNHMLSDTGNRKAADKLIQNLDANHDGRISFDEYWTLIGGITGPIAKLIHEQEQQSSS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q96FQ6 [UniProt boundaries chain B]=2-103 [UniProt coverage chain B]=99% [Name chain B]=Protein S100-A16 [UniProt sequence chain B]=MSDCYTELEKAVIVLVENFYKYVSKYSLVKNKISKSSFREMLQKELNHMLSDTGNRKAADKLIQNLDANHDGRISFDEYWTLIGGITGPIAKLIHEQEQQSSS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000186 [Entry] [Entry number]=379 [Entry name]=S100A16 (Ca-bound) [PDB ID]=2l51 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q96FQ6 [UniProt boundaries chain A]=2-103 [UniProt coverage chain A]=99% [Name chain A]=Protein S100-A16 [UniProt sequence chain A]=MSDCYTELEKAVIVLVENFYKYVSKYSLVKNKISKSSFREMLQKELNHMLSDTGNRKAADKLIQNLDANHDGRISFDEYWTLIGGITGPIAKLIHEQEQQSSS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q96FQ6 [UniProt boundaries chain B]=2-103 [UniProt coverage chain B]=99% [Name chain B]=Protein S100-A16 [UniProt sequence chain B]=MSDCYTELEKAVIVLVENFYKYVSKYSLVKNKISKSSFREMLQKELNHMLSDTGNRKAADKLIQNLDANHDGRISFDEYWTLIGGITGPIAKLIHEQEQQSSS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000187 [Entry] [Entry number]=380 [Entry name]=DNA-recognition fold of Sso7c4 [PDB ID]=2l66 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=D0KRA5 [UniProt boundaries chain A]=2-54 [UniProt coverage chain A]=98% [Name chain A]=Transcriptional regulator, AbrB family [UniProt sequence chain A]=MAVEEIVKVSRNYQVTIPAKVRQKFQIKEGDLVKVTFDESEGVVKIQLLKEPWK [Source organism chain A]=Saccharolobus solfataricus [UniProt ID chain B]=D0KRA5 [UniProt boundaries chain B]=2-54 [UniProt coverage chain B]=98% [Name chain B]=Transcriptional regulator, AbrB family [UniProt sequence chain B]=MAVEEIVKVSRNYQVTIPAKVRQKFQIKEGDLVKVTFDESEGVVKIQLLKEPWK [Source organism chain B]=Saccharolobus solfataricus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharolobus solfataricus [Accession]=MF7000188 [Entry] [Entry number]=381 [Entry name]=Histone-like protein, Sso7c4 [PDB ID]=5itj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=A0A0E3K9N8 [UniProt boundaries chain A]=2-49 [UniProt coverage chain A]=88% [Name chain A]=AbrB/MazE/SpoVT family DNA-binding domain-containing protein [UniProt sequence chain A]=MAVEEIVKVSRNYQVTIPAKVRQKFQIKEGDLVKVTFDESEGVVKIQLLKEPWK [Source organism chain A]=Saccharolobus solfataricus [UniProt ID chain B]=A0A0E3K9N8 [UniProt boundaries chain B]=2-49 [UniProt coverage chain B]=88% [Name chain B]=AbrB/MazE/SpoVT family DNA-binding domain-containing protein [UniProt sequence chain B]=MAVEEIVKVSRNYQVTIPAKVRQKFQIKEGDLVKVTFDESEGVVKIQLLKEPWK [Source organism chain B]=Saccharolobus solfataricus [ExpTech]=X-ray [Resolution]=1.63 [Source organism]=Saccharolobus solfataricus [Accession]=MF7000189 [Entry] [Entry number]=382 [Entry name]=Phage φ29-encoded protein p56 [PDB ID]=2le2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The authors suggest that monomeric p56 would probably exhibit reduced stability. Indeed, p56 solution structure strongly suggests that folding and dimerization are strongly coupled (PMID:21890898). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q38503 [UniProt boundaries chain A]=1-56 [UniProt coverage chain A]=100% [Name chain A]=Protein p56 [UniProt sequence chain A]=MVQNDFVDSYDVTMLLQDDDGKQYYEYHKGLSLSDFEVLYGNTADEIIKLRLDKVL [Source organism chain A]=Bacillus phage phi29 [UniProt ID chain B]=Q38503 [UniProt boundaries chain B]=1-56 [UniProt coverage chain B]=100% [Name chain B]=Protein p56 [UniProt sequence chain B]=MVQNDFVDSYDVTMLLQDDDGKQYYEYHKGLSLSDFEVLYGNTADEIIKLRLDKVL [Source organism chain B]=Bacillus phage phi29 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus phage phi29 [Accession]=MF7000190 [Entry] [Entry number]=383 [Entry name]=ID-1 HLH homodimer (mouse) [PDB ID]=6mgm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Basic helix-loop-helix (bHLH) [Sequence domain]=Helix-loop-helix DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294, PMID:9488706). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100009,MF2110021,MF2110023,MF2100010,MF7000192,MF7000402,MF7000403,MF7000444,MF7000371 [UniProt ID chain A]=P20067 [UniProt boundaries chain A]=61-104 [UniProt coverage chain A]=26% [Name chain A]=DNA-binding protein inhibitor ID-1 [UniProt sequence chain A]=MKVASGSAAAAAGPSCSLKAGRTAGEVVLGLSEQSVAISRCAGTRLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTTGGRGLPVRAPLSTLNGEISALAAEVRSESEYYIILQWETEATGGGCPPSLLFRRIAI [Source organism chain A]=Mus musculus [UniProt ID chain B]=P20067 [UniProt boundaries chain B]=55-104 [UniProt coverage chain B]=29% [Name chain B]=DNA-binding protein inhibitor ID-1 [UniProt sequence chain B]=MKVASGSAAAAAGPSCSLKAGRTAGEVVLGLSEQSVAISRCAGTRLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTTGGRGLPVRAPLSTLNGEISALAAEVRSESEYYIILQWETEATGGGCPPSLLFRRIAI [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.79 [Source organism]=Mus musculus [Accession]=MF7000192 [Entry] [Entry number]=384 [Entry name]=BST2/Tetherin [PDB ID]=2xg7 [Chains]=C,A [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Bone marrow stromal antigen 2 [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:20880831). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain C]=N/A [Similar structures]=MF7000193,MF7000283 [UniProt ID chain A]=Q10589 [UniProt boundaries chain A]=72-151 [UniProt coverage chain A]=44% [Name chain A]=Bone marrow stromal antigen 2 [UniProt sequence chain A]=MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ [Source organism chain A]=Homo sapiens [UniProt ID chain C]=Q10589 [UniProt boundaries chain C]=77-151 [UniProt coverage chain C]=41% [Name chain C]=Bone marrow stromal antigen 2 [UniProt sequence chain C]=MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ [Source organism chain C]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.45 [Source organism]=Homo sapiens [Accession]=MF7000193 [Entry] [Entry number]=385 [Entry name]=C-terminal of Get (Saccharomyces cerevisiae) [PDB ID]=3vej [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ubiquitin-like proteins [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=In thermal denaturation measurements of the Get5 dimerization domain two-state melting curve was seen, no folded monomers observed (PMID:22262836). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q12285 [UniProt boundaries chain A]=175-212 [UniProt coverage chain A]=17% [Name chain A]=Ubiquitin-like protein MDY2 [UniProt sequence chain A]=MSTSASGPEHEFVSKFLTLATLTEPKLPKSYTKPLKDVTNLGVPLPTLKYKYKQNRAKKLKLHQDQQGQDNAAVHLTLKKIQAPKFSIEHDFSPSDTILQIKQHLISEEKASHISEIKLLLKGKVLHDNLFLSDLKVTPANSTITVMIKPNPTISKEPEAEKSTNSPAPAPPQELTVPWDDIEALLKNNFENDQAAVRQVMERLQKGWSLAK [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=Q12285 [UniProt boundaries chain B]=175-212 [UniProt coverage chain B]=17% [Name chain B]=Ubiquitin-like protein MDY2 [UniProt sequence chain B]=MSTSASGPEHEFVSKFLTLATLTEPKLPKSYTKPLKDVTNLGVPLPTLKYKYKQNRAKKLKLHQDQQGQDNAAVHLTLKKIQAPKFSIEHDFSPSDTILQIKQHLISEEKASHISEIKLLLKGKVLHDNLFLSDLKVTPANSTITVMIKPNPTISKEPEAEKSTNSPAPAPPQELTVPWDDIEALLKNNFENDQAAVRQVMERLQKGWSLAK [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=1.23 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000194 [Entry] [Entry number]=386 [Entry name]=C-terminal of Get (Saccharomyces cerevisiae) [PDB ID]=2lnz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ubiquitin-like proteins [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=In thermal denaturation measurements of the Get5 dimerization domain two-state melting curve was seen, no folded monomers observed (PMID:22262836). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q12285 [UniProt boundaries chain A]=173-212 [UniProt coverage chain A]=18% [Name chain A]=Ubiquitin-like protein MDY2 [UniProt sequence chain A]=MSTSASGPEHEFVSKFLTLATLTEPKLPKSYTKPLKDVTNLGVPLPTLKYKYKQNRAKKLKLHQDQQGQDNAAVHLTLKKIQAPKFSIEHDFSPSDTILQIKQHLISEEKASHISEIKLLLKGKVLHDNLFLSDLKVTPANSTITVMIKPNPTISKEPEAEKSTNSPAPAPPQELTVPWDDIEALLKNNFENDQAAVRQVMERLQKGWSLAK [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=Q12285 [UniProt boundaries chain B]=173-212 [UniProt coverage chain B]=18% [Name chain B]=Ubiquitin-like protein MDY2 [UniProt sequence chain B]=MSTSASGPEHEFVSKFLTLATLTEPKLPKSYTKPLKDVTNLGVPLPTLKYKYKQNRAKKLKLHQDQQGQDNAAVHLTLKKIQAPKFSIEHDFSPSDTILQIKQHLISEEKASHISEIKLLLKGKVLHDNLFLSDLKVTPANSTITVMIKPNPTISKEPEAEKSTNSPAPAPPQELTVPWDDIEALLKNNFENDQAAVRQVMERLQKGWSLAK [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000195 [Entry] [Entry number]=387 [Entry name]=C-terminal of Get5 (A. fumigatus) [PDB ID]=2lo0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ubiquitin-like proteins [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=In thermal denaturation measurements of the Get5 dimerization domain two-state melting curve was seen, no folded monomers observed (PMID:22262836). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q4WE50 [UniProt boundaries chain A]=228-272 [UniProt coverage chain A]=16% [Name chain A]=Golgi to ER traffic protein 5 [UniProt sequence chain A]=MSTVDQSTVTTALSSSSSNRHQGNDTYSIPKHSGTTSTITITMNEVSFVKSYLSTLDSRPIKLRSDHVFDPEQVGLRVPYTLPRLHAPHPEMPKKTKQPLAPGSSKSITVHLKSARNPALEFSLPNTALTTTSVQDLKDAVRERVTDAQGNKISLDKIKILYKRKPVTGKTIAEVLADEPVRLSGGKEVEFGVMIIGGAQVAVSAGAGERASAEQKESYEPPKPAVGPSGESVVATEAFWDDLQGFLEQRLKDYDEANKLRVLFKEAWRSSF [Source organism chain A]=Af293) [UniProt ID chain B]=Q4WE50 [UniProt boundaries chain B]=228-272 [UniProt coverage chain B]=16% [Name chain B]=Golgi to ER traffic protein 5 [UniProt sequence chain B]=MSTVDQSTVTTALSSSSSNRHQGNDTYSIPKHSGTTSTITITMNEVSFVKSYLSTLDSRPIKLRSDHVFDPEQVGLRVPYTLPRLHAPHPEMPKKTKQPLAPGSSKSITVHLKSARNPALEFSLPNTALTTTSVQDLKDAVRERVTDAQGNKISLDKIKILYKRKPVTGKTIAEVLADEPVRLSGGKEVEFGVMIIGGAQVAVSAGAGERASAEQKESYEPPKPAVGPSGESVVATEAFWDDLQGFLEQRLKDYDEANKLRVLFKEAWRSSF [Source organism chain B]=Af293) [ExpTech]=NMR [Resolution]=N/A [Source organism]=Af293) [Accession]=MF7000196 [Entry] [Entry number]=388 [Entry name]=N-terminal of FLASH [PDB ID]=6ano [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=CASP8-associated protein 2 [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:29020104). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000197,MF7000198 [UniProt ID chain B]=Q9UKL3 [UniProt boundaries chain B]=70-137 [UniProt coverage chain B]=3% [Name chain B]=CASP8-associated protein 2 [UniProt sequence chain B]=MAADDDNGDGTSLFDVFSASPLKNNDEGSLDIYAGLDSAVSDSASKSCVPSRNCLDLYEEILTEEGTAKEATYNDLQVEYGKCQLQMKELMKKFKEIQTQNFSLINENQSLKKNISALIKTARVEINRKDEEISNLHQRLSEFPHFRNNHKTARTFDTVKTKDLKSRSPHLDDCSKTDHRAKSDVSKDVHHSTSLPNLEKEGKPHSDKRSTSHLPTSVEKHCTNGVWSRSHYQVGEGSSNEDSRRGRKDIRHSQFNRGTERVRKDLSTGCGDGEPRILEASQRLQGHPEKYGKGEPKTESKSSKFKSNSDSDYKGERINSSWEKETPGERSHSRVDSQSDKKLERQSERSQNINRKEVKSQDKEERKVDQKPKSVVKDQDHWRRSERASLPHSKNEITFSHNSSKYHLEERRGWEDCKRDKSVNSHSFQDGRCPSSLSNSRTHKNIDSKEVDAMHQWENTPLKAERHRTEDKRKREQESKEENRHIRNEKRVPTEHLQKTNKETKKTTTDLKKQNEPKTDKGEVLDNGVSEGADNKELAMKAESGPNETKNKDLKLSFMKKLNLTLSPAKKQPVSQDNQHKITDIPKSSGVCDSESSMQVKTVAYVPSISEHILGEAAVSEHTMGETKSTLLEPKVALLAVTEPRIGISETNKEDENSLLVRSVDNTMHCEEPICGTETSFPSPMEIQQTESLFPSTGMKQTINNGRAAAPVVMDVLQTDVSQNFGLELDTKRNDNSDYCGISEGMEMKVALSTTVSETTESILQPSIEEADILPIMLSEDNNPKFEPSVIVTPLVESKSCHLEPCLPKETLDSSLQQTELMDHRMATGETNSVYHDDDNSVLSIDLNHLRPIPEAISPLNSPVRPVAKVLRNESPPQVPVYNNSHKDVFLPNSAHSTSKSQSDLNKENQKPIYKSDKCTEADTCKNSPLDELEEGEIRSDSETSKPQESFEKNSKRRVSADVRKSKTIPRRGKSTVCLDKDSRKTHVRIHQTNNKWNKRPDKSSRSSKTEKKDKVMSTSSLEKIVPIIAVPSSEQEIMHMLRMIRKHVRKNYMKFKAKFSLIQFHRIIESAILSFTSLIKHLNLHKISKSVTTLQKNLCDIIESKLKQVKKNGIVDRLFEQQLPDMKKKLWKFVDDQLDYLFAKLKKILVCDSKSFGRDSDEGKLEKTSKQNAQYSNSQKRSVDNSNRELLKEKLSKSEDPVHYKSLVGCKKSEENYQDQNNSSINTVKHDIKKNFNICFDNIKNSQSEERSLEVHCPSTPKSEKNEGSSIEDAQTSQHATLKPERSFEILTEQQASSLTFNLVSDAQMGEIFKSLLQGSDLLDSSVNCTEKSEWELKTPEKQLLETLKCESIPACTTEELVSGVASPCPKMISDDNWSLLSSEKGPSLSSGLSLPVHPDVLDESCMFEVSTNLPLSKDNVCSVEKSKPCVSSILLEDLAVSLTVPSPLKSDGHLSFLKPDMSSSSTPEEVISAHFSEDALLEEEDASEQDIHLALESDNSSSKSSCSSSWTSRSVAPGFQYHPNLPMHAVIMEKSNDHFIVKIRRATPSTSSGLKQSMMPDELLTSLPRHGKEADEGPEKEYISCQNTVFKSVEELENSNKNVDGSKSTHEEQSSMIQTQVPDIYEFLKDASDKMGHSDEVADECFKLHQVWETKVPESIEELPSMEEISHSVGEHLPNTYVDLTKDPVTETKNLGEFIEVTVLHIDQLGCSGGNLNQSAQILDNSLQADTVGAFIDLTQDASSEAKSEGNHPALAVEDLGCGVIQVDEDNCKEEKAQVANRPLKCIVEETYIDLTTESPSSCEVKKDELKSEPGSNCDNSELPGTLHNSHKKRRNISDLNHPHKKQRKETDLTNKEKTKKPTQDSCENTEAHQKKASKKKAPPVTKDPSSLKATPGIKDSSAALATSTSLSAKNVIKKKGEIIILWTRNDDREILLECQKRGPSFKTFAYLAAKLDKNPNQVSERFQQLMKLFEKSKCR [Source organism chain B]=Homo sapiens [UniProt ID chain A]=Q9UKL3 [UniProt boundaries chain A]=71-137 [UniProt coverage chain A]=3% [Name chain A]=CASP8-associated protein 2 [UniProt sequence chain A]=MAADDDNGDGTSLFDVFSASPLKNNDEGSLDIYAGLDSAVSDSASKSCVPSRNCLDLYEEILTEEGTAKEATYNDLQVEYGKCQLQMKELMKKFKEIQTQNFSLINENQSLKKNISALIKTARVEINRKDEEISNLHQRLSEFPHFRNNHKTARTFDTVKTKDLKSRSPHLDDCSKTDHRAKSDVSKDVHHSTSLPNLEKEGKPHSDKRSTSHLPTSVEKHCTNGVWSRSHYQVGEGSSNEDSRRGRKDIRHSQFNRGTERVRKDLSTGCGDGEPRILEASQRLQGHPEKYGKGEPKTESKSSKFKSNSDSDYKGERINSSWEKETPGERSHSRVDSQSDKKLERQSERSQNINRKEVKSQDKEERKVDQKPKSVVKDQDHWRRSERASLPHSKNEITFSHNSSKYHLEERRGWEDCKRDKSVNSHSFQDGRCPSSLSNSRTHKNIDSKEVDAMHQWENTPLKAERHRTEDKRKREQESKEENRHIRNEKRVPTEHLQKTNKETKKTTTDLKKQNEPKTDKGEVLDNGVSEGADNKELAMKAESGPNETKNKDLKLSFMKKLNLTLSPAKKQPVSQDNQHKITDIPKSSGVCDSESSMQVKTVAYVPSISEHILGEAAVSEHTMGETKSTLLEPKVALLAVTEPRIGISETNKEDENSLLVRSVDNTMHCEEPICGTETSFPSPMEIQQTESLFPSTGMKQTINNGRAAAPVVMDVLQTDVSQNFGLELDTKRNDNSDYCGISEGMEMKVALSTTVSETTESILQPSIEEADILPIMLSEDNNPKFEPSVIVTPLVESKSCHLEPCLPKETLDSSLQQTELMDHRMATGETNSVYHDDDNSVLSIDLNHLRPIPEAISPLNSPVRPVAKVLRNESPPQVPVYNNSHKDVFLPNSAHSTSKSQSDLNKENQKPIYKSDKCTEADTCKNSPLDELEEGEIRSDSETSKPQESFEKNSKRRVSADVRKSKTIPRRGKSTVCLDKDSRKTHVRIHQTNNKWNKRPDKSSRSSKTEKKDKVMSTSSLEKIVPIIAVPSSEQEIMHMLRMIRKHVRKNYMKFKAKFSLIQFHRIIESAILSFTSLIKHLNLHKISKSVTTLQKNLCDIIESKLKQVKKNGIVDRLFEQQLPDMKKKLWKFVDDQLDYLFAKLKKILVCDSKSFGRDSDEGKLEKTSKQNAQYSNSQKRSVDNSNRELLKEKLSKSEDPVHYKSLVGCKKSEENYQDQNNSSINTVKHDIKKNFNICFDNIKNSQSEERSLEVHCPSTPKSEKNEGSSIEDAQTSQHATLKPERSFEILTEQQASSLTFNLVSDAQMGEIFKSLLQGSDLLDSSVNCTEKSEWELKTPEKQLLETLKCESIPACTTEELVSGVASPCPKMISDDNWSLLSSEKGPSLSSGLSLPVHPDVLDESCMFEVSTNLPLSKDNVCSVEKSKPCVSSILLEDLAVSLTVPSPLKSDGHLSFLKPDMSSSSTPEEVISAHFSEDALLEEEDASEQDIHLALESDNSSSKSSCSSSWTSRSVAPGFQYHPNLPMHAVIMEKSNDHFIVKIRRATPSTSSGLKQSMMPDELLTSLPRHGKEADEGPEKEYISCQNTVFKSVEELENSNKNVDGSKSTHEEQSSMIQTQVPDIYEFLKDASDKMGHSDEVADECFKLHQVWETKVPESIEELPSMEEISHSVGEHLPNTYVDLTKDPVTETKNLGEFIEVTVLHIDQLGCSGGNLNQSAQILDNSLQADTVGAFIDLTQDASSEAKSEGNHPALAVEDLGCGVIQVDEDNCKEEKAQVANRPLKCIVEETYIDLTTESPSSCEVKKDELKSEPGSNCDNSELPGTLHNSHKKRRNISDLNHPHKKQRKETDLTNKEKTKKPTQDSCENTEAHQKKASKKKAPPVTKDPSSLKATPGIKDSSAALATSTSLSAKNVIKKKGEIIILWTRNDDREILLECQKRGPSFKTFAYLAAKLDKNPNQVSERFQQLMKLFEKSKCR [Source organism chain A]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.61 [Source organism]=Homo sapiens [Accession]=MF7000197 [Entry] [Entry number]=389 [Entry name]=N-terminal of FLASH (C54S/C83A) [PDB ID]=6ap0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=CASP8-associated protein 2 [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:29020104). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000197,MF7000198 [UniProt ID chain B]=Q9UKL3 [UniProt boundaries chain B]=52-137 [UniProt coverage chain B]=4% [Name chain B]=CASP8-associated protein 2 [UniProt sequence chain B]=MAADDDNGDGTSLFDVFSASPLKNNDEGSLDIYAGLDSAVSDSASKSCVPSRNCLDLYEEILTEEGTAKEATYNDLQVEYGKCQLQMKELMKKFKEIQTQNFSLINENQSLKKNISALIKTARVEINRKDEEISNLHQRLSEFPHFRNNHKTARTFDTVKTKDLKSRSPHLDDCSKTDHRAKSDVSKDVHHSTSLPNLEKEGKPHSDKRSTSHLPTSVEKHCTNGVWSRSHYQVGEGSSNEDSRRGRKDIRHSQFNRGTERVRKDLSTGCGDGEPRILEASQRLQGHPEKYGKGEPKTESKSSKFKSNSDSDYKGERINSSWEKETPGERSHSRVDSQSDKKLERQSERSQNINRKEVKSQDKEERKVDQKPKSVVKDQDHWRRSERASLPHSKNEITFSHNSSKYHLEERRGWEDCKRDKSVNSHSFQDGRCPSSLSNSRTHKNIDSKEVDAMHQWENTPLKAERHRTEDKRKREQESKEENRHIRNEKRVPTEHLQKTNKETKKTTTDLKKQNEPKTDKGEVLDNGVSEGADNKELAMKAESGPNETKNKDLKLSFMKKLNLTLSPAKKQPVSQDNQHKITDIPKSSGVCDSESSMQVKTVAYVPSISEHILGEAAVSEHTMGETKSTLLEPKVALLAVTEPRIGISETNKEDENSLLVRSVDNTMHCEEPICGTETSFPSPMEIQQTESLFPSTGMKQTINNGRAAAPVVMDVLQTDVSQNFGLELDTKRNDNSDYCGISEGMEMKVALSTTVSETTESILQPSIEEADILPIMLSEDNNPKFEPSVIVTPLVESKSCHLEPCLPKETLDSSLQQTELMDHRMATGETNSVYHDDDNSVLSIDLNHLRPIPEAISPLNSPVRPVAKVLRNESPPQVPVYNNSHKDVFLPNSAHSTSKSQSDLNKENQKPIYKSDKCTEADTCKNSPLDELEEGEIRSDSETSKPQESFEKNSKRRVSADVRKSKTIPRRGKSTVCLDKDSRKTHVRIHQTNNKWNKRPDKSSRSSKTEKKDKVMSTSSLEKIVPIIAVPSSEQEIMHMLRMIRKHVRKNYMKFKAKFSLIQFHRIIESAILSFTSLIKHLNLHKISKSVTTLQKNLCDIIESKLKQVKKNGIVDRLFEQQLPDMKKKLWKFVDDQLDYLFAKLKKILVCDSKSFGRDSDEGKLEKTSKQNAQYSNSQKRSVDNSNRELLKEKLSKSEDPVHYKSLVGCKKSEENYQDQNNSSINTVKHDIKKNFNICFDNIKNSQSEERSLEVHCPSTPKSEKNEGSSIEDAQTSQHATLKPERSFEILTEQQASSLTFNLVSDAQMGEIFKSLLQGSDLLDSSVNCTEKSEWELKTPEKQLLETLKCESIPACTTEELVSGVASPCPKMISDDNWSLLSSEKGPSLSSGLSLPVHPDVLDESCMFEVSTNLPLSKDNVCSVEKSKPCVSSILLEDLAVSLTVPSPLKSDGHLSFLKPDMSSSSTPEEVISAHFSEDALLEEEDASEQDIHLALESDNSSSKSSCSSSWTSRSVAPGFQYHPNLPMHAVIMEKSNDHFIVKIRRATPSTSSGLKQSMMPDELLTSLPRHGKEADEGPEKEYISCQNTVFKSVEELENSNKNVDGSKSTHEEQSSMIQTQVPDIYEFLKDASDKMGHSDEVADECFKLHQVWETKVPESIEELPSMEEISHSVGEHLPNTYVDLTKDPVTETKNLGEFIEVTVLHIDQLGCSGGNLNQSAQILDNSLQADTVGAFIDLTQDASSEAKSEGNHPALAVEDLGCGVIQVDEDNCKEEKAQVANRPLKCIVEETYIDLTTESPSSCEVKKDELKSEPGSNCDNSELPGTLHNSHKKRRNISDLNHPHKKQRKETDLTNKEKTKKPTQDSCENTEAHQKKASKKKAPPVTKDPSSLKATPGIKDSSAALATSTSLSAKNVIKKKGEIIILWTRNDDREILLECQKRGPSFKTFAYLAAKLDKNPNQVSERFQQLMKLFEKSKCR [Source organism chain B]=Homo sapiens [UniProt ID chain A]=Q9UKL3 [UniProt boundaries chain A]=56-137 [UniProt coverage chain A]=4% [Name chain A]=CASP8-associated protein 2 [UniProt sequence chain A]=MAADDDNGDGTSLFDVFSASPLKNNDEGSLDIYAGLDSAVSDSASKSCVPSRNCLDLYEEILTEEGTAKEATYNDLQVEYGKCQLQMKELMKKFKEIQTQNFSLINENQSLKKNISALIKTARVEINRKDEEISNLHQRLSEFPHFRNNHKTARTFDTVKTKDLKSRSPHLDDCSKTDHRAKSDVSKDVHHSTSLPNLEKEGKPHSDKRSTSHLPTSVEKHCTNGVWSRSHYQVGEGSSNEDSRRGRKDIRHSQFNRGTERVRKDLSTGCGDGEPRILEASQRLQGHPEKYGKGEPKTESKSSKFKSNSDSDYKGERINSSWEKETPGERSHSRVDSQSDKKLERQSERSQNINRKEVKSQDKEERKVDQKPKSVVKDQDHWRRSERASLPHSKNEITFSHNSSKYHLEERRGWEDCKRDKSVNSHSFQDGRCPSSLSNSRTHKNIDSKEVDAMHQWENTPLKAERHRTEDKRKREQESKEENRHIRNEKRVPTEHLQKTNKETKKTTTDLKKQNEPKTDKGEVLDNGVSEGADNKELAMKAESGPNETKNKDLKLSFMKKLNLTLSPAKKQPVSQDNQHKITDIPKSSGVCDSESSMQVKTVAYVPSISEHILGEAAVSEHTMGETKSTLLEPKVALLAVTEPRIGISETNKEDENSLLVRSVDNTMHCEEPICGTETSFPSPMEIQQTESLFPSTGMKQTINNGRAAAPVVMDVLQTDVSQNFGLELDTKRNDNSDYCGISEGMEMKVALSTTVSETTESILQPSIEEADILPIMLSEDNNPKFEPSVIVTPLVESKSCHLEPCLPKETLDSSLQQTELMDHRMATGETNSVYHDDDNSVLSIDLNHLRPIPEAISPLNSPVRPVAKVLRNESPPQVPVYNNSHKDVFLPNSAHSTSKSQSDLNKENQKPIYKSDKCTEADTCKNSPLDELEEGEIRSDSETSKPQESFEKNSKRRVSADVRKSKTIPRRGKSTVCLDKDSRKTHVRIHQTNNKWNKRPDKSSRSSKTEKKDKVMSTSSLEKIVPIIAVPSSEQEIMHMLRMIRKHVRKNYMKFKAKFSLIQFHRIIESAILSFTSLIKHLNLHKISKSVTTLQKNLCDIIESKLKQVKKNGIVDRLFEQQLPDMKKKLWKFVDDQLDYLFAKLKKILVCDSKSFGRDSDEGKLEKTSKQNAQYSNSQKRSVDNSNRELLKEKLSKSEDPVHYKSLVGCKKSEENYQDQNNSSINTVKHDIKKNFNICFDNIKNSQSEERSLEVHCPSTPKSEKNEGSSIEDAQTSQHATLKPERSFEILTEQQASSLTFNLVSDAQMGEIFKSLLQGSDLLDSSVNCTEKSEWELKTPEKQLLETLKCESIPACTTEELVSGVASPCPKMISDDNWSLLSSEKGPSLSSGLSLPVHPDVLDESCMFEVSTNLPLSKDNVCSVEKSKPCVSSILLEDLAVSLTVPSPLKSDGHLSFLKPDMSSSSTPEEVISAHFSEDALLEEEDASEQDIHLALESDNSSSKSSCSSSWTSRSVAPGFQYHPNLPMHAVIMEKSNDHFIVKIRRATPSTSSGLKQSMMPDELLTSLPRHGKEADEGPEKEYISCQNTVFKSVEELENSNKNVDGSKSTHEEQSSMIQTQVPDIYEFLKDASDKMGHSDEVADECFKLHQVWETKVPESIEELPSMEEISHSVGEHLPNTYVDLTKDPVTETKNLGEFIEVTVLHIDQLGCSGGNLNQSAQILDNSLQADTVGAFIDLTQDASSEAKSEGNHPALAVEDLGCGVIQVDEDNCKEEKAQVANRPLKCIVEETYIDLTTESPSSCEVKKDELKSEPGSNCDNSELPGTLHNSHKKRRNISDLNHPHKKQRKETDLTNKEKTKKPTQDSCENTEAHQKKASKKKAPPVTKDPSSLKATPGIKDSSAALATSTSLSAKNVIKKKGEIIILWTRNDDREILLECQKRGPSFKTFAYLAAKLDKNPNQVSERFQQLMKLFEKSKCR [Source organism chain A]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.58 [Source organism]=Homo sapiens [Accession]=MF7000198 [Entry] [Entry number]=390 [Entry name]=Myo10 [PDB ID]=2lw9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:23012428). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9HD67 [UniProt boundaries chain A]=883-933 [UniProt coverage chain A]=2% [Name chain A]=Unconventional myosin-X [UniProt sequence chain A]=MDNFFTEGTRVWLRENGQHFPSTVNSCAEGIVVFRTDYGQVFTYKQSTITHQKVTAMHPTNEEGVDDMASLTELHGGSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVERAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMDVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYACCFEWVIKKINSRIKGNEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLRESLEQKLEKRREEEVSHAAMVIRAHVLGFLARKQYRKVLYCVVIIQKNYRAFLLRRRFLHLKKAAIVFQKQLRGQIARRVYRQLLAEKREQEEKKKQEEEEKKKREEEERERERERREAELRAQQEEETRKQQELEALQKSQKEAELTRELEKQKENKQVEEILRLEKEIEDLQRMKEQQELSLTEASLQKLQERRDQELRRLEEEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEFSSELAESACEEKPNFNFSQPYPEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNDTVVPTSPSADSTVLLAPSVQDSGSLHNSSSGESTYCMPQNAGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRCSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTTKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHASTDQEIQEMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGSEMEKYALFTYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTVVADVLAKFEKLAATSEVGDLPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHHPAPEENLQVLAALRLQYLQGDYTLHAAIPPLEEVYSLQRLKARISQSTKTFTPCERLEKRRTSFLEGTLRRSFRTGSVVRQKVEEEQMLDMWIKEEVSSARASIIDKWRKFQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSASSQGSSR [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9HD67 [UniProt boundaries chain B]=883-933 [UniProt coverage chain B]=2% [Name chain B]=Unconventional myosin-X [UniProt sequence chain B]=MDNFFTEGTRVWLRENGQHFPSTVNSCAEGIVVFRTDYGQVFTYKQSTITHQKVTAMHPTNEEGVDDMASLTELHGGSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVERAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMDVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYACCFEWVIKKINSRIKGNEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLRESLEQKLEKRREEEVSHAAMVIRAHVLGFLARKQYRKVLYCVVIIQKNYRAFLLRRRFLHLKKAAIVFQKQLRGQIARRVYRQLLAEKREQEEKKKQEEEEKKKREEEERERERERREAELRAQQEEETRKQQELEALQKSQKEAELTRELEKQKENKQVEEILRLEKEIEDLQRMKEQQELSLTEASLQKLQERRDQELRRLEEEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEFSSELAESACEEKPNFNFSQPYPEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNDTVVPTSPSADSTVLLAPSVQDSGSLHNSSSGESTYCMPQNAGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRCSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTTKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHASTDQEIQEMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGSEMEKYALFTYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTVVADVLAKFEKLAATSEVGDLPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHHPAPEENLQVLAALRLQYLQGDYTLHAAIPPLEEVYSLQRLKARISQSTKTFTPCERLEKRRTSFLEGTLRRSFRTGSVVRQKVEEEQMLDMWIKEEVSSARASIIDKWRKFQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSASSQGSSR [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000199 [Entry] [Entry number]=391 [Entry name]=Coiled coil domain of Huntingtin-interacting protein 1 [PDB ID]=3i00 [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:20179344). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=None [UniProt ID chain A]=O00291 [UniProt boundaries chain A]=370-445 [UniProt coverage chain A]=7% [Name chain A]=Huntingtin-interacting protein 1 [UniProt sequence chain A]=MDRMASSMKQVPNPLPKVLSRRGVGAGLEAAERESFERTQTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFFQLTVEMFDYLECELNLFQTVFNSLDMSRSVSVTAAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLPADTLQGHRDRFMEQFTKLKDLFYRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEASSPDSEPVLEKDDLMDMDASQQNLFDNKFDDIFGSSFSSDPFNFNSQNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEEPPLISCAGSADHLLSTVTSISSCIEQLEKSWSQYLACPEDISGLLHSITLLAHLTSDAIAHGATTCLRAPPEPADSLTEACKQYGRETLAYLASLEEEGSLENADSTAMRNCLSKIKAIGEELLPRGLDIKQEELGDLVDKEMAATSAAIETATARIEEMLSKSRAGDTGVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQIEETDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELAGVAEGWEEGTEASPPTLQEVVTEKE [Source organism chain A]=Homo sapiens [UniProt ID chain B-2]=O00291 [UniProt boundaries chain B-2]=367-446 [UniProt coverage chain B-2]=7% [Name chain B-2]=Huntingtin-interacting protein 1 [UniProt sequence chain B-2]=MDRMASSMKQVPNPLPKVLSRRGVGAGLEAAERESFERTQTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFFQLTVEMFDYLECELNLFQTVFNSLDMSRSVSVTAAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLPADTLQGHRDRFMEQFTKLKDLFYRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEASSPDSEPVLEKDDLMDMDASQQNLFDNKFDDIFGSSFSSDPFNFNSQNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEEPPLISCAGSADHLLSTVTSISSCIEQLEKSWSQYLACPEDISGLLHSITLLAHLTSDAIAHGATTCLRAPPEPADSLTEACKQYGRETLAYLASLEEEGSLENADSTAMRNCLSKIKAIGEELLPRGLDIKQEELGDLVDKEMAATSAAIETATARIEEMLSKSRAGDTGVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQIEETDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELAGVAEGWEEGTEASPPTLQEVVTEKE [Source organism chain B-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Homo sapiens [Accession]=MF7000200 [Entry] [Entry number]=392 [Entry name]=UPF0066 protein AF0241 [PDB ID]=2nv4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms. AF_0241 is a dimer, both in solution and in the crystal (PMID:17588214). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O29998 [UniProt boundaries chain A]=1-133 [UniProt coverage chain A]=95% [Name chain A]=S-adenosyl-L-methionine-binding protein AF_0241 [UniProt sequence chain A]=MILKPIGVVKSPFKTQNDAPRQGRFSDAVSEIAIFDEYADGLHKIENLRHIIVLYWMDKASRDKLRVVPPGETEERGVFTTRSPSRPNPIGLCVVEILEVERNRLKVRWLDALDGSPVIDIKKYSPEIDCVNQLEGQQP [Source organism chain A]=100126 / VC-16) [UniProt ID chain B]=O29998 [UniProt boundaries chain B]=1-133 [UniProt coverage chain B]=95% [Name chain B]=S-adenosyl-L-methionine-binding protein AF_0241 [UniProt sequence chain B]=MILKPIGVVKSPFKTQNDAPRQGRFSDAVSEIAIFDEYADGLHKIENLRHIIVLYWMDKASRDKLRVVPPGETEERGVFTTRSPSRPNPIGLCVVEILEVERNRLKVRWLDALDGSPVIDIKKYSPEIDCVNQLEGQQP [Source organism chain B]=100126 / VC-16) [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=100126 / VC-16) [Accession]=MF7000201 [Entry] [Entry number]=394 [Entry name]=DLLRKN-containing coiled coil domain of Huntingtin-interacting protein 1 [PDB ID]=2no2 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:17257618). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=O00291 [UniProt boundaries chain A]=482-581 [UniProt coverage chain A]=9% [Name chain A]=Huntingtin-interacting protein 1 [UniProt sequence chain A]=MDRMASSMKQVPNPLPKVLSRRGVGAGLEAAERESFERTQTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFFQLTVEMFDYLECELNLFQTVFNSLDMSRSVSVTAAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLPADTLQGHRDRFMEQFTKLKDLFYRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEASSPDSEPVLEKDDLMDMDASQQNLFDNKFDDIFGSSFSSDPFNFNSQNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEEPPLISCAGSADHLLSTVTSISSCIEQLEKSWSQYLACPEDISGLLHSITLLAHLTSDAIAHGATTCLRAPPEPADSLTEACKQYGRETLAYLASLEEEGSLENADSTAMRNCLSKIKAIGEELLPRGLDIKQEELGDLVDKEMAATSAAIETATARIEEMLSKSRAGDTGVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQIEETDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELAGVAEGWEEGTEASPPTLQEVVTEKE [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=O00291 [UniProt boundaries chain A-2]=482-581 [UniProt coverage chain A-2]=9% [Name chain A-2]=Huntingtin-interacting protein 1 [UniProt sequence chain A-2]=MDRMASSMKQVPNPLPKVLSRRGVGAGLEAAERESFERTQTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFFQLTVEMFDYLECELNLFQTVFNSLDMSRSVSVTAAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLPADTLQGHRDRFMEQFTKLKDLFYRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEASSPDSEPVLEKDDLMDMDASQQNLFDNKFDDIFGSSFSSDPFNFNSQNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEEPPLISCAGSADHLLSTVTSISSCIEQLEKSWSQYLACPEDISGLLHSITLLAHLTSDAIAHGATTCLRAPPEPADSLTEACKQYGRETLAYLASLEEEGSLENADSTAMRNCLSKIKAIGEELLPRGLDIKQEELGDLVDKEMAATSAAIETATARIEEMLSKSRAGDTGVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQIEETDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELAGVAEGWEEGTEASPPTLQEVVTEKE [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Homo sapiens [Accession]=MF7000204 [Entry] [Entry number]=395 [Entry name]=Coiled coil domain of MDV1 [PDB ID]=2xu6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:21149566). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P47025 [UniProt boundaries chain A]=231-291 [UniProt coverage chain A]=8% [Name chain A]=Mitochondrial division protein 1 [UniProt sequence chain A]=MSVNDQITHIGKTLSTTASAFLNYQKSNSNTQDVLTNNGPYKNLLSNTVNNASSTSYFYKRTEHGRFVKNASNTFEDIYSKTRRGDVFRNKFTDNKTCFRMLTYISDDLLNEIPTKEGLKSDADGKLLTEGGENENLRKNASKKETSLFQGFKSYLPIAELAIENTERLNYDTNGTSGTVGAKDVMSKTNERDEIHTELPNFQDSFLIPPGVETKKISSSYSPSALKSFSQTLVNSLEFLNIQKNSTLSEIRDIEVEVENLRQKKEKLLGKIANIEQNQLLLEDNLKQIDDRLDFLEEYGLEVIEANSDENAEDDGMSERKALKNDAIRNEGVTTESISSEASNLPPRRRQQLRDDNSLNRLGAFYSKSKKRHRKSFPTFQQLYEPGTKIGSIMSTHDDFLTCLDFDAPFGTLCTAGYLDHTVKIWDLSKQNKIGELAGHLATINCMQINRDYGTLVTGGRDAALKLWNLNLAQQLYQETQNLTSPTNHIDSPCVHTFEAHTDEVTALSLDPSFLVSGSQDRTIRQWDLRSGKCLQTIDLSFANVLTTSTNVDLSKSTLLTQRNERPSIGALQSFDAALATGTKDGVVRLWDLRSGKVIRTLKGHTDAITSLKFDSACLVTGSYDRTVRIWDLRTGLLNKFHAYSAPVLSLDLFQENAAVVVADEPSVQIYDSEKDESWSCVEQGNETSVSTVKYKENYMVEGRENGDVNIWAV [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P47025 [UniProt boundaries chain B]=231-292 [UniProt coverage chain B]=8% [Name chain B]=Mitochondrial division protein 1 [UniProt sequence chain B]=MSVNDQITHIGKTLSTTASAFLNYQKSNSNTQDVLTNNGPYKNLLSNTVNNASSTSYFYKRTEHGRFVKNASNTFEDIYSKTRRGDVFRNKFTDNKTCFRMLTYISDDLLNEIPTKEGLKSDADGKLLTEGGENENLRKNASKKETSLFQGFKSYLPIAELAIENTERLNYDTNGTSGTVGAKDVMSKTNERDEIHTELPNFQDSFLIPPGVETKKISSSYSPSALKSFSQTLVNSLEFLNIQKNSTLSEIRDIEVEVENLRQKKEKLLGKIANIEQNQLLLEDNLKQIDDRLDFLEEYGLEVIEANSDENAEDDGMSERKALKNDAIRNEGVTTESISSEASNLPPRRRQQLRDDNSLNRLGAFYSKSKKRHRKSFPTFQQLYEPGTKIGSIMSTHDDFLTCLDFDAPFGTLCTAGYLDHTVKIWDLSKQNKIGELAGHLATINCMQINRDYGTLVTGGRDAALKLWNLNLAQQLYQETQNLTSPTNHIDSPCVHTFEAHTDEVTALSLDPSFLVSGSQDRTIRQWDLRSGKCLQTIDLSFANVLTTSTNVDLSKSTLLTQRNERPSIGALQSFDAALATGTKDGVVRLWDLRSGKVIRTLKGHTDAITSLKFDSACLVTGSYDRTVRIWDLRTGLLNKFHAYSAPVLSLDLFQENAAVVVADEPSVQIYDSEKDESWSCVEQGNETSVSTVKYKENYMVEGRENGDVNIWAV [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000205 [Entry] [Entry number]=396 [Entry name]=NblA (T. vulcanus) [PDB ID]=2q8v [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. Most likely the dimer is the basic structural unit since 2 M urea does not monomerize the NblA dimers (PMID:18718907). No monomers could be detected for any of the NblA homologs. The NblA monomer has a helix-loop-helix motif which dimerizes into an open, four-helical bundle, identical to the previously determined NblA structure from Anabaena (PMID:18718907). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=A7LBW5 [UniProt boundaries chain A]=8-60 [UniProt coverage chain A]=84% [Name chain A]=NblA [UniProt sequence chain A]=MEQRFPELNVDLSFEQEFQMRVMEEQVSAMSLQEARELLLQASRLLMMKDNVIRSLVKRAARS [Source organism chain A]=Thermostichus vulcanus str Copeland [UniProt ID chain B]=A7LBW5 [UniProt boundaries chain B]=12-62 [UniProt coverage chain B]=80% [Name chain B]=NblA [UniProt sequence chain B]=MEQRFPELNVDLSFEQEFQMRVMEEQVSAMSLQEARELLLQASRLLMMKDNVIRSLVKRAARS [Source organism chain B]=Thermostichus vulcanus str Copeland [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Thermostichus vulcanus str Copeland [Accession]=MF7000206 [Entry] [Entry number]=399 [Entry name]=Chorismate mutase (Corynebacterium glutamicum) [PDB ID]=5hub [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Chorismate mutase type II [Evidence level]=Indirect evidence [Evidence text]=The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000162,MF7000212,MF7000163,MF7000211,MF7000164,MF7000165,MF7000209,MF7000210 [UniProt ID chain A]=Q8NS29 [UniProt boundaries chain A]=21-99 [UniProt coverage chain A]=76% [Name chain A]=Chorismate mutase [UniProt sequence chain A]=MCMTNAGDNFEIRMPSGTDDPLSDAEIQKYREEINRLDREILDAVKRRTKISQTIGKTRMSSGGTRLVHTREVAIINQFREEIGEEGPALAGILLRMGRGKLG [Source organism chain A]=534) [UniProt ID chain A-2]=Q8NS29 [UniProt boundaries chain A-2]=21-99 [UniProt coverage chain A-2]=76% [Name chain A-2]=Chorismate mutase [UniProt sequence chain A-2]=MCMTNAGDNFEIRMPSGTDDPLSDAEIQKYREEINRLDREILDAVKRRTKISQTIGKTRMSSGGTRLVHTREVAIINQFREEIGEEGPALAGILLRMGRGKLG [Source organism chain A-2]=534) [ExpTech]=X-ray [Resolution]=1.06 [Source organism]=534) [Accession]=MF7000209 [Entry] [Entry number]=400 [Entry name]=Chorismate mutase (Mycobacterium tuberculosis) [PDB ID]=5mpv [Chains]=D,D-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Chorismate mutase type II [Evidence level]=Indirect evidence [Evidence text]=The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain D]=N/A [Evidence chain D-2]=N/A [Similar structures]=MF7000162,MF7000212,MF7000163,MF7000211,MF7000164,MF7000165,MF7000209,MF7000210 [UniProt ID chain D]=P9WIC1 [UniProt boundaries chain D]=26-93 [UniProt coverage chain D]=64% [Name chain D]=Intracellular chorismate mutase [UniProt sequence chain D]=MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH [Source organism chain D]=Mycobacterium tuberculosis [UniProt ID chain D-2]=P9WIC1 [UniProt boundaries chain D-2]=26-93 [UniProt coverage chain D-2]=64% [Name chain D-2]=Intracellular chorismate mutase [UniProt sequence chain D-2]=MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH [Source organism chain D-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.49 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000210 [Entry] [Entry number]=401 [Entry name]=Chorismate mutase (Mycobacterium tuberculosis) [PDB ID]=2vkl [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Chorismate mutase type II [Evidence level]=Indirect evidence [Evidence text]=The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000162,MF7000212,MF7000163,MF7000211,MF7000164,MF7000165,MF7000209,MF7000210 [UniProt ID chain A]=P9WIC1 [UniProt boundaries chain A]=28-104 [UniProt coverage chain A]=73% [Name chain A]=Intracellular chorismate mutase [UniProt sequence chain A]=MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=P9WIC1 [UniProt boundaries chain A-2]=28-104 [UniProt coverage chain A-2]=73% [Name chain A-2]=Intracellular chorismate mutase [UniProt sequence chain A-2]=MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000211 [Entry] [Entry number]=402 [Entry name]=Chorismate mutase (Mycobacterium tuberculosis) [PDB ID]=2qbv [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Chorismate mutase type II [Evidence level]=Indirect evidence [Evidence text]=The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000162,MF7000212,MF7000163,MF7000211,MF7000164,MF7000165,MF7000209,MF7000210 [UniProt ID chain A]=P9WIC1 [UniProt boundaries chain A]=28-100 [UniProt coverage chain A]=69% [Name chain A]=Intracellular chorismate mutase [UniProt sequence chain A]=MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=P9WIC1 [UniProt boundaries chain A-2]=28-100 [UniProt coverage chain A-2]=69% [Name chain A-2]=Intracellular chorismate mutase [UniProt sequence chain A-2]=MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000212 [Entry] [Entry number]=403 [Entry name]=MitoNEET [PDB ID]=2qd0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=43-106 [UniProt coverage chain A]=59% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9NZ45 [UniProt boundaries chain B]=38-106 [UniProt coverage chain B]=63% [Name chain B]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain B]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.81 [Source organism]=Homo sapiens [Accession]=MF7000213 [Entry] [Entry number]=404 [Entry name]=MitoNEET [PDB ID]=2r13 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=33-105 [UniProt coverage chain A]=67% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q9NZ45 [UniProt boundaries chain A-2]=33-105 [UniProt coverage chain A-2]=67% [Name chain A-2]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A-2]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF7000214 [Entry] [Entry number]=405 [Entry name]=Coiled coil domain of Stu2 [PDB ID]=6bl7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:29187574). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P46675 [UniProt boundaries chain A]=657-755 [UniProt coverage chain A]=11% [Name chain A]=Protein STU2 [UniProt sequence chain A]=MSGEEEVDYTTLPLEERLTYKLWKARLEAYKELNQLFRNSVGDISRDDNIQIYWRDPTLFAQYITDSNVVAQEQAIVALNSLIDAFASSSLKNAHNITLISTWTPLLVEKGLTSSRATTKTQSMSCILSLCGLDTSITQSVELVIPFFEKKLPKLIAAAANCVYELMAAFGLTNVNVQTFLPELLKHVPQLAGHGDRNVRSQTMNLIVEIYKVTGNNSDLLEEILFKKLKPIQVKDLHKLFAKVGDEPSSSKMLFEWEKRELEKKRSQEEEARKRKSILSNDEGEYQIDKDGDTLMGMETDMPPSKQQSGVQIDTFSMLPEETILDKLPKDFQERITSSKWKDRVEALEEFWDSVLSQTKKLKSTSQNYSNLLGIYGHIIQKDANIQAVALAAQSVELICDKLKTPGFSKDYVSLVFTPLLDRTKEKKPSVIEAIRKALLTICKYYDPLASSGRNEDMLKDILEHMKHKTPQIRMECTQLFNASMKEEKDGYSTLQRYLKDEVVPIVIQIVNDTQPAIRTIGFESFAILIKIFGMNTFVKTLEHLDNLKRKKIEETVKTLPNFSIASGSTHSTIETNKQTGPMENKFLLKKSSVLPSKRVASSPLRNDNKSKVNPIGSVASASKPSMVAANNKSRVLLTSKSLATPKNVVANSTDKNEKLIEEYKYRLQKLQNDEMIWTKERQSLLEKMNNTENYKIEMIKENEMLREQLKEAQSKLNEKNIQLRSKEIDVNKLSDRVLSLENELRNMEIELDRNKKRNDTNLQSMGTISSYSIPSSTVSSNYGVKSLSSALPFKEEEDVRRKEDVNYERRSSESIGDLPHRVNSLNIRPYRKNGTGVSSVSDDLDIDFNDSFASEESYKRAAAVTSTLKARIEKMKAKSRREGTTRT [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P46675 [UniProt boundaries chain B]=658-755 [UniProt coverage chain B]=11% [Name chain B]=Protein STU2 [UniProt sequence chain B]=MSGEEEVDYTTLPLEERLTYKLWKARLEAYKELNQLFRNSVGDISRDDNIQIYWRDPTLFAQYITDSNVVAQEQAIVALNSLIDAFASSSLKNAHNITLISTWTPLLVEKGLTSSRATTKTQSMSCILSLCGLDTSITQSVELVIPFFEKKLPKLIAAAANCVYELMAAFGLTNVNVQTFLPELLKHVPQLAGHGDRNVRSQTMNLIVEIYKVTGNNSDLLEEILFKKLKPIQVKDLHKLFAKVGDEPSSSKMLFEWEKRELEKKRSQEEEARKRKSILSNDEGEYQIDKDGDTLMGMETDMPPSKQQSGVQIDTFSMLPEETILDKLPKDFQERITSSKWKDRVEALEEFWDSVLSQTKKLKSTSQNYSNLLGIYGHIIQKDANIQAVALAAQSVELICDKLKTPGFSKDYVSLVFTPLLDRTKEKKPSVIEAIRKALLTICKYYDPLASSGRNEDMLKDILEHMKHKTPQIRMECTQLFNASMKEEKDGYSTLQRYLKDEVVPIVIQIVNDTQPAIRTIGFESFAILIKIFGMNTFVKTLEHLDNLKRKKIEETVKTLPNFSIASGSTHSTIETNKQTGPMENKFLLKKSSVLPSKRVASSPLRNDNKSKVNPIGSVASASKPSMVAANNKSRVLLTSKSLATPKNVVANSTDKNEKLIEEYKYRLQKLQNDEMIWTKERQSLLEKMNNTENYKIEMIKENEMLREQLKEAQSKLNEKNIQLRSKEIDVNKLSDRVLSLENELRNMEIELDRNKKRNDTNLQSMGTISSYSIPSSTVSSNYGVKSLSSALPFKEEEDVRRKEDVNYERRSSESIGDLPHRVNSLNIRPYRKNGTGVSSVSDDLDIDFNDSFASEESYKRAAAVTSTLKARIEKMKAKSRREGTTRT [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000215 [Entry] [Entry number]=406 [Entry name]=XLF [PDB ID]=2r9a [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=C-terminal coiled coil dimerization subdomain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Dimerization is mediated by a coiled coil subdomain. Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815). The combined effects of burying extensive hydrophobic surface and structural support gained by wrapping α5 and α6 onto α4 suggest that the XLF dimer is highly stable. Only the C-terminal three helices (residues 128-224) participate in dimer formation (MSF), the globular N-terminal domain does not. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9H9Q4 [UniProt boundaries chain A]=1-224 [UniProt coverage chain A]=74% [Name chain A]=Non-homologous end-joining factor 1 [UniProt sequence chain A]=MEELEQGLLMQPWAWLQLAENSLLAKVFITKQGYALLVSDLQQVWHEQVDTSVVSQRAKELNKRLTAPPAAFLCHLDNLLRPLLKDAAHPSEATFSCDCVADALILRVRSELSGLPFYWNFHCMLASPSLVSQHLIRPLMGMSLALQCQVRELATLLHMKDLEIQDYQESGATLIRDRLKTEPFEENSFLEQFMIEKLPEACSIGDGKPFVMNLQDLYMAVTTQEVQVGQKHQGAGDPHTSNSASLQGIDSQCVNQPEQLVSSAPTLSAPEKESTGTSGPLQRPQLSKVKRKKPRGLFS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9H9Q4 [UniProt boundaries chain B]=1-224 [UniProt coverage chain B]=74% [Name chain B]=Non-homologous end-joining factor 1 [UniProt sequence chain B]=MEELEQGLLMQPWAWLQLAENSLLAKVFITKQGYALLVSDLQQVWHEQVDTSVVSQRAKELNKRLTAPPAAFLCHLDNLLRPLLKDAAHPSEATFSCDCVADALILRVRSELSGLPFYWNFHCMLASPSLVSQHLIRPLMGMSLALQCQVRELATLLHMKDLEIQDYQESGATLIRDRLKTEPFEENSFLEQFMIEKLPEACSIGDGKPFVMNLQDLYMAVTTQEVQVGQKHQGAGDPHTSNSASLQGIDSQCVNQPEQLVSSAPTLSAPEKESTGTSGPLQRPQLSKVKRKKPRGLFS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Homo sapiens [Accession]=MF7000216 [Entry] [Entry number]=407 [Entry name]=Coiled coil domain of spectrin [PDB ID]=2spc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:8266097). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P13395 [UniProt boundaries chain A]=1391-1497 [UniProt coverage chain A]=4% [Name chain A]=Spectrin alpha chain [UniProt sequence chain A]=MENFTPKEVKILETVEDIQERREQVLSRYNDFKIETRQKREKLEDSRRFQYFKRDADELESWIHEKLQAASEESYRDPTNLQAKIQKHQAFEAEVSAHSNAIVSLDNTGQEMINQQHFASESIQVRLDELHKLWELLLSRLAEKGLKLQQALVLVQFLRQCEEVMFWIKDKETFVTADEFGQDLEHVEVLQRKFDEFQKDMASQEYRVTEVNQLADKLVQDGHPERDTITKRKEELNEAWQRLKQLAIVRQEKLFGAHEIQRFNRDADETVAWIAEKDVVLSSDDYGRDLASVQALQRKHEGVERDLAALEDKVSTLGAEAQRLCSIHADHSDQIRDKQAEIANYWQSLTTKARERKQKLDESYYLHRFLADFRDLVSWINGMKAIISADELAKDVAGAEALLERHQEHKGEIDAREDSFKLTTESGQKLLEREHYAAAEIQEKLAALENDKSSLLSLWEDRRILYEQCMDLQLFYRDTEQADTWMAKQEAFLANEDLGDSLDSVEALIKKHEDFEKSLAAQEEKIKALDIFATKLIDGQHYAADDVAQRRQMLLARRAALQEKSSKRRQLLEDSNRYQQFERDCDETKGWISEKLKFATDDSYLDPTNLNGKMQKHQNFEHELNANKSRIEDITNVGTELIEKQHYAADQINTRMQEIVVLWETLVQASDKKGTKLNEACQQQQFNRTIEDIELWLSEIEGQLLSEDHGKDLTSVQNLQKKHALLEADVMAHQDRIESIKVAANKFIESGHFDADNIRNKEGNLSARYAALAAPMGERKQHLLDSLQVQQLFRDLEDEAAWIREKEPIAASTNRGRDLIGVQNLIKKHQAVLAEINNHEARLLNVISSGENMLKDQPFASDDIRQRLEALQEQWNTLKEKSSQRKQDLDDSLQAHQYFADANEAESWMREKEPIATGSDYGKDEDSSEALLKKHEALVSDLEAFGNTIQALQEQAKNCRQQETPVVDITGKECVVALYDYTEKSPREVSMKKGDVLTLLNSNNKDWWKVEVNDRQGFVPAAYIKKIDAGLSASQQNLVDNHSIAKRQNQINSQYDNLLALARERQNKLNETVKAYVLVREAADLAQWIRDKENHAQIADVVGEDLEEVEVLQKKFDDFNDDLKANEVRLANMNEIAVQLTSLGQTEAALKIQTQMQDLNEKWNNLQTLTAEKASQLGSAHEVQRFHRDIDETKDWIAEKANALNNDDLGKDLRSVQTLQRKHEGVERDLAALRDKIRQLDETANRLMQSHPDTAEQTYAKQKEINEMWDQIITKSTARKEKLLDSYDLQRFLSDYRDLLAWINSMMSLVTSDELANDVTGAEALIERHQEHRTEIDARAGTFGAFEQFGNELLQANHYASPEIKEKIEDLAKAREDLEKAWTERRLQLEQNLDLQLYMRDCELAESWMSAREAFLNADDDANAGGNVEALIKKHEDFDKAINGHEQKIAALQTVADQLIAQNHYASNLVDEKRKQVLERWRHLKEGLIEKRSRLGDEQTLQQFSRDADEIENWIAEKLQLATEESYKDPANIQSKHQKHQAFEAELAANADRIQSVLAMGGNLIDKKQCSGSEDAVQKRLTQIADQWEYLTHKTTEKSLKLKEANKQRTYIAAVKDLDFWLGEVESLLTTEDSGKDLASVQNLMKKHQLVEADIVAHEDRIKDMNNQADSLVESGQFDTAGIQEKRQSINERYERICNLAAHRQARLNEALTLHQFFRDIADEESWIKEKKLLVGSDDYGRDLTGVQNLKKKHKRLEAELGSHEPAIQAVQEAGEKLMDVSNLGVPEIEQRLKALNQAWAELKNLAATRGQKLDESLTYQQFLAQVEEEEAWITEKQQLLSVEDYGDSMAAVQGLLKKHDAFETDFTAHKDRCSLICDQGSELVEAKNHHGESIAQRCQQLRLKLDNLSALAARRKGALLDNSAYLQFMWKADVVESWIDDKENYVRSDEFGRDLSTVQTLLTKQETFDAGLNAFEQEGIHNITALKDQLINASHAQSPAILKRHGDVIARWQKLRDASNTRKDRLLAMQEQFRQIEELYLTFAKKASAFNSWFENAEEDLTDPVRCNSIEEIRALRDAHAQFQASLSSAEADFKALAALDQKIKSFNVGPNPYTWFTMEALEETWRNLQKIIEERDGELAKEAKRQEENDKLRKEFAKHANLFHQWLTETRTSMMEGSGSLEQQLEALRVKATEVRARRVDLKKIEELGALLEEHLILDNRYTEHSTVGLAQQWDQLDQLSMRMQHNLEQQIQARNHSGVSEDSLKEFSMMFKHFDKDKSGKLNHQEFKSCLRALGYDLPMVEEGQPDPEFEAILDVVDPNRDGYVSLQEYIAFMISKETENVQSYEEIENAFRAITAADRPYVTKEELYCNLTKDMADYCVQRMKPFSEPRSGQPIKDALDYIDFTRTLFQN [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=P13395 [UniProt boundaries chain B]=1391-1497 [UniProt coverage chain B]=4% [Name chain B]=Spectrin alpha chain [UniProt sequence chain B]=MENFTPKEVKILETVEDIQERREQVLSRYNDFKIETRQKREKLEDSRRFQYFKRDADELESWIHEKLQAASEESYRDPTNLQAKIQKHQAFEAEVSAHSNAIVSLDNTGQEMINQQHFASESIQVRLDELHKLWELLLSRLAEKGLKLQQALVLVQFLRQCEEVMFWIKDKETFVTADEFGQDLEHVEVLQRKFDEFQKDMASQEYRVTEVNQLADKLVQDGHPERDTITKRKEELNEAWQRLKQLAIVRQEKLFGAHEIQRFNRDADETVAWIAEKDVVLSSDDYGRDLASVQALQRKHEGVERDLAALEDKVSTLGAEAQRLCSIHADHSDQIRDKQAEIANYWQSLTTKARERKQKLDESYYLHRFLADFRDLVSWINGMKAIISADELAKDVAGAEALLERHQEHKGEIDAREDSFKLTTESGQKLLEREHYAAAEIQEKLAALENDKSSLLSLWEDRRILYEQCMDLQLFYRDTEQADTWMAKQEAFLANEDLGDSLDSVEALIKKHEDFEKSLAAQEEKIKALDIFATKLIDGQHYAADDVAQRRQMLLARRAALQEKSSKRRQLLEDSNRYQQFERDCDETKGWISEKLKFATDDSYLDPTNLNGKMQKHQNFEHELNANKSRIEDITNVGTELIEKQHYAADQINTRMQEIVVLWETLVQASDKKGTKLNEACQQQQFNRTIEDIELWLSEIEGQLLSEDHGKDLTSVQNLQKKHALLEADVMAHQDRIESIKVAANKFIESGHFDADNIRNKEGNLSARYAALAAPMGERKQHLLDSLQVQQLFRDLEDEAAWIREKEPIAASTNRGRDLIGVQNLIKKHQAVLAEINNHEARLLNVISSGENMLKDQPFASDDIRQRLEALQEQWNTLKEKSSQRKQDLDDSLQAHQYFADANEAESWMREKEPIATGSDYGKDEDSSEALLKKHEALVSDLEAFGNTIQALQEQAKNCRQQETPVVDITGKECVVALYDYTEKSPREVSMKKGDVLTLLNSNNKDWWKVEVNDRQGFVPAAYIKKIDAGLSASQQNLVDNHSIAKRQNQINSQYDNLLALARERQNKLNETVKAYVLVREAADLAQWIRDKENHAQIADVVGEDLEEVEVLQKKFDDFNDDLKANEVRLANMNEIAVQLTSLGQTEAALKIQTQMQDLNEKWNNLQTLTAEKASQLGSAHEVQRFHRDIDETKDWIAEKANALNNDDLGKDLRSVQTLQRKHEGVERDLAALRDKIRQLDETANRLMQSHPDTAEQTYAKQKEINEMWDQIITKSTARKEKLLDSYDLQRFLSDYRDLLAWINSMMSLVTSDELANDVTGAEALIERHQEHRTEIDARAGTFGAFEQFGNELLQANHYASPEIKEKIEDLAKAREDLEKAWTERRLQLEQNLDLQLYMRDCELAESWMSAREAFLNADDDANAGGNVEALIKKHEDFDKAINGHEQKIAALQTVADQLIAQNHYASNLVDEKRKQVLERWRHLKEGLIEKRSRLGDEQTLQQFSRDADEIENWIAEKLQLATEESYKDPANIQSKHQKHQAFEAELAANADRIQSVLAMGGNLIDKKQCSGSEDAVQKRLTQIADQWEYLTHKTTEKSLKLKEANKQRTYIAAVKDLDFWLGEVESLLTTEDSGKDLASVQNLMKKHQLVEADIVAHEDRIKDMNNQADSLVESGQFDTAGIQEKRQSINERYERICNLAAHRQARLNEALTLHQFFRDIADEESWIKEKKLLVGSDDYGRDLTGVQNLKKKHKRLEAELGSHEPAIQAVQEAGEKLMDVSNLGVPEIEQRLKALNQAWAELKNLAATRGQKLDESLTYQQFLAQVEEEEAWITEKQQLLSVEDYGDSMAAVQGLLKKHDAFETDFTAHKDRCSLICDQGSELVEAKNHHGESIAQRCQQLRLKLDNLSALAARRKGALLDNSAYLQFMWKADVVESWIDDKENYVRSDEFGRDLSTVQTLLTKQETFDAGLNAFEQEGIHNITALKDQLINASHAQSPAILKRHGDVIARWQKLRDASNTRKDRLLAMQEQFRQIEELYLTFAKKASAFNSWFENAEEDLTDPVRCNSIEEIRALRDAHAQFQASLSSAEADFKALAALDQKIKSFNVGPNPYTWFTMEALEETWRNLQKIIEERDGELAKEAKRQEENDKLRKEFAKHANLFHQWLTETRTSMMEGSGSLEQQLEALRVKATEVRARRVDLKKIEELGALLEEHLILDNRYTEHSTVGLAQQWDQLDQLSMRMQHNLEQQIQARNHSGVSEDSLKEFSMMFKHFDKDKSGKLNHQEFKSCLRALGYDLPMVEEGQPDPEFEAILDVVDPNRDGYVSLQEYIAFMISKETENVQSYEEIENAFRAITAADRPYVTKEELYCNLTKDMADYCVQRMKPFSEPRSGQPIKDALDYIDFTRTLFQN [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Drosophila melanogaster [Accession]=MF7000217 [Entry] [Entry number]=408 [Entry name]=GamS (bacteriophage lambda) [PDB ID]=2uuz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Host-nuclease inhibitor protein Gam [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. However, most likely dimer is the basic structural unit, since 2 M urea does not monomerize the NblA dimers. There are extensie helix packing interactions between the monomers (PMID:18718907). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000218,MF7000219 [UniProt ID chain A]=P03702 [UniProt boundaries chain A]=49-138 [UniProt coverage chain A]=65% [Name chain A]=Host-nuclease inhibitor protein gam [UniProt sequence chain A]=MDINTETEIKQKHSLTPFPVFLISPAFRGRYFHSYFRSSAMNAYYIQDRLEAQSWARHYQQLAREEKEAELADDMEKGLPQHLFESLCIDHLQRHGASKKSITRAFDDDVEFQERMAEHIRYMVETIAHHQVDIDSEV [Source organism chain A]=Escherichia phage lambda [UniProt ID chain B]=P03702 [UniProt boundaries chain B]=53-138 [UniProt coverage chain B]=62% [Name chain B]=Host-nuclease inhibitor protein gam [UniProt sequence chain B]=MDINTETEIKQKHSLTPFPVFLISPAFRGRYFHSYFRSSAMNAYYIQDRLEAQSWARHYQQLAREEKEAELADDMEKGLPQHLFESLCIDHLQRHGASKKSITRAFDDDVEFQERMAEHIRYMVETIAHHQVDIDSEV [Source organism chain B]=Escherichia phage lambda [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Escherichia phage lambda [Accession]=MF7000218 [Entry] [Entry number]=409 [Entry name]=GamS (bacteriophage lambda) [PDB ID]=2uv1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Host-nuclease inhibitor protein Gam [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. However, most likely dimer is the basic structural unit, since 2 M urea does not monomerize the NblA dimers. There are extensie helix packing interactions between the monomers (PMID:18718907). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000218,MF7000219 [UniProt ID chain A]=P03702 [UniProt boundaries chain A]=60-137 [UniProt coverage chain A]=56% [Name chain A]=Host-nuclease inhibitor protein gam [UniProt sequence chain A]=MDINTETEIKQKHSLTPFPVFLISPAFRGRYFHSYFRSSAMNAYYIQDRLEAQSWARHYQQLAREEKEAELADDMEKGLPQHLFESLCIDHLQRHGASKKSITRAFDDDVEFQERMAEHIRYMVETIAHHQVDIDSEV [Source organism chain A]=Escherichia phage lambda [UniProt ID chain B]=P03702 [UniProt boundaries chain B]=59-137 [UniProt coverage chain B]=57% [Name chain B]=Host-nuclease inhibitor protein gam [UniProt sequence chain B]=MDINTETEIKQKHSLTPFPVFLISPAFRGRYFHSYFRSSAMNAYYIQDRLEAQSWARHYQQLAREEKEAELADDMEKGLPQHLFESLCIDHLQRHGASKKSITRAFDDDVEFQERMAEHIRYMVETIAHHQVDIDSEV [Source organism chain B]=Escherichia phage lambda [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Escherichia phage lambda [Accession]=MF7000219 [Entry] [Entry number]=410 [Entry name]=Dimerization domain of LAP2alpha [PDB ID]=2v0x [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:17562312). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q61033 [UniProt boundaries chain A]=465-685 [UniProt coverage chain A]=31% [Name chain A]=Lamina-associated polypeptide 2, isoforms alpha/zeta [UniProt sequence chain A]=MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLAAGANSKGPPDFSSDEEREPTPVLGSGASVGRGRGAVGRKATKKTDKPRLEDKDDLDVTELSNEELLDQLVRYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTVSSSAENTRQNGSNDSDRYSDNDEGKKKEHKKVKSARDCVPFSELASTPSGAFFQGISFPEISTRPPLGRTELQAAKKVQTTKRDPPRETCTDTALPGKGQTHKLAPGRSLFIPSESSYDRCVEKSSSPSSQREFAARLVSAAASPSLIRETTTTYSKDIVENICRGGKSRAQPLRAEEPGVSDQSVFSSEREVLQESERSQVISPPLAQAIRDYVNSLLVQGGVGSLPGTSDSVPTLDVENICKRLSQSSYQDSESLSPPRKVPRLSEKPARGGDSGSCVAFQNTPGSEHRSSFAKSVVSHSLTTLGVEVSKPPPQHDKIEASEPSFPLHESILKVVEEEWQQIDRQLPSVACRYPVSSIEAARILSVPKVDDEILGFISEATPRAATQASSTESCDKHLDLALCRSYEAAASALQIAAHTAFVAKSLQADISQAAQIINSDPSDAQQALRILNRTYDAASYLCDAAFDEVRMSACAMGSSTMGRRYLWLKDCKISPASKNKLTVAPFKGGTLFGGEVHKVIKKRGNKQ [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q61033 [UniProt boundaries chain B]=465-689 [UniProt coverage chain B]=32% [Name chain B]=Lamina-associated polypeptide 2, isoforms alpha/zeta [UniProt sequence chain B]=MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLAAGANSKGPPDFSSDEEREPTPVLGSGASVGRGRGAVGRKATKKTDKPRLEDKDDLDVTELSNEELLDQLVRYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTVSSSAENTRQNGSNDSDRYSDNDEGKKKEHKKVKSARDCVPFSELASTPSGAFFQGISFPEISTRPPLGRTELQAAKKVQTTKRDPPRETCTDTALPGKGQTHKLAPGRSLFIPSESSYDRCVEKSSSPSSQREFAARLVSAAASPSLIRETTTTYSKDIVENICRGGKSRAQPLRAEEPGVSDQSVFSSEREVLQESERSQVISPPLAQAIRDYVNSLLVQGGVGSLPGTSDSVPTLDVENICKRLSQSSYQDSESLSPPRKVPRLSEKPARGGDSGSCVAFQNTPGSEHRSSFAKSVVSHSLTTLGVEVSKPPPQHDKIEASEPSFPLHESILKVVEEEWQQIDRQLPSVACRYPVSSIEAARILSVPKVDDEILGFISEATPRAATQASSTESCDKHLDLALCRSYEAAASALQIAAHTAFVAKSLQADISQAAQIINSDPSDAQQALRILNRTYDAASYLCDAAFDEVRMSACAMGSSTMGRRYLWLKDCKISPASKNKLTVAPFKGGTLFGGEVHKVIKKRGNKQ [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Mus musculus [Accession]=MF7000220 [Entry] [Entry number]=411 [Entry name]=Stationary Phase Survival Protein SurE (Salmonella typhimurium) [PDB ID]=2v4n [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Survival protein SurE [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding (PMID:23409101). Domain-swapped dimer with extensive swap region and large dimer interface. Dimeric in solution (gel filtration, DLS). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000821,MF7000221,MF7000222,MF7000224,MF7000227,MF7000223,MF7000225,MF7000226 [UniProt ID chain A]=P66881 [UniProt boundaries chain A]=1-253 [UniProt coverage chain A]=100% [Name chain A]=5'/3'-nucleotidase SurE [UniProt sequence chain A]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain A]=Salmonella typhimurium [UniProt ID chain A-2]=P66881 [UniProt boundaries chain A-2]=1-253 [UniProt coverage chain A-2]=100% [Name chain A-2]=5'/3'-nucleotidase SurE [UniProt sequence chain A-2]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain A-2]=Salmonella typhimurium [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Salmonella typhimurium [Accession]=MF7000221 [Entry] [Entry number]=412 [Entry name]=SurE H234A mutant (Salmonella typhimurium) [PDB ID]=4g9o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Survival protein SurE [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding (PMID:23409101). Domain-swapped dimer with extensive swap region and large dimer interface. Dimeric in solution (gel filtration, DLS). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000821,MF7000221,MF7000222,MF7000224,MF7000227,MF7000223,MF7000225,MF7000226 [UniProt ID chain A]=P66881 [UniProt boundaries chain A]=1-252 [UniProt coverage chain A]=99% [Name chain A]=5'/3'-nucleotidase SurE [UniProt sequence chain A]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain A]=Salmonella typhimurium [UniProt ID chain B]=P66881 [UniProt boundaries chain B]=1-253 [UniProt coverage chain B]=100% [Name chain B]=5'/3'-nucleotidase SurE [UniProt sequence chain B]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain B]=Salmonella typhimurium [ExpTech]=X-ray [Resolution]=2.12 [Source organism]=Salmonella typhimurium [Accession]=MF7000222 [Entry] [Entry number]=413 [Entry name]=SurE, E112A/D230A mutant (Salmonella typhimurium) [PDB ID]=4xh8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Survival protein SurE [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding (PMID:23409101). Domain-swapped dimer with extensive swap region and large dimer interface. Dimeric in solution (gel filtration, DLS). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000821,MF7000221,MF7000222,MF7000224,MF7000227,MF7000223,MF7000225,MF7000226 [UniProt ID chain A]=P66881 [UniProt boundaries chain A]=1-253 [UniProt coverage chain A]=100% [Name chain A]=5'/3'-nucleotidase SurE [UniProt sequence chain A]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain A]=Salmonella typhimurium [UniProt ID chain B]=P66881 [UniProt boundaries chain B]=1-253 [UniProt coverage chain B]=100% [Name chain B]=5'/3'-nucleotidase SurE [UniProt sequence chain B]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain B]=Salmonella typhimurium [ExpTech]=X-ray [Resolution]=3.56 [Source organism]=Salmonella typhimurium [Accession]=MF7000223 [Entry] [Entry number]=414 [Entry name]=SurE D230A/H234A mutant (Salmonella typhimurium) [PDB ID]=4gad [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Survival protein SurE [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding (PMID:23409101). Domain-swapped dimer with extensive swap region and large dimer interface. Dimeric in solution (gel filtration, DLS). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000821,MF7000221,MF7000222,MF7000224,MF7000227,MF7000223,MF7000225,MF7000226 [UniProt ID chain A]=P66881 [UniProt boundaries chain A]=1-251 [UniProt coverage chain A]=99% [Name chain A]=5'/3'-nucleotidase SurE [UniProt sequence chain A]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain A]=Salmonella typhimurium [UniProt ID chain B]=P66881 [UniProt boundaries chain B]=3-253 [UniProt coverage chain B]=99% [Name chain B]=5'/3'-nucleotidase SurE [UniProt sequence chain B]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain B]=Salmonella typhimurium [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Salmonella typhimurium [Accession]=MF7000224 [Entry] [Entry number]=415 [Entry name]=SurE, E112A mutant F222 form (Salmonella typhimurium) [PDB ID]=4ryt [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Survival protein SurE [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding (PMID:23409101). Domain-swapped dimer with extensive swap region and large dimer interface. Dimeric in solution (gel filtration, DLS). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000821,MF7000221,MF7000222,MF7000224,MF7000227,MF7000223,MF7000225,MF7000226 [UniProt ID chain A]=P66881 [UniProt boundaries chain A]=1-253 [UniProt coverage chain A]=100% [Name chain A]=5'/3'-nucleotidase SurE [UniProt sequence chain A]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain A]=Salmonella typhimurium [UniProt ID chain A-2]=P66881 [UniProt boundaries chain A-2]=1-253 [UniProt coverage chain A-2]=100% [Name chain A-2]=5'/3'-nucleotidase SurE [UniProt sequence chain A-2]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain A-2]=Salmonella typhimurium [ExpTech]=X-ray [Resolution]=2.09 [Source organism]=Salmonella typhimurium [Accession]=MF7000225 [Entry] [Entry number]=416 [Entry name]=SurE, E112A/H234A mutant F222 form (Salmonella typhimurium) [PDB ID]=4xep [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Survival protein SurE [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding (PMID:23409101). Domain-swapped dimer with extensive swap region and large dimer interface. Dimeric in solution (gel filtration, DLS). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000821,MF7000221,MF7000222,MF7000224,MF7000227,MF7000223,MF7000225,MF7000226 [UniProt ID chain A]=P66881 [UniProt boundaries chain A]=1-253 [UniProt coverage chain A]=100% [Name chain A]=5'/3'-nucleotidase SurE [UniProt sequence chain A]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain A]=Salmonella typhimurium [UniProt ID chain A-2]=P66881 [UniProt boundaries chain A-2]=1-253 [UniProt coverage chain A-2]=100% [Name chain A-2]=5'/3'-nucleotidase SurE [UniProt sequence chain A-2]=MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFDNGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLNGYQHYDTAAAVTCALLRGLSREPLRTGRILNVNVPDLPLAQVKGIRVTRCGSRHPADKVIPQEDPRGNTLYWIGPPGDKYDAGPDTDFAAVDEGYVSVTPLHVDLTAHSAHDVVSDWLDSVGVGTQW [Source organism chain A-2]=Salmonella typhimurium [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Salmonella typhimurium [Accession]=MF7000226 [Entry] [Entry number]=417 [Entry name]=SurE (Coxiella burnetii) [PDB ID]=3ty2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Survival protein SurE [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding (PMID:23409101). Domain-swapped dimer with extensive swap region and large dimer interface. Dimeric in solution (gel filtration, DLS). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000821,MF7000221,MF7000222,MF7000224,MF7000227,MF7000223,MF7000225,MF7000226 [UniProt ID chain A]=Q9KI21 [UniProt boundaries chain A]=8-258 [UniProt coverage chain A]=97% [Name chain A]=5'-nucleotidase SurE [UniProt sequence chain A]=MKKTATPKLRLLLSNDDGVYAKGLAILAKTLADLGEVDVVAPDRNRSGASNSLTLNAPLHIKNLENGMISVEGTPTDCVHLAITGVLPEMPDMVVAGINAGPNLGDDVWYSGTVAAAMEGRFLGLPALAVSLGGELFRYYETAAKVVYQLIQRIEKDPLPPSTILNINVPDLPYEELKGFEVTRLGTRHRAEPTIRQIDPRGHPIYWVGAAGPEQDSGPGTDFFAMNHHCVSITPLRVDLTHYEAFDQLASWVKRLEM [Source organism chain A]=Coxiella burnetii [UniProt ID chain B]=Q9KI21 [UniProt boundaries chain B]=8-258 [UniProt coverage chain B]=97% [Name chain B]=5'-nucleotidase SurE [UniProt sequence chain B]=MKKTATPKLRLLLSNDDGVYAKGLAILAKTLADLGEVDVVAPDRNRSGASNSLTLNAPLHIKNLENGMISVEGTPTDCVHLAITGVLPEMPDMVVAGINAGPNLGDDVWYSGTVAAAMEGRFLGLPALAVSLGGELFRYYETAAKVVYQLIQRIEKDPLPPSTILNINVPDLPYEELKGFEVTRLGTRHRAEPTIRQIDPRGHPIYWVGAAGPEQDSGPGTDFFAMNHHCVSITPLRVDLTHYEAFDQLASWVKRLEM [Source organism chain B]=Coxiella burnetii [ExpTech]=X-ray [Resolution]=1.89 [Source organism]=Coxiella burnetii [Accession]=MF7000227 [Entry] [Entry number]=419 [Entry name]=N-terminal domain of DivIVA [PDB ID]=2wuj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=DivIVA protein [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:20502438). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000229,MF7000345 [UniProt ID chain A]=P71021 [UniProt boundaries chain A]=3-52 [UniProt coverage chain A]=30% [Name chain A]=Septum site-determining protein DivIVA [UniProt sequence chain A]=MPLTPNDIHNKTFTKSFRGYDEDEVNEFLAQVRKDYEIVLRKKTELEAKVNELDERIGHFANIEETLNKSILVAQEAAEDVKRNSQKEAKLIVREAEKNADRIINESLSKSRKIAMEIEELKKQSKVFRTRFQMLIEAQLDLLKNDDWDHLLEYEVDAVFEEKE [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P71021 [UniProt boundaries chain B]=3-52 [UniProt coverage chain B]=30% [Name chain B]=Septum site-determining protein DivIVA [UniProt sequence chain B]=MPLTPNDIHNKTFTKSFRGYDEDEVNEFLAQVRKDYEIVLRKKTELEAKVNELDERIGHFANIEETLNKSILVAQEAAEDVKRNSQKEAKLIVREAEKNADRIINESLSKSRKIAMEIEELKKQSKVFRTRFQMLIEAQLDLLKNDDWDHLLEYEVDAVFEEKE [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Bacillus subtilis [Accession]=MF7000229 [Entry] [Entry number]=420 [Entry name]=Hypothetical protein ORF131 (Pyrobaculum Spherical Virus) [PDB ID]=2x5c [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disoder of the monomeric forms. However, the dimeric structure is highly intertwined, with extensive helix packing interactions between the monomers. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q6ZYH1 [UniProt boundaries chain A]=29-127 [UniProt coverage chain A]=76% [Name chain A]=Uncharacterized protein [UniProt sequence chain A]=MGETPEGPMPNKKGKSEGGQIRTIPLKYYKQEYDMAADLVRMLRGLGVFMHAKCPRCGAEGSVSIVETKNGYKYLVIRHPDGGTHTVPKTDISAILKELCEVKKDLEYVLKRYKEYEEEGGVKFCAEGRK [Source organism chain A]=Pyrobaculum spherical virus [UniProt ID chain A-2]=Q6ZYH1 [UniProt boundaries chain A-2]=29-129 [UniProt coverage chain A-2]=77% [Name chain A-2]=Uncharacterized protein [UniProt sequence chain A-2]=MGETPEGPMPNKKGKSEGGQIRTIPLKYYKQEYDMAADLVRMLRGLGVFMHAKCPRCGAEGSVSIVETKNGYKYLVIRHPDGGTHTVPKTDISAILKELCEVKKDLEYVLKRYKEYEEEGGVKFCAEGRK [Source organism chain A-2]=Pyrobaculum spherical virus [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Pyrobaculum spherical virus [Accession]=MF7000374 [Entry] [Entry number]=421 [Entry name]=Dimerization domain of Qua1 [PDB ID]=2xa6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Each monomer consists of two antiparallel α-helices connected by a short loop. The two subunits are arranged perpendicular to each other in an unusual four-helix topology (PMID:20610388). Qua1 forms obligate dimers in which dimer dissociation and unfolding of the monomer secondary structure occur simultaneously and a folded monomeric Qua1 domain likely does not exist (PMID:22982292). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q07666 [UniProt boundaries chain A]=99-135 [UniProt coverage chain A]=8% [Name chain A]=KH domain-containing, RNA-binding, signal transduction-associated protein 1 [UniProt sequence chain A]=MQRRDDPAARMSRSSGRSGSMDPSGAHPSVRQTPSRQPPLPHRSRGGGGGSRGGARASPATQPPPLLPPSATGPDATVGGPAPTPLLPPSATASVKMEPENKYLPELMAEKDSLDPSFTHAMQLLTAEIEKIQKGDSKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVPVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGAITRGATVTRGVPPPPTVRGAPAPRARTAGIQRIPLPPPPAPETYEEYGYDDTYAEQSYEGYEGYYSQSQGDSEYYDYGHGEVQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q07666 [UniProt boundaries chain B]=99-135 [UniProt coverage chain B]=8% [Name chain B]=KH domain-containing, RNA-binding, signal transduction-associated protein 1 [UniProt sequence chain B]=MQRRDDPAARMSRSSGRSGSMDPSGAHPSVRQTPSRQPPLPHRSRGGGGGSRGGARASPATQPPPLLPPSATGPDATVGGPAPTPLLPPSATASVKMEPENKYLPELMAEKDSLDPSFTHAMQLLTAEIEKIQKGDSKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVPVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGAITRGATVTRGVPPPPTVRGAPAPRARTAGIQRIPLPPPPAPETYEEYGYDDTYAEQSYEGYEGYYSQSQGDSEYYDYGHGEVQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000231 [Entry] [Entry number]=422 [Entry name]=DR2231 [PDB ID]=2yf9 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Phosphoribosyl-ATP pyrophosphohydrolase [Evidence level]=Direct evidence [Evidence text]=Phosphoribosyl-ATP pyrophosphohydrolases show a very unusual interlaced segment-swapped dimer, which implies that this obligatory dimer assembly is important for their function. Size-exclusion chromatography combined with static light scattering confirmed that the dimer is the major oligomeric state in solution (PMID:20944217). Upon dimer formation, DR2231 helices 2 and 3 from one monomer stack antiparallel to helices 2′ and 3′ of the other monomer, respectively. A stable four-helix bundle is formed in the center. The intertwining of the two hairpin structures produces an extensive subunit-subunit interface (PMID:21733847). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000284,MF7000232,MF7000233 [UniProt ID chain A]=Q9RS96 [UniProt boundaries chain A]=7-143 [UniProt coverage chain A]=92% [Name chain A]=HAD superfamily Cof-like phosphohydrolase [UniProt sequence chain A]=MSDLPCPPTNAERLHEFHRAIGAATPERPTPPPPELLRLRQTLLDEESAEVRAEIDHLLARQAAGEALSAGDLAPLAHELADLLYVTYGALDQLGIDADAVFAEVHRANLSKASGPRRADGKQLKPEGWRPADVRGVIERLQHAPADD [Source organism chain A]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [UniProt ID chain A-2]=Q9RS96 [UniProt boundaries chain A-2]=7-143 [UniProt coverage chain A-2]=92% [Name chain A-2]=HAD superfamily Cof-like phosphohydrolase [UniProt sequence chain A-2]=MSDLPCPPTNAERLHEFHRAIGAATPERPTPPPPELLRLRQTLLDEESAEVRAEIDHLLARQAAGEALSAGDLAPLAHELADLLYVTYGALDQLGIDADAVFAEVHRANLSKASGPRRADGKQLKPEGWRPADVRGVIERLQHAPADD [Source organism chain A-2]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [Accession]=MF7000232 [Entry] [Entry number]=423 [Entry name]=DR2232 (E46A mutant) [PDB ID]=5hwu [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Phosphoribosyl-ATP pyrophosphohydrolase [Evidence level]=Direct evidence [Evidence text]=Phosphoribosyl-ATP pyrophosphohydrolases show a very unusual interlaced segment-swapped dimer, which implies that this obligatory dimer assembly is important for their function. Size-exclusion chromatography combined with static light scattering confirmed that the dimer is the major oligomeric state in solution (PMID:20944217). Upon dimer formation, DR2231 helices 2 and 3 from one monomer stack antiparallel to helices 2′ and 3′ of the other monomer, respectively. A stable four-helix bundle is formed in the center. The intertwining of the two hairpin structures produces an extensive subunit-subunit interface (PMID:21733847). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000284,MF7000232,MF7000233 [UniProt ID chain A]=Q9RS96 [UniProt boundaries chain A]=7-144 [UniProt coverage chain A]=93% [Name chain A]=HAD superfamily Cof-like phosphohydrolase [UniProt sequence chain A]=MSDLPCPPTNAERLHEFHRAIGAATPERPTPPPPELLRLRQTLLDEESAEVRAEIDHLLARQAAGEALSAGDLAPLAHELADLLYVTYGALDQLGIDADAVFAEVHRANLSKASGPRRADGKQLKPEGWRPADVRGVIERLQHAPADD [Source organism chain A]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [UniProt ID chain B]=Q9RS96 [UniProt boundaries chain B]=7-144 [UniProt coverage chain B]=93% [Name chain B]=HAD superfamily Cof-like phosphohydrolase [UniProt sequence chain B]=MSDLPCPPTNAERLHEFHRAIGAATPERPTPPPPELLRLRQTLLDEESAEVRAEIDHLLARQAAGEALSAGDLAPLAHELADLLYVTYGALDQLGIDADAVFAEVHRANLSKASGPRRADGKQLKPEGWRPADVRGVIERLQHAPADD [Source organism chain B]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [Accession]=MF7000233 [Entry] [Entry number]=424 [Entry name]=Uncharacterized protein TTHA1756 [PDB ID]=2yzt [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=TTHA1013/TTHA0281-like [Evidence level]=No contradicting information [Evidence text]=Crystal structure and gel filtration indicate that TTHA1756 intrinsically forms a dimer. THA1756 forms a dimer through the formation of an eight-stranded b-sheet with b4 of one subunit intervening between b1 and b4 of the other subunit (PMID:18338381). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000977,MF7000234 [UniProt ID chain A]=Q5SHH4 [UniProt boundaries chain A]=1-67 [UniProt coverage chain A]=100% [Name chain A]=Type II toxin-antitoxin system HicB family antitoxin [UniProt sequence chain A]=MRRRYRVVVERDEEGYFVAHVPELHAHTQAQSFEELLRRLQEAIAVSLEEERAEVVGLEGALEIEAA [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SHH4 [UniProt boundaries chain A-2]=1-67 [UniProt coverage chain A-2]=100% [Name chain A-2]=Type II toxin-antitoxin system HicB family antitoxin [UniProt sequence chain A-2]=MRRRYRVVVERDEEGYFVAHVPELHAHTQAQSFEELLRRLQEAIAVSLEEERAEVVGLEGALEIEAA [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Thermus thermophilus [Accession]=MF7000234 [Entry] [Entry number]=425 [Entry name]=GrpE (Thermus thermophilus) [PDB ID]=3a6m [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Ubiquitin-like proteins [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Dimerization is mediated by a coiled coil subdomain taking up more 50% of the protein chains. Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815). The head domain is an independently folding unit, while the coiled coil region is responsible for dimerization and folds cooperatively. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q56236 [UniProt boundaries chain A]=4-171 [UniProt coverage chain A]=94% [Name chain A]=Protein GrpE [UniProt sequence chain A]=MEERNHENTLEKDLEAVGQEAQALEERLKAAEEELKGLKDKYLRLLADFDNYRKRMEEELKAREREGVLKALRALLPVLDDLDRALEFAEASPESIRQGVRAIRDGFFRILAGLGVEEVPGEGEAFDPRYHEAVGLLPGEPGKVAKVFQRGFRMGEALVRPARVAVGEEKREEADLE [Source organism chain A]=Thermus thermophilus [UniProt ID chain B]=Q56236 [UniProt boundaries chain B]=7-170 [UniProt coverage chain B]=92% [Name chain B]=Protein GrpE [UniProt sequence chain B]=MEERNHENTLEKDLEAVGQEAQALEERLKAAEEELKGLKDKYLRLLADFDNYRKRMEEELKAREREGVLKALRALLPVLDDLDRALEFAEASPESIRQGVRAIRDGFFRILAGLGVEEVPGEGEAFDPRYHEAVGLLPGEPGKVAKVFQRGFRMGEALVRPARVAVGEEKREEADLE [Source organism chain B]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=3.23 [Source organism]=Thermus thermophilus [Accession]=MF7000235 [Entry] [Entry number]=429 [Entry name]=YdjA (Escherichia coli) [PDB ID]=3bm1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P0ACY1 [UniProt boundaries chain A]=1-183 [UniProt coverage chain A]=100% [Name chain A]=Putative NAD(P)H nitroreductase YdjA [UniProt sequence chain A]=MDALELLINRRSASRLAEPAPTGEQLQNILRAGMRAPDHKSMQPWHFFVIEGEGRERFSAVLEQGAIAAGSDDKAIDKARNAPFRAPLIITVVAKCEENHKVPRWEQEMSAGCAVMAMQMAAVAQGFGGIWRSGALTESPVVREAFGCREQDKIVGFLYLGTPQLKASTSINVPDPTPFVTYF [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0ACY1 [UniProt boundaries chain B]=1-183 [UniProt coverage chain B]=100% [Name chain B]=Putative NAD(P)H nitroreductase YdjA [UniProt sequence chain B]=MDALELLINRRSASRLAEPAPTGEQLQNILRAGMRAPDHKSMQPWHFFVIEGEGRERFSAVLEQGAIAAGSDDKAIDKARNAPFRAPLIITVVAKCEENHKVPRWEQEMSAGCAVMAMQMAAVAQGFGGIWRSGALTESPVVREAFGCREQDKIVGFLYLGTPQLKASTSINVPDPTPFVTYF [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Escherichia coli [Accession]=MF7000239 [Entry] [Entry number]=430 [Entry name]=YdjA (Escherichia coli) [PDB ID]=3bm2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P0ACY1 [UniProt boundaries chain A]=1-183 [UniProt coverage chain A]=100% [Name chain A]=Putative NAD(P)H nitroreductase YdjA [UniProt sequence chain A]=MDALELLINRRSASRLAEPAPTGEQLQNILRAGMRAPDHKSMQPWHFFVIEGEGRERFSAVLEQGAIAAGSDDKAIDKARNAPFRAPLIITVVAKCEENHKVPRWEQEMSAGCAVMAMQMAAVAQGFGGIWRSGALTESPVVREAFGCREQDKIVGFLYLGTPQLKASTSINVPDPTPFVTYF [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0ACY1 [UniProt boundaries chain B]=1-183 [UniProt coverage chain B]=100% [Name chain B]=Putative NAD(P)H nitroreductase YdjA [UniProt sequence chain B]=MDALELLINRRSASRLAEPAPTGEQLQNILRAGMRAPDHKSMQPWHFFVIEGEGRERFSAVLEQGAIAAGSDDKAIDKARNAPFRAPLIITVVAKCEENHKVPRWEQEMSAGCAVMAMQMAAVAQGFGGIWRSGALTESPVVREAFGCREQDKIVGFLYLGTPQLKASTSINVPDPTPFVTYF [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Escherichia coli [Accession]=MF7000240 [Entry] [Entry number]=433 [Entry name]=MarR [PDB ID]=3bpv [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=O26413 [UniProt boundaries chain A]=5-141 [UniProt coverage chain A]=93% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MDRDIPLKGLLSIILRSHRVFIGRELGHLNLTDAQVACLLRIHREPGIKQDELATFFHVDKGTIARTLRRLEESGFIEREQDPENRRRYILEVTRRGEEIIPLILKVEERWEDLLFRDFTEDERKLFRKMCRRLAEEAVRMRGEWR [Source organism chain A]=10044 / NBRC 100330 / Delta H) [UniProt ID chain A-2]=O26413 [UniProt boundaries chain A-2]=5-141 [UniProt coverage chain A-2]=93% [Name chain A-2]=Transcriptional regulator [UniProt sequence chain A-2]=MDRDIPLKGLLSIILRSHRVFIGRELGHLNLTDAQVACLLRIHREPGIKQDELATFFHVDKGTIARTLRRLEESGFIEREQDPENRRRYILEVTRRGEEIIPLILKVEERWEDLLFRDFTEDERKLFRKMCRRLAEEAVRMRGEWR [Source organism chain A-2]=10044 / NBRC 100330 / Delta H) [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=10044 / NBRC 100330 / Delta H) [Accession]=MF7000243 [Entry] [Entry number]=434 [Entry name]=MarR [PDB ID]=3bpx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=O26413 [UniProt boundaries chain A]=1-145 [UniProt coverage chain A]=99% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MDRDIPLKGLLSIILRSHRVFIGRELGHLNLTDAQVACLLRIHREPGIKQDELATFFHVDKGTIARTLRRLEESGFIEREQDPENRRRYILEVTRRGEEIIPLILKVEERWEDLLFRDFTEDERKLFRKMCRRLAEEAVRMRGEWR [Source organism chain A]=10044 / NBRC 100330 / Delta H) [UniProt ID chain B]=O26413 [UniProt boundaries chain B]=4-141 [UniProt coverage chain B]=94% [Name chain B]=Transcriptional regulator [UniProt sequence chain B]=MDRDIPLKGLLSIILRSHRVFIGRELGHLNLTDAQVACLLRIHREPGIKQDELATFFHVDKGTIARTLRRLEESGFIEREQDPENRRRYILEVTRRGEEIIPLILKVEERWEDLLFRDFTEDERKLFRKMCRRLAEEAVRMRGEWR [Source organism chain B]=10044 / NBRC 100330 / Delta H) [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=10044 / NBRC 100330 / Delta H) [Accession]=MF7000244 [Entry] [Entry number]=436 [Entry name]=Transcriptional regulator SlyA (Enterococcus faecalis) [PDB ID]=1lj9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=Q82ZP8 [UniProt boundaries chain A]=2-145 [UniProt coverage chain A]=96% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MTDILREIGMIARALDSISNIEFKELSLTRGQYLYLVRVCENPGIIQEKIAELIKVDRTTAARAIKRLEEQGFIYRQEDASNKKIKRIYATEKGKNVYPIIVRENQHSNQVALQGLSEVEISQLADYLVRMRKNVSEDWEFVKKGNTRNY [Source organism chain A]=Enterococcus faecalis [UniProt ID chain B]=Q82ZP8 [UniProt boundaries chain B]=2-143 [UniProt coverage chain B]=94% [Name chain B]=Transcriptional regulator, MarR family [UniProt sequence chain B]=MTDILREIGMIARALDSISNIEFKELSLTRGQYLYLVRVCENPGIIQEKIAELIKVDRTTAARAIKRLEEQGFIYRQEDASNKKIKRIYATEKGKNVYPIIVRENQHSNQVALQGLSEVEISQLADYLVRMRKNVSEDWEFVKKGNTRNY [Source organism chain B]=Enterococcus faecalis [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Enterococcus faecalis [Accession]=MF7000246 [Entry] [Entry number]=439 [Entry name]=MarR protein Rv2887 (Mycobacterium tuberculosis) [PDB ID]=5hsm [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=P9WME9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=99% [Name chain A]=HTH-type transcriptional repressor Rv2887 [UniProt sequence chain A]=MGLADDAPLGYLLYRVGAVLRPEVSAALSPLGLTLPEFVCLRMLSQSPGLSSAELARHASVTPQAMNTVLRKLEDAGAVARPASVSSGRSLPATLTARGRALAKRAEAVVRAADARVLARLTAPQQREFKRMLEKLGSD [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=P9WME9 [UniProt boundaries chain A-2]=1-138 [UniProt coverage chain A-2]=99% [Name chain A-2]=HTH-type transcriptional repressor Rv2887 [UniProt sequence chain A-2]=MGLADDAPLGYLLYRVGAVLRPEVSAALSPLGLTLPEFVCLRMLSQSPGLSSAELARHASVTPQAMNTVLRKLEDAGAVARPASVSSGRSLPATLTARGRALAKRAEAVVRAADARVLARLTAPQQREFKRMLEKLGSD [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000249 [Entry] [Entry number]=440 [Entry name]=MarR protein Rv2887 (Mycobacterium tuberculosis) [PDB ID]=5x7z [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=P9WME9 [UniProt boundaries chain A]=7-138 [UniProt coverage chain A]=94% [Name chain A]=HTH-type transcriptional repressor Rv2887 [UniProt sequence chain A]=MGLADDAPLGYLLYRVGAVLRPEVSAALSPLGLTLPEFVCLRMLSQSPGLSSAELARHASVTPQAMNTVLRKLEDAGAVARPASVSSGRSLPATLTARGRALAKRAEAVVRAADARVLARLTAPQQREFKRMLEKLGSD [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=P9WME9 [UniProt boundaries chain A-2]=7-138 [UniProt coverage chain A-2]=94% [Name chain A-2]=HTH-type transcriptional repressor Rv2887 [UniProt sequence chain A-2]=MGLADDAPLGYLLYRVGAVLRPEVSAALSPLGLTLPEFVCLRMLSQSPGLSSAELARHASVTPQAMNTVLRKLEDAGAVARPASVSSGRSLPATLTARGRALAKRAEAVVRAADARVLARLTAPQQREFKRMLEKLGSD [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000250 [Entry] [Entry number]=441 [Entry name]=MgrA [PDB ID]=2bv6 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (SarA type) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The major component linking the two monomers are α1-helices. The dimerization surface is highly hydrophobic and conserved (PMID:16455801). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000812,MF7000813,MF7000251,MF7000252,MF7000253,MF7000254,MF7000814,MF7000815 [UniProt ID chain A]=P0C1S0 [UniProt boundaries chain A]=5-141 [UniProt coverage chain A]=93% [Name chain A]=HTH-type transcriptional regulator MgrA [UniProt sequence chain A]=MSDQHNLKEQLCFSLYNAQRQVNRYYSNKVFKKYNLTYPQFLVLTILWDESPVNVKKVVTELALDTGTVSPLLKRMEQVDLIKRERSEVDQREVFIHLTDKSETIRPELSNASDKVASASSLSQDEVKELNRLLGKVIHAFDETKEK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain A-2]=P0C1S0 [UniProt boundaries chain A-2]=5-141 [UniProt coverage chain A-2]=93% [Name chain A-2]=HTH-type transcriptional regulator MgrA [UniProt sequence chain A-2]=MSDQHNLKEQLCFSLYNAQRQVNRYYSNKVFKKYNLTYPQFLVLTILWDESPVNVKKVVTELALDTGTVSPLLKRMEQVDLIKRERSEVDQREVFIHLTDKSETIRPELSNASDKVASASSLSQDEVKELNRLLGKVIHAFDETKEK [Source organism chain A-2]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.8 [Source organism]=Staphylococcus aureus [Accession]=MF7000251 [Entry] [Entry number]=442 [Entry name]=SarZ (Staphylococcus aureus) [PDB ID]=3hrm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (SarA type) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The major component linking the two monomers are α1-helices. The dimerization surface is highly hydrophobic and conserved (PMID:16455801). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000812,MF7000813,MF7000251,MF7000252,MF7000253,MF7000254,MF7000814,MF7000815 [UniProt ID chain A]=A0A0H3KA72 [UniProt boundaries chain A]=7-141 [UniProt coverage chain A]=91% [Name chain A]=MarR family regulatory protein [UniProt sequence chain A]=MYVENSYLSKQLCFLFYVSSKEIIKKYTNYLKEYDLTYTGYIVLMAIENDEKLNIKKLGERVFLDSGTLTPLLKKLEKKDYVVRTREEKDERNLQISLTEQGKAIKSPLAEISVKVFNEFNISEREASDIINNLRNFVSKNFDYSDKK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=A0A0H3KA72 [UniProt boundaries chain B]=7-139 [UniProt coverage chain B]=89% [Name chain B]=MarR family regulatory protein [UniProt sequence chain B]=MYVENSYLSKQLCFLFYVSSKEIIKKYTNYLKEYDLTYTGYIVLMAIENDEKLNIKKLGERVFLDSGTLTPLLKKLEKKDYVVRTREEKDERNLQISLTEQGKAIKSPLAEISVKVFNEFNISEREASDIINNLRNFVSKNFDYSDKK [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Staphylococcus aureus [Accession]=MF7000252 [Entry] [Entry number]=443 [Entry name]=SarZ (Staphylococcus aureus) [PDB ID]=3hse [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (SarA type) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The major component linking the two monomers are α1-helices. The dimerization surface is highly hydrophobic and conserved (PMID:16455801). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000812,MF7000813,MF7000251,MF7000252,MF7000253,MF7000254,MF7000814,MF7000815 [UniProt ID chain A]=A0A0H3KA72 [UniProt boundaries chain A]=7-139 [UniProt coverage chain A]=89% [Name chain A]=MarR family regulatory protein [UniProt sequence chain A]=MYVENSYLSKQLCFLFYVSSKEIIKKYTNYLKEYDLTYTGYIVLMAIENDEKLNIKKLGERVFLDSGTLTPLLKKLEKKDYVVRTREEKDERNLQISLTEQGKAIKSPLAEISVKVFNEFNISEREASDIINNLRNFVSKNFDYSDKK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=A0A0H3KA72 [UniProt boundaries chain B]=7-139 [UniProt coverage chain B]=89% [Name chain B]=MarR family regulatory protein [UniProt sequence chain B]=MYVENSYLSKQLCFLFYVSSKEIIKKYTNYLKEYDLTYTGYIVLMAIENDEKLNIKKLGERVFLDSGTLTPLLKKLEKKDYVVRTREEKDERNLQISLTEQGKAIKSPLAEISVKVFNEFNISEREASDIINNLRNFVSKNFDYSDKK [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.90 [Source organism]=Staphylococcus aureus [Accession]=MF7000253 [Entry] [Entry number]=444 [Entry name]=SarZ, mutant C13E (Staphylococcus aureus) [PDB ID]=4gxo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (SarA type) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The major component linking the two monomers are α1-helices. The dimerization surface is highly hydrophobic and conserved (PMID:16455801). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000812,MF7000813,MF7000251,MF7000252,MF7000253,MF7000254,MF7000814,MF7000815 [UniProt ID chain A]=A0A0H3KA72 [UniProt boundaries chain A]=7-141 [UniProt coverage chain A]=91% [Name chain A]=MarR family regulatory protein [UniProt sequence chain A]=MYVENSYLSKQLCFLFYVSSKEIIKKYTNYLKEYDLTYTGYIVLMAIENDEKLNIKKLGERVFLDSGTLTPLLKKLEKKDYVVRTREEKDERNLQISLTEQGKAIKSPLAEISVKVFNEFNISEREASDIINNLRNFVSKNFDYSDKK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=A0A0H3KA72 [UniProt boundaries chain B]=7-139 [UniProt coverage chain B]=89% [Name chain B]=MarR family regulatory protein [UniProt sequence chain B]=MYVENSYLSKQLCFLFYVSSKEIIKKYTNYLKEYDLTYTGYIVLMAIENDEKLNIKKLGERVFLDSGTLTPLLKKLEKKDYVVRTREEKDERNLQISLTEQGKAIKSPLAEISVKVFNEFNISEREASDIINNLRNFVSKNFDYSDKK [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Staphylococcus aureus [Accession]=MF7000254 [Entry] [Entry number]=445 [Entry name]=MarR (Clostridioides difficile) [PDB ID]=5eri [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=A0A031WDA8 [UniProt boundaries chain A]=2-148 [UniProt coverage chain A]=98% [Name chain A]=DNA-binding transcriptional repressor MarR [UniProt sequence chain A]=MIKTLDSNILREVGTLSRAVNSINDIKYKELKLQKGQFTFLTRICENPGINLVELSNMLKVDKATTTKAIQKLIKAGYVDKKQDKFDKRGYNLTPTDKSLEVYELIIEEENRSIEICFDNFTDEEKQVVTKLLEKMSKNVENEWFKVKR [Source organism chain A]=Clostridioides difficile [UniProt ID chain A-2]=A0A031WDA8 [UniProt boundaries chain A-2]=2-148 [UniProt coverage chain A-2]=98% [Name chain A-2]=DNA-binding transcriptional repressor MarR [UniProt sequence chain A-2]=MIKTLDSNILREVGTLSRAVNSINDIKYKELKLQKGQFTFLTRICENPGINLVELSNMLKVDKATTTKAIQKLIKAGYVDKKQDKFDKRGYNLTPTDKSLEVYELIIEEENRSIEICFDNFTDEEKQVVTKLLEKMSKNVENEWFKVKR [Source organism chain A-2]=Clostridioides difficile [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Clostridioides difficile [Accession]=MF7000255 [Entry] [Entry number]=446 [Entry name]=MarR (Bradyrhizobium japonicum) [PDB ID]=7kym [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=A0A0A3XYM8 [UniProt boundaries chain A]=9-160 [UniProt coverage chain A]=95% [Name chain A]=MarR family transcriptional regulator [UniProt sequence chain A]=MARESKSRWKSGPPRTRDQLQTYIPYLFNRLANRWNLDQNRDLSDHGINNVVFRTLSVLFIYKTLTVNEVAVLAVTEQSTASRMVESMVSSGLVKREIAEEDQRRRVVGLTPDGEALLRKIWPIMASNYDKLIEGIEPDDIEVCARVLARMVENIRQNQI [Source organism chain A]=Bradyrhizobium japonicum [UniProt ID chain B-2]=A0A0A3XYM8 [UniProt boundaries chain B-2]=12-160 [UniProt coverage chain B-2]=93% [Name chain B-2]=MarR family transcriptional regulator [UniProt sequence chain B-2]=MARESKSRWKSGPPRTRDQLQTYIPYLFNRLANRWNLDQNRDLSDHGINNVVFRTLSVLFIYKTLTVNEVAVLAVTEQSTASRMVESMVSSGLVKREIAEEDQRRRVVGLTPDGEALLRKIWPIMASNYDKLIEGIEPDDIEVCARVLARMVENIRQNQI [Source organism chain B-2]=Bradyrhizobium japonicum [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Bradyrhizobium japonicum [Accession]=MF7000256 [Entry] [Entry number]=447 [Entry name]=MazG (Escherichia coli) [PDB ID]=3cra [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=MazG nucleotide pyrophosphohydrolase domain [Evidence level]=Direct evidence [Evidence text]=CD denaturatrion fits two state model. A four-state thermal denaturation model fits all data including DSC in (dimeric N2 native, two dimeric intermadiate I2,S2, and monomeric denatured D states). The authors state that both native like intermediete states are dimeric. Thermally denatured monomeric state is not fully unfolded and contains a significant fraction of residual α-helical structure (PMID:19523960). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000257,MF7000258 [UniProt ID chain A]=P0AEY3 [UniProt boundaries chain A]=2-260 [UniProt coverage chain A]=98% [Name chain A]=Nucleoside triphosphate pyrophosphohydrolase [UniProt sequence chain A]=MNQIDRLLTIMQRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAIAREDFDDLRGELGDLLFQVVFYAQMAQEEGRFDFNDICAAISDKLERRHPHVFADSSAENSSEVLARWEQIKTEERAQKAQHSALDDIPRSLPALMRAQKIQKRCANVGFDWTTLGPVVDKVYEEIDEVMYEARQAVVDQAKLEEEMGDLLFATVNLARHLGTKAEIALQKANEKFERRFREVERIVAARGLEMTGVDLETMEEVWQQVKRQEIDL [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AEY3 [UniProt boundaries chain B]=2-261 [UniProt coverage chain B]=98% [Name chain B]=Nucleoside triphosphate pyrophosphohydrolase [UniProt sequence chain B]=MNQIDRLLTIMQRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAIAREDFDDLRGELGDLLFQVVFYAQMAQEEGRFDFNDICAAISDKLERRHPHVFADSSAENSSEVLARWEQIKTEERAQKAQHSALDDIPRSLPALMRAQKIQKRCANVGFDWTTLGPVVDKVYEEIDEVMYEARQAVVDQAKLEEEMGDLLFATVNLARHLGTKAEIALQKANEKFERRFREVERIVAARGLEMTGVDLETMEEVWQQVKRQEIDL [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Escherichia coli [Accession]=MF7000257 [Entry] [Entry number]=448 [Entry name]=MazG (Escherichia coli) [PDB ID]=3crc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=MazG nucleotide pyrophosphohydrolase domain [Evidence level]=Direct evidence [Evidence text]=CD denaturatrion fits two state model. A four-state thermal denaturation model fits all data including DSC in (dimeric N2 native, two dimeric intermadiate I2,S2, and monomeric denatured D states). The authors state that both native like intermediete states are dimeric. Thermally denatured monomeric state is not fully unfolded and contains a significant fraction of residual α-helical structure (PMID:19523960). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000257,MF7000258 [UniProt ID chain A]=P0AEY3 [UniProt boundaries chain A]=2-260 [UniProt coverage chain A]=98% [Name chain A]=Nucleoside triphosphate pyrophosphohydrolase [UniProt sequence chain A]=MNQIDRLLTIMQRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAIAREDFDDLRGELGDLLFQVVFYAQMAQEEGRFDFNDICAAISDKLERRHPHVFADSSAENSSEVLARWEQIKTEERAQKAQHSALDDIPRSLPALMRAQKIQKRCANVGFDWTTLGPVVDKVYEEIDEVMYEARQAVVDQAKLEEEMGDLLFATVNLARHLGTKAEIALQKANEKFERRFREVERIVAARGLEMTGVDLETMEEVWQQVKRQEIDL [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AEY3 [UniProt boundaries chain B]=2-261 [UniProt coverage chain B]=98% [Name chain B]=Nucleoside triphosphate pyrophosphohydrolase [UniProt sequence chain B]=MNQIDRLLTIMQRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAIAREDFDDLRGELGDLLFQVVFYAQMAQEEGRFDFNDICAAISDKLERRHPHVFADSSAENSSEVLARWEQIKTEERAQKAQHSALDDIPRSLPALMRAQKIQKRCANVGFDWTTLGPVVDKVYEEIDEVMYEARQAVVDQAKLEEEMGDLLFATVNLARHLGTKAEIALQKANEKFERRFREVERIVAARGLEMTGVDLETMEEVWQQVKRQEIDL [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Escherichia coli [Accession]=MF7000258 [Entry] [Entry number]=449 [Entry name]=NpR1517 [PDB ID]=3e56 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Monomeric Npun_R1517 is poorly packed alone with a large gap between α2 and α3. In the crystal, however, two symmetry-related Npun_R1517 molecules form an extensively interlocked dimer that is well packed and appears to be the functional biological assembly. There is beta sheet augmentation between the monomers. The authors imply that the monomer would be poorly packed (unstable) alone (PMID:19089958). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=B2IZS7 [UniProt boundaries chain A]=13-87 [UniProt coverage chain A]=79% [Name chain A]=Npun R1517 domain-containing protein [UniProt sequence chain A]=MNSKALPRQINNLEVGVYECEIHLKFRLIEEKSLLSDREQLLQVLLDALTEGSDDFLETLQASVKAQEVSEFKASPQMRRQLMRLRNAAENPPT [Source organism chain A]=Nostoc punctiforme [UniProt ID chain A-2]=B2IZS7 [UniProt boundaries chain A-2]=13-87 [UniProt coverage chain A-2]=79% [Name chain A-2]=Npun R1517 domain-containing protein [UniProt sequence chain A-2]=MNSKALPRQINNLEVGVYECEIHLKFRLIEEKSLLSDREQLLQVLLDALTEGSDDFLETLQASVKAQEVSEFKASPQMRRQLMRLRNAAENPPT [Source organism chain A-2]=Nostoc punctiforme [ExpTech]=X-ray [Resolution]=2.01 [Source organism]=Nostoc punctiforme [Accession]=MF7000259 [Entry] [Entry number]=453 [Entry name]=Soluble chemoreceptor from Thermotoga maritima [PDB ID]=3g67 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Methyl-accepting chemotaxis protein (MCP) signalling domain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:19149470). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000917,MF7000147,MF7000263,MF7000264 [UniProt ID chain A]=Q7DFA3 [UniProt boundaries chain A]=41-253 [UniProt coverage chain A]=76% [Name chain A]=Methyl-accepting chemotaxis protein, putative [UniProt sequence chain A]=MREREIVDKLTSAFFAENTIISFTSQLDEALTRKLRRMQRRIEEVKERFVNLNRLFQELVGDFQAKSDQLVSVIQDMEKISENIMEELKKSGTNVDQIVERVKEASSQIGETLENIRSIEKLIQNIMRIARETNILALNATIEAARAGEAGKGFMIVANEVQNLSNETNEVTKQIVEKAREILESSQRSLENLEFMANLFETVGKTLQNMVRFMENNVKLLQEVRNSLDTSKESLSEKSAEIDSATKVLEETAGGFTTINRVINSVITAQRKLKDLKI [Source organism chain A]=/ MSB8) [UniProt ID chain B]=Q7DFA3 [UniProt boundaries chain B]=41-252 [UniProt coverage chain B]=76% [Name chain B]=Methyl-accepting chemotaxis protein, putative [UniProt sequence chain B]=MREREIVDKLTSAFFAENTIISFTSQLDEALTRKLRRMQRRIEEVKERFVNLNRLFQELVGDFQAKSDQLVSVIQDMEKISENIMEELKKSGTNVDQIVERVKEASSQIGETLENIRSIEKLIQNIMRIARETNILALNATIEAARAGEAGKGFMIVANEVQNLSNETNEVTKQIVEKAREILESSQRSLENLEFMANLFETVGKTLQNMVRFMENNVKLLQEVRNSLDTSKESLSEKSAEIDSATKVLEETAGGFTTINRVINSVITAQRKLKDLKI [Source organism chain B]=/ MSB8) [ExpTech]=X-ray [Resolution]=2.17 [Source organism]=/ MSB8) [Accession]=MF7000263 [Entry] [Entry number]=454 [Entry name]=Soluble chemoreceptor from Thermotoga maritima (Asn217Ile mutant) [PDB ID]=3g6b [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Methyl-accepting chemotaxis protein (MCP) signalling domain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:19149470). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000917,MF7000147,MF7000263,MF7000264 [UniProt ID chain A]=Q7DFA3 [UniProt boundaries chain A]=41-253 [UniProt coverage chain A]=76% [Name chain A]=Methyl-accepting chemotaxis protein, putative [UniProt sequence chain A]=MREREIVDKLTSAFFAENTIISFTSQLDEALTRKLRRMQRRIEEVKERFVNLNRLFQELVGDFQAKSDQLVSVIQDMEKISENIMEELKKSGTNVDQIVERVKEASSQIGETLENIRSIEKLIQNIMRIARETNILALNATIEAARAGEAGKGFMIVANEVQNLSNETNEVTKQIVEKAREILESSQRSLENLEFMANLFETVGKTLQNMVRFMENNVKLLQEVRNSLDTSKESLSEKSAEIDSATKVLEETAGGFTTINRVINSVITAQRKLKDLKI [Source organism chain A]=/ MSB8) [UniProt ID chain B]=Q7DFA3 [UniProt boundaries chain B]=41-252 [UniProt coverage chain B]=76% [Name chain B]=Methyl-accepting chemotaxis protein, putative [UniProt sequence chain B]=MREREIVDKLTSAFFAENTIISFTSQLDEALTRKLRRMQRRIEEVKERFVNLNRLFQELVGDFQAKSDQLVSVIQDMEKISENIMEELKKSGTNVDQIVERVKEASSQIGETLENIRSIEKLIQNIMRIARETNILALNATIEAARAGEAGKGFMIVANEVQNLSNETNEVTKQIVEKAREILESSQRSLENLEFMANLFETVGKTLQNMVRFMENNVKLLQEVRNSLDTSKESLSEKSAEIDSATKVLEETAGGFTTINRVINSVITAQRKLKDLKI [Source organism chain B]=/ MSB8) [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=/ MSB8) [Accession]=MF7000264 [Entry] [Entry number]=455 [Entry name]=N-terminal EFC/F-BAR domain of Syp1 [PDB ID]=3g9g [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=yeast AH/BAR domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The overall structure is a crescent-shaped homodimer, as for other BAR domains. The two monomers interact tightly to form an antiparallel dimer with extensive buried surface area of 4000 Å2. Consistent with dimer formation, both full-length Syp1 and the EFC/F-BAR domain migrated as dimers by gel filtration. The EFC/F-BAR monomer consists of three central helices and six small helices with short connecting loops. The six long helices in the dimer form an 80 Å-long helical bundle. The small helices cap the two ends of the long helical bundle (PMID:19713939). The Syp1 EFC/F-BAR domain shows structural similarity to other EFC/F-BAR domains, and some other BAR domains were demonstrated to exhibit two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P25623 [UniProt boundaries chain A]=1-250 [UniProt coverage chain A]=28% [Name chain A]=Suppressor of yeast profilin deletion [UniProt sequence chain A]=MTEQRTKYADSILTTKSPYEATETIRIRLSQVKLLNKDFYLLFKELANLKRNYAQQLRKIIAENEDITKILNAQMIESNVLTPQEMSAFRFNSLGELRNVWDTVIEELKSDLKSSTEYYNTLDQQVVRELKESVENNTSWRESKDLHSKLSKNAASIEHYSKNNENSSHLEEARRQWDQQSPYLFELFETIDYNRLDTLKNCMLRFQTSFSDYLLNTTKECETVMTKFLAFEPQSEIDRFAKDASQYNFQLSSSSKEVVPNNASPASATGARPVSVSNGAANTEREKKSPQKDKRKSAFGNIGHRLASASSSLTHNDLMNNEFSDSTNNSSLKSKKSSHTLRSKVGSIFGRNKTKNKRQQQSSSNSHIQASITETPNNSSTRVSSTATSSIYQKQRRPTYSSSKSNNWTPGEASDTPPLPPHATPKNVDAPVTADTPPAQTFTPSEVPPSTPQQSSPPTAKEPDSSNLPKTVPISISQPPLQPQSKTKPLPVEPASPSISLPTATVDNQPSGQVDSRPLHIRAPALPPSRKQNFIHNRDSQLYDSLPNHGSGATPTSSSLSSIPQERPVSTLSSQITGELRELNPQATGSSTSLVGQSLFQHSSLDTSQFGLNASIAEVLNASFKDGMLQNSQLIGEIALNYLPNSVMNSPLPIGINLRINNGAKFEKVILNQAFIERVAPEEFKVNPSFIDSRTLGAIKYSIKEPIAPIVIHPVWRFESHQASVVLTVKMSPSLPDEISQIVIEDLVVFVNIDGANATSALSKPQGSFSKEKKRITWRFKEPVVLTRNGEGQRLIARFITDGLAHESAKGVITKFTISETDNVALPHSGAGSGITLTCQELDENNPFGGEWLDVNTKRTLTTGNYHGLA [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=P25623 [UniProt boundaries chain A-2]=1-250 [UniProt coverage chain A-2]=28% [Name chain A-2]=Suppressor of yeast profilin deletion [UniProt sequence chain A-2]=MTEQRTKYADSILTTKSPYEATETIRIRLSQVKLLNKDFYLLFKELANLKRNYAQQLRKIIAENEDITKILNAQMIESNVLTPQEMSAFRFNSLGELRNVWDTVIEELKSDLKSSTEYYNTLDQQVVRELKESVENNTSWRESKDLHSKLSKNAASIEHYSKNNENSSHLEEARRQWDQQSPYLFELFETIDYNRLDTLKNCMLRFQTSFSDYLLNTTKECETVMTKFLAFEPQSEIDRFAKDASQYNFQLSSSSKEVVPNNASPASATGARPVSVSNGAANTEREKKSPQKDKRKSAFGNIGHRLASASSSLTHNDLMNNEFSDSTNNSSLKSKKSSHTLRSKVGSIFGRNKTKNKRQQQSSSNSHIQASITETPNNSSTRVSSTATSSIYQKQRRPTYSSSKSNNWTPGEASDTPPLPPHATPKNVDAPVTADTPPAQTFTPSEVPPSTPQQSSPPTAKEPDSSNLPKTVPISISQPPLQPQSKTKPLPVEPASPSISLPTATVDNQPSGQVDSRPLHIRAPALPPSRKQNFIHNRDSQLYDSLPNHGSGATPTSSSLSSIPQERPVSTLSSQITGELRELNPQATGSSTSLVGQSLFQHSSLDTSQFGLNASIAEVLNASFKDGMLQNSQLIGEIALNYLPNSVMNSPLPIGINLRINNGAKFEKVILNQAFIERVAPEEFKVNPSFIDSRTLGAIKYSIKEPIAPIVIHPVWRFESHQASVVLTVKMSPSLPDEISQIVIEDLVVFVNIDGANATSALSKPQGSFSKEKKRITWRFKEPVVLTRNGEGQRLIARFITDGLAHESAKGVITKFTISETDNVALPHSGAGSGITLTCQELDENNPFGGEWLDVNTKRTLTTGNYHGLA [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000265 [Entry] [Entry number]=458 [Entry name]=glcT PRD domain (Bacillus subtilis) [PDB ID]=3gwh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. However, it is a very highly intertwined dimer, where the helices of the two monomers are fully supporting each other in the dimeric form, resembling histone domain dimers. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O31691 [UniProt boundaries chain A]=179-273 [UniProt coverage chain A]=33% [Name chain A]=PtsGHI operon antiterminator [UniProt sequence chain A]=MNGSFTVKKVLNNNVLIASHHKYSEVVLIGKGIGFGKKQDDVIEDKGYDKMFILKDEKEQKQFKKLLDYVDEKLVDISNDVIYHISNRTNHSLNEHIHIALTDHIAFAIKRQQQGFDMKNPFLMETQSLYPEEYQIAKEVIDMINEKAGLCLPEGEIGFIALHIHSALTNRPLSEVNQHSQLMAQLVEVIEDSFQMKVNKESVNYLRLIRHIRFTIERIKKEEPTKEPEKLMLLLKNEYPLCYNTAWKLIKILQQTLKKPVHEAEAVYLTLHLYRLTNKIS [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=O31691 [UniProt boundaries chain B]=178-273 [UniProt coverage chain B]=34% [Name chain B]=PtsGHI operon antiterminator [UniProt sequence chain B]=MNGSFTVKKVLNNNVLIASHHKYSEVVLIGKGIGFGKKQDDVIEDKGYDKMFILKDEKEQKQFKKLLDYVDEKLVDISNDVIYHISNRTNHSLNEHIHIALTDHIAFAIKRQQQGFDMKNPFLMETQSLYPEEYQIAKEVIDMINEKAGLCLPEGEIGFIALHIHSALTNRPLSEVNQHSQLMAQLVEVIEDSFQMKVNKESVNYLRLIRHIRFTIERIKKEEPTKEPEKLMLLLKNEYPLCYNTAWKLIKILQQTLKKPVHEAEAVYLTLHLYRLTNKIS [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Bacillus subtilis [Accession]=MF7000268 [Entry] [Entry number]=460 [Entry name]=FAD-binding domain from mimivirus sulfhydryl oxidase R596 [PDB ID]=3gwn [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=ERV/ALR sulfhydryl oxidase domain [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000866,MF7000270,MF7000867,MF7000868,MF7000869,MF7000870 [UniProt ID chain A]=Q5UP54 [UniProt boundaries chain A]=33-144 [UniProt coverage chain A]=38% [Name chain A]=Probable FAD-linked sulfhydryl oxidase R596 [UniProt sequence chain A]=MSLSKQVVPTHRVEIAPNSESTCKMDHSNYQHNGLITKIWGTAGWTFNHAVTFGYPLNPTSDDKRRYKNYFISLGDVLPCRLCRESYKKFITTGKTALTNEVLRNRHTLTKWFYDVHNAVNNKLEVDYGLSYEDVVNKYESFRAKCGKPVPTVKGCVTPLDHKAFSFKKLYYMDAPIVSLDKVENFVRIARMRGISDKYFCFLELATVLNGDFNELKKQSSWEYRNKYCQKKIRHMRENAIPSIEEQGYWKGTPTIDELKLLLFLCSNLNRTEVNDAINNVERLESTHYIEN [Source organism chain A]=Acanthamoeba polyphaga mimivirus [UniProt ID chain B]=Q5UP54 [UniProt boundaries chain B]=33-144 [UniProt coverage chain B]=38% [Name chain B]=Probable FAD-linked sulfhydryl oxidase R596 [UniProt sequence chain B]=MSLSKQVVPTHRVEIAPNSESTCKMDHSNYQHNGLITKIWGTAGWTFNHAVTFGYPLNPTSDDKRRYKNYFISLGDVLPCRLCRESYKKFITTGKTALTNEVLRNRHTLTKWFYDVHNAVNNKLEVDYGLSYEDVVNKYESFRAKCGKPVPTVKGCVTPLDHKAFSFKKLYYMDAPIVSLDKVENFVRIARMRGISDKYFCFLELATVLNGDFNELKKQSSWEYRNKYCQKKIRHMRENAIPSIEEQGYWKGTPTIDELKLLLFLCSNLNRTEVNDAINNVERLESTHYIEN [Source organism chain B]=Acanthamoeba polyphaga mimivirus [ExpTech]=X-ray [Resolution]=1.78 [Source organism]=Acanthamoeba polyphaga mimivirus [Accession]=MF7000270 [Entry] [Entry number]=461 [Entry name]=C-terminal domain of a putative HIV-1 gp41 fusion intermediate [PDB ID]=3gwo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Envelope glycoprotein gp160 helix hairpin [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:19846514). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000271,MF7000272 [UniProt ID chain A]=Q70626 [UniProt boundaries chain A]=631-683 [UniProt coverage chain A]=6% [Name chain A]=Envelope glycoprotein gp160 [UniProt sequence chain A]=MRVKEKYQHLRRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGGMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKHDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEVVIRSANLTDNVKTIIVQLNQSVEINCTRPNNNTRKRIRIQRGPGRTFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQYGNNKTIIFKQSSGGDLEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGNNNNGSEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGHSPLSFQTHLPTPGGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL [Source organism chain A]= [UniProt ID chain B]=Q70626 [UniProt boundaries chain B]=641-681 [UniProt coverage chain B]=4% [Name chain B]=Envelope glycoprotein gp160 [UniProt sequence chain B]=MRVKEKYQHLRRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGGMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKHDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEVVIRSANLTDNVKTIIVQLNQSVEINCTRPNNNTRKRIRIQRGPGRTFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQYGNNKTIIFKQSSGGDLEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGNNNNGSEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGHSPLSFQTHLPTPGGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.65 [Source organism]= [Accession]=MF7000271 [Entry] [Entry number]=462 [Entry name]=C-terminal domain of a putative HIV-1 gp41 fusion intermediate [PDB ID]=3h01 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Envelope glycoprotein gp160 helix hairpin [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:19846514). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000271,MF7000272 [UniProt ID chain A]=Q70626 [UniProt boundaries chain A]=630-683 [UniProt coverage chain A]=6% [Name chain A]=Envelope glycoprotein gp160 [UniProt sequence chain A]=MRVKEKYQHLRRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGGMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKHDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEVVIRSANLTDNVKTIIVQLNQSVEINCTRPNNNTRKRIRIQRGPGRTFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQYGNNKTIIFKQSSGGDLEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGNNNNGSEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGHSPLSFQTHLPTPGGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL [Source organism chain A]= [UniProt ID chain B]=Q70626 [UniProt boundaries chain B]=638-683 [UniProt coverage chain B]=5% [Name chain B]=Envelope glycoprotein gp160 [UniProt sequence chain B]=MRVKEKYQHLRRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGGMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKHDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEVVIRSANLTDNVKTIIVQLNQSVEINCTRPNNNTRKRIRIQRGPGRTFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQYGNNKTIIFKQSSGGDLEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGNNNNGSEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGHSPLSFQTHLPTPGGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.70 [Source organism]= [Accession]=MF7000272 [Entry] [Entry number]=463 [Entry name]=Nucleosome assembly protein (Plasmodium falciparum) [PDB ID]=3gyv [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Nucleosome assembly protein (NAP) [Sequence domain]=Nucleosome assembly protein (NAP) [Evidence level]=Indirect evidence [Evidence text]=A long α-helix is responsible for homodimerization via a previously uncharacterized antiparallel non-coiled-coil, and an alpha/beta domain is implicated in protein-protein interaction (PMID:16432217). The protein is dimer in solution (gel-filtration and glutaraldehyde cross-linking). The CD spectra revealed abundance of random coils in both PfNAPS and PfNAPL (30 and 45%, respectively) suggesting inherent flexibility in these proteins (PMID:15899528). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000275,MF7000276,MF7000273,MF7000274 [UniProt ID chain A]=Q8I608 [UniProt boundaries chain A]=36-281 [UniProt coverage chain A]=70% [Name chain A]=Nucleosome assembly protein [UniProt sequence chain A]=MAANEGNQPIPPEEEKEISSLLESIKIDDDKMTDLTEEQKETLKKLKLYQKEYYDYESKFEYELFLLRQKYHDLYGPIYDKRREALVGNGEAKIGTPNLPEFWLRALRNNNTVSHVIEDHDEEILVYLNDIRCDYIKKNKEKKEGFILSFYFATNPFFSNSVLTKTYHMKCVDCDNEPVLLHTEATVIDWYDNKNILKKNVVKKQHNKNSREVKTVQQTVNRDSFFHFFTSHKVPNSNVIKQLSKHEVAQLEMIIEGDYEVALTIKERIIPYAVDYYLGIIIESESNSIVSDVDSSYSSSENNSNYNSYESNNSAYNDENSNVDTNEYDDNEEEEEGAKSNEDPLTS [Source organism chain A]=Plasmodium falciparum [UniProt ID chain A-2]=Q8I608 [UniProt boundaries chain A-2]=36-281 [UniProt coverage chain A-2]=70% [Name chain A-2]=Nucleosome assembly protein [UniProt sequence chain A-2]=MAANEGNQPIPPEEEKEISSLLESIKIDDDKMTDLTEEQKETLKKLKLYQKEYYDYESKFEYELFLLRQKYHDLYGPIYDKRREALVGNGEAKIGTPNLPEFWLRALRNNNTVSHVIEDHDEEILVYLNDIRCDYIKKNKEKKEGFILSFYFATNPFFSNSVLTKTYHMKCVDCDNEPVLLHTEATVIDWYDNKNILKKNVVKKQHNKNSREVKTVQQTVNRDSFFHFFTSHKVPNSNVIKQLSKHEVAQLEMIIEGDYEVALTIKERIIPYAVDYYLGIIIESESNSIVSDVDSSYSSSENNSNYNSYESNNSAYNDENSNVDTNEYDDNEEEEEGAKSNEDPLTS [Source organism chain A-2]=Plasmodium falciparum [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Plasmodium falciparum [Accession]=MF7000273 [Entry] [Entry number]=464 [Entry name]=Nucleosome assembly protein (Plasmodium falciparum) [PDB ID]=3gyw [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Nucleosome assembly protein (NAP) [Sequence domain]=Nucleosome assembly protein (NAP) [Evidence level]=Indirect evidence [Evidence text]=A long α-helix is responsible for homodimerization via a previously uncharacterized antiparallel non-coiled-coil, and an alpha/beta domain is implicated in protein-protein interaction (PMID:16432217). The protein is dimer in solution (gel-filtration and glutaraldehyde cross-linking). The CD spectra revealed abundance of random coils in both PfNAPS and PfNAPL (30 and 45%, respectively) suggesting inherent flexibility in these proteins (PMID:15899528). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000275,MF7000276,MF7000273,MF7000274 [UniProt ID chain A]=Q8I608 [UniProt boundaries chain A]=35-281 [UniProt coverage chain A]=71% [Name chain A]=Nucleosome assembly protein [UniProt sequence chain A]=MAANEGNQPIPPEEEKEISSLLESIKIDDDKMTDLTEEQKETLKKLKLYQKEYYDYESKFEYELFLLRQKYHDLYGPIYDKRREALVGNGEAKIGTPNLPEFWLRALRNNNTVSHVIEDHDEEILVYLNDIRCDYIKKNKEKKEGFILSFYFATNPFFSNSVLTKTYHMKCVDCDNEPVLLHTEATVIDWYDNKNILKKNVVKKQHNKNSREVKTVQQTVNRDSFFHFFTSHKVPNSNVIKQLSKHEVAQLEMIIEGDYEVALTIKERIIPYAVDYYLGIIIESESNSIVSDVDSSYSSSENNSNYNSYESNNSAYNDENSNVDTNEYDDNEEEEEGAKSNEDPLTS [Source organism chain A]=Plasmodium falciparum [UniProt ID chain A-2]=Q8I608 [UniProt boundaries chain A-2]=35-281 [UniProt coverage chain A-2]=71% [Name chain A-2]=Nucleosome assembly protein [UniProt sequence chain A-2]=MAANEGNQPIPPEEEKEISSLLESIKIDDDKMTDLTEEQKETLKKLKLYQKEYYDYESKFEYELFLLRQKYHDLYGPIYDKRREALVGNGEAKIGTPNLPEFWLRALRNNNTVSHVIEDHDEEILVYLNDIRCDYIKKNKEKKEGFILSFYFATNPFFSNSVLTKTYHMKCVDCDNEPVLLHTEATVIDWYDNKNILKKNVVKKQHNKNSREVKTVQQTVNRDSFFHFFTSHKVPNSNVIKQLSKHEVAQLEMIIEGDYEVALTIKERIIPYAVDYYLGIIIESESNSIVSDVDSSYSSSENNSNYNSYESNNSAYNDENSNVDTNEYDDNEEEEEGAKSNEDPLTS [Source organism chain A-2]=Plasmodium falciparum [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Plasmodium falciparum [Accession]=MF7000274 [Entry] [Entry number]=465 [Entry name]=Nucleosome assembly protein 1 (NAP-1) [PDB ID]=2ayu [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Nucleosome assembly protein (NAP) [Sequence domain]=Nucleosome assembly protein (NAP) [Evidence level]=Indirect evidence [Evidence text]=A long α-helix is responsible for homodimerization via a previously uncharacterized antiparallel non-coiled-coil, and an alpha/beta domain is implicated in protein-protein interaction (PMID:16432217). The protein is dimer in solution (gel-filtration and glutaraldehyde cross-linking). The CD spectra revealed abundance of random coils in both PfNAPS and PfNAPL (30 and 45%, respectively) suggesting inherent flexibility in these proteins (PMID:15899528). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000275,MF7000276,MF7000273,MF7000274 [UniProt ID chain A]=P25293 [UniProt boundaries chain A]=70-370 [UniProt coverage chain A]=72% [Name chain A]=Nucleosome assembly protein [UniProt sequence chain A]=MSDPIRTKPKSSMQIDNAPTPHNTPASVLNPSYLKNGNPVRAQAQEQDDKIGTINEEDILANQPLLLQSIQDRLGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKEFQVEMFELENKFLQKYKPIWEQRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEKAQNDSEEEQVKGIPSFWLTALENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLLFRFDSSANPFFTNDILCKTYFYQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQRNKTTKQVRTIEKITPIESFFNFFDPPKIQNEDQDEELEEDLEERLALDYSIGEQLKDKLIPRAVDWFTGAALEFEFEEDEEEADEDEDEEEDDDHGLEDDDGESAEEQDDFAGRPEQAPECKQS [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=P25293 [UniProt boundaries chain A-2]=70-370 [UniProt coverage chain A-2]=72% [Name chain A-2]=Nucleosome assembly protein [UniProt sequence chain A-2]=MSDPIRTKPKSSMQIDNAPTPHNTPASVLNPSYLKNGNPVRAQAQEQDDKIGTINEEDILANQPLLLQSIQDRLGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKEFQVEMFELENKFLQKYKPIWEQRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEKAQNDSEEEQVKGIPSFWLTALENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLLFRFDSSANPFFTNDILCKTYFYQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQRNKTTKQVRTIEKITPIESFFNFFDPPKIQNEDQDEELEEDLEERLALDYSIGEQLKDKLIPRAVDWFTGAALEFEFEEDEEEADEDEDEEEDDDHGLEDDDGESAEEQDDFAGRPEQAPECKQS [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=3.00 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000275 [Entry] [Entry number]=466 [Entry name]=Nucleosome assembly protein 1 (NAP-1) [PDB ID]=2z2r [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Nucleosome assembly protein (NAP) [Sequence domain]=Nucleosome assembly protein (NAP) [Evidence level]=Indirect evidence [Evidence text]=A long α-helix is responsible for homodimerization via a previously uncharacterized antiparallel non-coiled-coil, and an alpha/beta domain is implicated in protein-protein interaction (PMID:16432217). The protein is dimer in solution (gel-filtration and glutaraldehyde cross-linking). The CD spectra revealed abundance of random coils in both PfNAPS and PfNAPL (30 and 45%, respectively) suggesting inherent flexibility in these proteins (PMID:15899528). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000275,MF7000276,MF7000273,MF7000274 [UniProt ID chain A]=P25293 [UniProt boundaries chain A]=82-365 [UniProt coverage chain A]=68% [Name chain A]=Nucleosome assembly protein [UniProt sequence chain A]=MSDPIRTKPKSSMQIDNAPTPHNTPASVLNPSYLKNGNPVRAQAQEQDDKIGTINEEDILANQPLLLQSIQDRLGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKEFQVEMFELENKFLQKYKPIWEQRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEKAQNDSEEEQVKGIPSFWLTALENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLLFRFDSSANPFFTNDILCKTYFYQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQRNKTTKQVRTIEKITPIESFFNFFDPPKIQNEDQDEELEEDLEERLALDYSIGEQLKDKLIPRAVDWFTGAALEFEFEEDEEEADEDEDEEEDDDHGLEDDDGESAEEQDDFAGRPEQAPECKQS [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P25293 [UniProt boundaries chain B]=83-365 [UniProt coverage chain B]=67% [Name chain B]=Nucleosome assembly protein [UniProt sequence chain B]=MSDPIRTKPKSSMQIDNAPTPHNTPASVLNPSYLKNGNPVRAQAQEQDDKIGTINEEDILANQPLLLQSIQDRLGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKEFQVEMFELENKFLQKYKPIWEQRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEKAQNDSEEEQVKGIPSFWLTALENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLLFRFDSSANPFFTNDILCKTYFYQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQRNKTTKQVRTIEKITPIESFFNFFDPPKIQNEDQDEELEEDLEERLALDYSIGEQLKDKLIPRAVDWFTGAALEFEFEEDEEEADEDEDEEEDDDHGLEDDDGESAEEQDDFAGRPEQAPECKQS [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=3.20 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000276 [Entry] [Entry number]=467 [Entry name]=Mycoplasma arthritidis-derived mitogen [PDB ID]=3kph [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=C-terminal helical dimerization subdomain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Intimately intertwined dimer, resulting in a highly twisted knot. Monomer structure in the apo form does not represent a stable fold (PMID:20417218). The entire C-terminal domains of these MAM molecules are involved in the domain swapping (PMID:20417218). Only the C-terminal subdomain mediates dimerization through MSF, the N-terminal domain is an independently folding unit. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q48898 [UniProt boundaries chain A]=42-237 [UniProt coverage chain A]=82% [Name chain A]=Superantigen [UniProt sequence chain A]=MKTKKLLIATVTLATGLLGILPLTSMKLRVENPKKAQKHFVQNLNNVVFTNKELEDIYNLSNKEETKEVLKLFKLKVNQFYRHAFGIVNDYNGLLEYKEIFNMMFLKLSVVFDTQRKEANNVEQIKRNIAILDEIMAKADNDLSYFISQNKNFQELWDKAVKLTKEMKIKLKGQKLDLRDGEVAINKVRELFGSDKNVKELWWFRSLLVKGVYLIKRYYEGDIELKTTSDFAKAVFED [Source organism chain A]=Metamycoplasma arthritidis [UniProt ID chain B]=Q48898 [UniProt boundaries chain B]=44-237 [UniProt coverage chain B]=81% [Name chain B]=Superantigen [UniProt sequence chain B]=MKTKKLLIATVTLATGLLGILPLTSMKLRVENPKKAQKHFVQNLNNVVFTNKELEDIYNLSNKEETKEVLKLFKLKVNQFYRHAFGIVNDYNGLLEYKEIFNMMFLKLSVVFDTQRKEANNVEQIKRNIAILDEIMAKADNDLSYFISQNKNFQELWDKAVKLTKEMKIKLKGQKLDLRDGEVAINKVRELFGSDKNVKELWWFRSLLVKGVYLIKRYYEGDIELKTTSDFAKAVFED [Source organism chain B]=Metamycoplasma arthritidis [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Metamycoplasma arthritidis [Accession]=MF7000277 [Entry] [Entry number]=468 [Entry name]=Beta-carbonic anhydrase CafC (wild type) [PDB ID]=6jqc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Carbonic anhydrase [Evidence level]=Indirect evidence [Evidence text]=The native carbonic anhydrase is dimeric in solution, in agreement with being a tightly associated dimer with a large, hydrophobic buried surface area. The extended β-sheet core consisting of ten β–strands is equally contributed by the two monomers, and the N-terminal helix of each monomer extends around the other monomer. Based on the highly intertwined structure, the monomeric form is most probably not a stable, independently folding unit. The two active sites are also located in clefts at the dimeric interface, further suggesting that dimer is the functional form (PMID:32515610). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000278,MF7000279,MF7000856,MF7000857,MF7000858,MF7000859 [UniProt ID chain A]=Q4WPJ0 [UniProt boundaries chain A]=1-164 [UniProt coverage chain A]=99% [Name chain A]=Carbonic anhydrase [UniProt sequence chain A]=MTNVADIEAANAQYAAAFTKGHLPLPPKRKLAVVTCMDARIDVFSVLGLTEGDAHVIRNAGGRASEALRSLIISQRLLGTEEVVVIHHTDCGMLTFSDEDIRAKIREELGEDASDIKFLPFRDLEASVREDVRFLRGSRLVQGNVTGYVYEVERGRLVRLDVSDI [Source organism chain A]=Af293) [UniProt ID chain B]=Q4WPJ0 [UniProt boundaries chain B]=1-164 [UniProt coverage chain B]=99% [Name chain B]=Carbonic anhydrase [UniProt sequence chain B]=MTNVADIEAANAQYAAAFTKGHLPLPPKRKLAVVTCMDARIDVFSVLGLTEGDAHVIRNAGGRASEALRSLIISQRLLGTEEVVVIHHTDCGMLTFSDEDIRAKIREELGEDASDIKFLPFRDLEASVREDVRFLRGSRLVQGNVTGYVYEVERGRLVRLDVSDI [Source organism chain B]=Af293) [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Af293) [Accession]=MF7000278 [Entry] [Entry number]=469 [Entry name]=Beta-carbonic anhydrase CafC (L25G and L78G mutant) [PDB ID]=6jqd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Carbonic anhydrase [Evidence level]=Indirect evidence [Evidence text]=The native carbonic anhydrase is dimeric in solution, in agreement with being a tightly associated dimer with a large, hydrophobic buried surface area. The extended β-sheet core consisting of ten β–strands is equally contributed by the two monomers, and the N-terminal helix of each monomer extends around the other monomer. Based on the highly intertwined structure, the monomeric form is most probably not a stable, independently folding unit. The two active sites are also located in clefts at the dimeric interface, further suggesting that dimer is the functional form (PMID:32515610). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000278,MF7000279,MF7000856,MF7000857,MF7000858,MF7000859 [UniProt ID chain A]=Q4WPJ0 [UniProt boundaries chain A]=1-164 [UniProt coverage chain A]=99% [Name chain A]=Carbonic anhydrase [UniProt sequence chain A]=MTNVADIEAANAQYAAAFTKGHLPLPPKRKLAVVTCMDARIDVFSVLGLTEGDAHVIRNAGGRASEALRSLIISQRLLGTEEVVVIHHTDCGMLTFSDEDIRAKIREELGEDASDIKFLPFRDLEASVREDVRFLRGSRLVQGNVTGYVYEVERGRLVRLDVSDI [Source organism chain A]=Af293) [UniProt ID chain B]=Q4WPJ0 [UniProt boundaries chain B]=1-164 [UniProt coverage chain B]=99% [Name chain B]=Carbonic anhydrase [UniProt sequence chain B]=MTNVADIEAANAQYAAAFTKGHLPLPPKRKLAVVTCMDARIDVFSVLGLTEGDAHVIRNAGGRASEALRSLIISQRLLGTEEVVVIHHTDCGMLTFSDEDIRAKIREELGEDASDIKFLPFRDLEASVREDVRFLRGSRLVQGNVTGYVYEVERGRLVRLDVSDI [Source organism chain B]=Af293) [ExpTech]=X-ray [Resolution]=1.69 [Source organism]=Af293) [Accession]=MF7000279 [Entry] [Entry number]=470 [Entry name]=Pur-α (Borrelia burgdorferi) [PDB ID]=3n8b [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=PUR domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Strongly intertwined dimer. Two PUR repeates are required to form a folded PUR domain (PMID:20976240). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O51076 [UniProt boundaries chain A]=3-77 [UniProt coverage chain A]=61% [Name chain A]=Transcriptional/translational repressor BpuR [UniProt sequence chain A]=MGERGEVYSEKLFTESERTYFFNVKENRKGDYFLNIVESKRSPSGDFERHSIFVYEENINEFESNLLKAIAVIKQKVSTGSVGSSARHNKGYGEYGERSKLDDSRFDKKSHLSGGRFKKKDY [Source organism chain A]= [UniProt ID chain B]=O51076 [UniProt boundaries chain B]=6-79 [UniProt coverage chain B]=60% [Name chain B]=Transcriptional/translational repressor BpuR [UniProt sequence chain B]=MGERGEVYSEKLFTESERTYFFNVKENRKGDYFLNIVESKRSPSGDFERHSIFVYEENINEFESNLLKAIAVIKQKVSTGSVGSSARHNKGYGEYGERSKLDDSRFDKKSHLSGGRFKKKDY [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.90 [Source organism]= [Accession]=MF7000280 [Entry] [Entry number]=471 [Entry name]=RNA polymerase II cofactor PC4 [PDB ID]=4bg7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=PC4-like fold [Sequence domain]=Transcriptional Coactivator p15 (PC4) [Evidence level]=Direct evidence [Evidence text]=In PC4 fold dimers there is beta sheet augmentation as well as coiled coil formation by helices from the two different monomers. The interface is quite large and there are many inter-chain hydrogen bonds and salt bridges, most of them are formed by conserved residues (PMID:22948907, PMID:24029071). The guanidine hydrochloride induced unfolding of PC4 (monitored using fluorescence) was best fitted to a two-state model (PMID:34534740). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000282,MF7000281,MF7000915,MF7000353 [UniProt ID chain A]=Q6QGH2 [UniProt boundaries chain A]=3-100 [UniProt coverage chain A]=96% [Name chain A]=Transcriptional coactivator p15 (PC4) C-terminal domain-containing protein [UniProt sequence chain A]=MSEQVNQNYEGHVDDQSIILWEKEGEQVRLTVSEFRGNLYMGIRYWLLDINDEWFPTKSGFSFPYTLETTSQLFYAFTQILSESEVLHEVQKRAEELKAKNA [Source organism chain A]=Escherichia phage T5 [UniProt ID chain B]=Q6QGH2 [UniProt boundaries chain B]=13-100 [UniProt coverage chain B]=86% [Name chain B]=Transcriptional coactivator p15 (PC4) C-terminal domain-containing protein [UniProt sequence chain B]=MSEQVNQNYEGHVDDQSIILWEKEGEQVRLTVSEFRGNLYMGIRYWLLDINDEWFPTKSGFSFPYTLETTSQLFYAFTQILSESEVLHEVQKRAEELKAKNA [Source organism chain B]=Escherichia phage T5 [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Escherichia phage T5 [Accession]=MF7000281 [Entry] [Entry number]=472 [Entry name]=MoSub1 (Magnaporthe oryzae) [PDB ID]=4agh [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=PC4-like fold [Sequence domain]=Transcriptional Coactivator p15 (PC4) [Evidence level]=Direct evidence [Evidence text]=In PC4 fold dimers there is beta sheet augmentation as well as coiled coil formation by helices from the two different monomers. The interface is quite large and there are many inter-chain hydrogen bonds and salt bridges, most of them are formed by conserved residues (PMID:22948907, PMID:24029071). The guanidine hydrochloride induced unfolding of PC4 (monitored using fluorescence) was best fitted to a two-state model (PMID:34534740). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000282,MF7000281,MF7000915,MF7000353 [UniProt ID chain A]=G4NEJ8 [UniProt boundaries chain A]=42-121 [UniProt coverage chain A]=49% [Name chain A]=Transcriptional coactivator p15 (PC4) C-terminal domain-containing protein [UniProt sequence chain A]=MAPKMTSKKRARDEEAQSGGSEAETKPAPVKKAKSKASNPGGSQVDAEGNPFWEISDKRRVGISQFKKMDFINIREYYEAGGEMKPGKKGIGLTVDQYTAFLKAIPAINAELRSRGHDITDDSDGGGAPVVAKPEGNAKKSTKKQEKKANIEATSDEGSGSD [Source organism chain A]=fungus) [UniProt ID chain A-2]=G4NEJ8 [UniProt boundaries chain A-2]=42-121 [UniProt coverage chain A-2]=49% [Name chain A-2]=Transcriptional coactivator p15 (PC4) C-terminal domain-containing protein [UniProt sequence chain A-2]=MAPKMTSKKRARDEEAQSGGSEAETKPAPVKKAKSKASNPGGSQVDAEGNPFWEISDKRRVGISQFKKMDFINIREYYEAGGEMKPGKKGIGLTVDQYTAFLKAIPAINAELRSRGHDITDDSDGGGAPVVAKPEGNAKKSTKKQEKKANIEATSDEGSGSD [Source organism chain A-2]=fungus) [ExpTech]=X-ray [Resolution]=1.79 [Source organism]=fungus) [Accession]=MF7000282 [Entry] [Entry number]=473 [Entry name]=Mouse BST-2/Tetherin Ectodomain [PDB ID]=3ni0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Bone marrow stromal antigen 2 [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:21084286). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000193,MF7000283 [UniProt ID chain A]=Q8R2Q8 [UniProt boundaries chain A]=57-151 [UniProt coverage chain A]=55% [Name chain A]=Bone marrow stromal antigen 2 [UniProt sequence chain A]=MAPSFYHYLPVPMDEMGGKQGWGSHRQWLGAAILVVLFGVTLVILTIYFAVTANSVACRDGLRAQAECRNTTHLLQRQLTRTQDSLLQAETQANSCNLTVVTLQESLEKKVSQALEQQARIKELENEVTKLNQELENLRIQKETSSTVQVNSGSSMVVSSLLVLKVSLFLLF [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q8R2Q8 [UniProt boundaries chain B]=58-144 [UniProt coverage chain B]=50% [Name chain B]=Bone marrow stromal antigen 2 [UniProt sequence chain B]=MAPSFYHYLPVPMDEMGGKQGWGSHRQWLGAAILVVLFGVTLVILTIYFAVTANSVACRDGLRAQAECRNTTHLLQRQLTRTQDSLLQAETQANSCNLTVVTLQESLEKKVSQALEQQARIKELENEVTKLNQELENLRIQKETSSTVQVNSGSSMVVSSLLVLKVSLFLLF [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Mus musculus [Accession]=MF7000283 [Entry] [Entry number]=474 [Entry name]=Putative NTP pyrophosphohydrolase [PDB ID]=3nl9 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Phosphoribosyl-ATP pyrophosphohydrolase [Evidence level]=Direct evidence [Evidence text]=Phosphoribosyl-ATP pyrophosphohydrolases show a very unusual interlaced segment-swapped dimer, which implies that this obligatory dimer assembly is important for their function. Size-exclusion chromatography combined with static light scattering confirmed that the dimer is the major oligomeric state in solution (PMID:20944217). Upon dimer formation, DR2231 helices 2 and 3 from one monomer stack antiparallel to helices 2′ and 3′ of the other monomer, respectively. A stable four-helix bundle is formed in the center. The intertwining of the two hairpin structures produces an extensive subunit-subunit interface (PMID:21733847). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000284,MF7000232,MF7000233 [UniProt ID chain A]=B1YMF4 [UniProt boundaries chain A]=2-170 [UniProt coverage chain A]=99% [Name chain A]=HAD family hydrolase [UniProt sequence chain A]=MKQPNYYQDVKQFHQTFHHPGADQPTAIPLDRGVKRATWTAEEAVVEFLHQSSQNETEFLAAIETFKAGLDQAVKKSLKETYPVTEVERLVGQGDALTDALYFIMGSFVEAGLEPGPLFEIVQQANMAKLGPDGQPIFRESDQKVMKPDGWLPPEPQLEAEVVRQMKEKA [Source organism chain A]=13490 / 255-15) [UniProt ID chain A-2]=B1YMF4 [UniProt boundaries chain A-2]=2-170 [UniProt coverage chain A-2]=99% [Name chain A-2]=HAD family hydrolase [UniProt sequence chain A-2]=MKQPNYYQDVKQFHQTFHHPGADQPTAIPLDRGVKRATWTAEEAVVEFLHQSSQNETEFLAAIETFKAGLDQAVKKSLKETYPVTEVERLVGQGDALTDALYFIMGSFVEAGLEPGPLFEIVQQANMAKLGPDGQPIFRESDQKVMKPDGWLPPEPQLEAEVVRQMKEKA [Source organism chain A-2]=13490 / 255-15) [ExpTech]=X-ray [Resolution]=1.78 [Source organism]=13490 / 255-15) [Accession]=MF7000284 [Entry] [Entry number]=475 [Entry name]=Oligomerization domain of H-NS [PDB ID]=1lr1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=H-NS histone-like proteins, N-terminal domain [Sequence domain]=H-NS histone-like proteins, N-terminal domain [Evidence level]=Direct evidence [Evidence text]=The intertwined H-NS dimerization domain defines a new structural fold, combining coiled coil interactions and domain swapping (PMID:12592399). The dimer is formed on the basis of the antiparallel coiled coil structure. The N-terminal oligomerization domain (residues 1-89) constitute the basic building block of the protein scaffold that binds DNA via the C-terminal domain (PMID:12460581). The dimeric form was detected in solution (sedimentation equilibrium and crosslinking experiments) (PMID:12592399). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000285,MF7000287,MF7000288,MF7000286 [UniProt ID chain A]=P0ACF8 [UniProt boundaries chain A]=2-58 [UniProt coverage chain A]=41% [Name chain A]=DNA-binding protein H-NS [UniProt sequence chain A]=MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSLAAVKSGTKAKRAQRPAKYSYVDENGETKTWTGQGRTPAVIKKAMDEQGKSLDDFLIKQ [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0ACF8 [UniProt boundaries chain B]=2-58 [UniProt coverage chain B]=41% [Name chain B]=DNA-binding protein H-NS [UniProt sequence chain B]=MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSLAAVKSGTKAKRAQRPAKYSYVDENGETKTWTGQGRTPAVIKKAMDEQGKSLDDFLIKQ [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF7000285 [Entry] [Entry number]=476 [Entry name]=N-terminal of H-NS dimer [PDB ID]=3nr7 [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=H-NS histone-like proteins, N-terminal domain [Sequence domain]=H-NS histone-like proteins, N-terminal domain [Evidence level]=Direct evidence [Evidence text]=The intertwined H-NS dimerization domain defines a new structural fold, combining coiled coil interactions and domain swapping (PMID:12592399). The dimer is formed on the basis of the antiparallel coiled coil structure. The N-terminal oligomerization domain (residues 1-89) constitute the basic building block of the protein scaffold that binds DNA via the C-terminal domain (PMID:12460581). The dimeric form was detected in solution (sedimentation equilibrium and crosslinking experiments) (PMID:12592399). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=MF7000285,MF7000287,MF7000288,MF7000286 [UniProt ID chain A]=P0A1S2 [UniProt boundaries chain A]=2-82 [UniProt coverage chain A]=59% [Name chain A]=DNA-binding protein H-NS [UniProt sequence chain A]=MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSMAAAKSGTKAKRAARPAKYSYVDENGETKTWTGQGRTPAVIKKAMEEQGKQLEDFLIKE [Source organism chain A]=Salmonella typhimurium [UniProt ID chain B-2]=P0A1S2 [UniProt boundaries chain B-2]=2-82 [UniProt coverage chain B-2]=59% [Name chain B-2]=DNA-binding protein H-NS [UniProt sequence chain B-2]=MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSMAAAKSGTKAKRAARPAKYSYVDENGETKTWTGQGRTPAVIKKAMEEQGKQLEDFLIKE [Source organism chain B-2]=Salmonella typhimurium [ExpTech]=X-ray [Resolution]=3.70 [Source organism]=Salmonella typhimurium [Accession]=MF7000286 [Entry] [Entry number]=477 [Entry name]=Dimerization motif of H-NS [PDB ID]=1ni8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=H-NS histone-like proteins, N-terminal domain [Sequence domain]=H-NS histone-like proteins, N-terminal domain [Evidence level]=Direct evidence [Evidence text]=The intertwined H-NS dimerization domain defines a new structural fold, combining coiled coil interactions and domain swapping (PMID:12592399). The dimer is formed on the basis of the antiparallel coiled coil structure. The N-terminal oligomerization domain (residues 1-89) constitute the basic building block of the protein scaffold that binds DNA via the C-terminal domain (PMID:12460581). The dimeric form was detected in solution (sedimentation equilibrium and crosslinking experiments) (PMID:12592399). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000285,MF7000287,MF7000288,MF7000286 [UniProt ID chain A]=P0ACF8 [UniProt boundaries chain A]=2-47 [UniProt coverage chain A]=33% [Name chain A]=DNA-binding protein H-NS [UniProt sequence chain A]=MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSLAAVKSGTKAKRAQRPAKYSYVDENGETKTWTGQGRTPAVIKKAMDEQGKSLDDFLIKQ [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0ACF8 [UniProt boundaries chain B]=2-47 [UniProt coverage chain B]=33% [Name chain B]=DNA-binding protein H-NS [UniProt sequence chain B]=MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSLAAVKSGTKAKRAQRPAKYSYVDENGETKTWTGQGRTPAVIKKAMDEQGKSLDDFLIKQ [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF7000287 [Entry] [Entry number]=478 [Entry name]=N-terminal dimerization domain of VicH [PDB ID]=1ov9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=H-NS histone-like proteins, N-terminal domain [Sequence domain]=H-NS histone-like proteins, N-terminal domain [Evidence level]=Direct evidence [Evidence text]=The intertwined H-NS dimerization domain defines a new structural fold, combining coiled coil interactions and domain swapping (PMID:12592399). The dimer is formed on the basis of the antiparallel coiled coil structure. The N-terminal oligomerization domain (residues 1-89) constitute the basic building block of the protein scaffold that binds DNA via the C-terminal domain (PMID:12460581). The dimeric form was detected in solution (sedimentation equilibrium and crosslinking experiments) (PMID:12592399). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000285,MF7000287,MF7000288,MF7000286 [UniProt ID chain A]=Q9KSX6 [UniProt boundaries chain A]=5-49 [UniProt coverage chain A]=32% [Name chain A]=DNA-binding protein [UniProt sequence chain A]=MVMSEITKTLLNIRSLRAYARELTIEQLEEALDKLTTVVQERKEAEAEEIAARAEQEAKLAAIAEQIAKDGIDLEALISALSGETKTKAKGKRAPRPAKYKYIDTNGEEKTWTGQGRTPSVIQKALDEGKSLEEFAL [Source organism chain A]=Vibrio cholerae serotype O1 [UniProt ID chain B]=Q9KSX6 [UniProt boundaries chain B]=5-52 [UniProt coverage chain B]=35% [Name chain B]=DNA-binding protein [UniProt sequence chain B]=MVMSEITKTLLNIRSLRAYARELTIEQLEEALDKLTTVVQERKEAEAEEIAARAEQEAKLAAIAEQIAKDGIDLEALISALSGETKTKAKGKRAPRPAKYKYIDTNGEEKTWTGQGRTPSVIQKALDEGKSLEEFAL [Source organism chain B]=Vibrio cholerae serotype O1 [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Vibrio cholerae serotype O1 [Accession]=MF7000288 [Entry] [Entry number]=481 [Entry name]=Actin nucleation cofactor Bud6 (yeast) [PDB ID]=3okq [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Actin interacting protein 3 [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:23161908). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000291,MF7000292 [UniProt ID chain A]=P41697 [UniProt boundaries chain A]=553-677 [UniProt coverage chain A]=15% [Name chain A]=Bud site selection protein 6 [UniProt sequence chain A]=MKMAVDDPTYGTPKIKRTASSSSSIETTVTKLLMSTKHLLQVLTQWSKGTTSGRLVSDAYVQLGNDFKVVSKFFMHAKVDMSDVGDVPMALRRVLEVTLREPPSDETLNKHLPKIREIIVTLLDKLKVKQAILKNMQQEHRISVKSHHQQNPSFTSNLSLGSEGTREGTPLSSRKSSIVRDQRQSDSVENSYGEKVNSTSTGTPSAQSAEATLTKPRTNIKQNLKSNNAPNASDDDDALSQLKKGTNLQRRASKRYSAYHMAKLTNQSTTEAAAAAGLMTTPSPSMLHLEETVRKSKLYGNNNNDDDRNINSAENKGKSIDDVSKASPLAKTPLPIENVRASPRRLSSVVTTSPDKAMNGTCPVFLRIGDKTKKCHVQLPTTKNALRLLFIERFAYSPGANSFPDIYIMDPQYGVFYELEELNLLDIKEGFVIELKLEENPNNTIKEFIDTVKMEISNSQNDIIRHLKEMSFGSAISGKQTEVLPQPGLEANKHDLVGQNKKDDDKTIKDIQYELGKIKQVHNINRSNINETIFNILRKVDNFKSLSFSAKNSSNRMYMEKSQTELGDLSDTLLSKVDDLQDVIEIMRKDVAERRSQPAKKKLETVSKDLENAQADVLKLQEFIDTEKPHWKKTWEAELDKVCEEQQFLTLQEELILDLKEDLGKALETFDLIKLCCEEQEKNPSRSKSNPILPIMRPGTFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMERKLKASNEFDDELENFVGNSNLKKSGGFEEVERIRKQKDEANLRAYFGPGFT [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=P41697 [UniProt boundaries chain A-2]=553-677 [UniProt coverage chain A-2]=15% [Name chain A-2]=Bud site selection protein 6 [UniProt sequence chain A-2]=MKMAVDDPTYGTPKIKRTASSSSSIETTVTKLLMSTKHLLQVLTQWSKGTTSGRLVSDAYVQLGNDFKVVSKFFMHAKVDMSDVGDVPMALRRVLEVTLREPPSDETLNKHLPKIREIIVTLLDKLKVKQAILKNMQQEHRISVKSHHQQNPSFTSNLSLGSEGTREGTPLSSRKSSIVRDQRQSDSVENSYGEKVNSTSTGTPSAQSAEATLTKPRTNIKQNLKSNNAPNASDDDDALSQLKKGTNLQRRASKRYSAYHMAKLTNQSTTEAAAAAGLMTTPSPSMLHLEETVRKSKLYGNNNNDDDRNINSAENKGKSIDDVSKASPLAKTPLPIENVRASPRRLSSVVTTSPDKAMNGTCPVFLRIGDKTKKCHVQLPTTKNALRLLFIERFAYSPGANSFPDIYIMDPQYGVFYELEELNLLDIKEGFVIELKLEENPNNTIKEFIDTVKMEISNSQNDIIRHLKEMSFGSAISGKQTEVLPQPGLEANKHDLVGQNKKDDDKTIKDIQYELGKIKQVHNINRSNINETIFNILRKVDNFKSLSFSAKNSSNRMYMEKSQTELGDLSDTLLSKVDDLQDVIEIMRKDVAERRSQPAKKKLETVSKDLENAQADVLKLQEFIDTEKPHWKKTWEAELDKVCEEQQFLTLQEELILDLKEDLGKALETFDLIKLCCEEQEKNPSRSKSNPILPIMRPGTFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMERKLKASNEFDDELENFVGNSNLKKSGGFEEVERIRKQKDEANLRAYFGPGFT [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.04 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000291 [Entry] [Entry number]=482 [Entry name]=Actin nucleation cofactor Bud6 (yeast) [PDB ID]=3onx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Actin interacting protein 3 [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:23161908). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000291,MF7000292 [UniProt ID chain A]=P41697 [UniProt boundaries chain A]=555-679 [UniProt coverage chain A]=15% [Name chain A]=Bud site selection protein 6 [UniProt sequence chain A]=MKMAVDDPTYGTPKIKRTASSSSSIETTVTKLLMSTKHLLQVLTQWSKGTTSGRLVSDAYVQLGNDFKVVSKFFMHAKVDMSDVGDVPMALRRVLEVTLREPPSDETLNKHLPKIREIIVTLLDKLKVKQAILKNMQQEHRISVKSHHQQNPSFTSNLSLGSEGTREGTPLSSRKSSIVRDQRQSDSVENSYGEKVNSTSTGTPSAQSAEATLTKPRTNIKQNLKSNNAPNASDDDDALSQLKKGTNLQRRASKRYSAYHMAKLTNQSTTEAAAAAGLMTTPSPSMLHLEETVRKSKLYGNNNNDDDRNINSAENKGKSIDDVSKASPLAKTPLPIENVRASPRRLSSVVTTSPDKAMNGTCPVFLRIGDKTKKCHVQLPTTKNALRLLFIERFAYSPGANSFPDIYIMDPQYGVFYELEELNLLDIKEGFVIELKLEENPNNTIKEFIDTVKMEISNSQNDIIRHLKEMSFGSAISGKQTEVLPQPGLEANKHDLVGQNKKDDDKTIKDIQYELGKIKQVHNINRSNINETIFNILRKVDNFKSLSFSAKNSSNRMYMEKSQTELGDLSDTLLSKVDDLQDVIEIMRKDVAERRSQPAKKKLETVSKDLENAQADVLKLQEFIDTEKPHWKKTWEAELDKVCEEQQFLTLQEELILDLKEDLGKALETFDLIKLCCEEQEKNPSRSKSNPILPIMRPGTFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMERKLKASNEFDDELENFVGNSNLKKSGGFEEVERIRKQKDEANLRAYFGPGFT [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P41697 [UniProt boundaries chain B]=555-679 [UniProt coverage chain B]=15% [Name chain B]=Bud site selection protein 6 [UniProt sequence chain B]=MKMAVDDPTYGTPKIKRTASSSSSIETTVTKLLMSTKHLLQVLTQWSKGTTSGRLVSDAYVQLGNDFKVVSKFFMHAKVDMSDVGDVPMALRRVLEVTLREPPSDETLNKHLPKIREIIVTLLDKLKVKQAILKNMQQEHRISVKSHHQQNPSFTSNLSLGSEGTREGTPLSSRKSSIVRDQRQSDSVENSYGEKVNSTSTGTPSAQSAEATLTKPRTNIKQNLKSNNAPNASDDDDALSQLKKGTNLQRRASKRYSAYHMAKLTNQSTTEAAAAAGLMTTPSPSMLHLEETVRKSKLYGNNNNDDDRNINSAENKGKSIDDVSKASPLAKTPLPIENVRASPRRLSSVVTTSPDKAMNGTCPVFLRIGDKTKKCHVQLPTTKNALRLLFIERFAYSPGANSFPDIYIMDPQYGVFYELEELNLLDIKEGFVIELKLEENPNNTIKEFIDTVKMEISNSQNDIIRHLKEMSFGSAISGKQTEVLPQPGLEANKHDLVGQNKKDDDKTIKDIQYELGKIKQVHNINRSNINETIFNILRKVDNFKSLSFSAKNSSNRMYMEKSQTELGDLSDTLLSKVDDLQDVIEIMRKDVAERRSQPAKKKLETVSKDLENAQADVLKLQEFIDTEKPHWKKTWEAELDKVCEEQQFLTLQEELILDLKEDLGKALETFDLIKLCCEEQEKNPSRSKSNPILPIMRPGTFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMERKLKASNEFDDELENFVGNSNLKKSGGFEEVERIRKQKDEANLRAYFGPGFT [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.90 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000292 [Entry] [Entry number]=483 [Entry name]=Spot14 [PDB ID]=3ont [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The S14 monomer is composed of three antiparallel α-helices. Helix 3 is longer, it allows it to interact with an adjacent monomer. Thereby, an antiparallel 4-helix bundle is created by packing the C terminus of helix 3 against the main body of the other monomer. There is an extensive dimer interface. A fraction of the residues are disordered in the monomer (DisProt:DP02820). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP02820 covers 100% of the sequence present in the structure [Evidence chain A-2]=The region(s) described in DP02820 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=Q62264 [UniProt boundaries chain A]=8-149 [UniProt coverage chain A]=94% [Name chain A]=Thyroid hormone-inducible hepatic protein [UniProt sequence chain A]=MQVLTKRYPKNCLLTVMDRYSAVVRNMEQVVMIPSLLRDVQLSGPGGSVQDGAPDLYTYFTMLKSICVEVDHGLLPREEWQAKVAGNETSEAENDAAETEEAEEDRISEELDLEAQFHLHFCSLHHILTHLTRKAQEVTRKYQEMTGQVL [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=Q62264 [UniProt boundaries chain A-2]=8-149 [UniProt coverage chain A-2]=94% [Name chain A-2]=Thyroid hormone-inducible hepatic protein [UniProt sequence chain A-2]=MQVLTKRYPKNCLLTVMDRYSAVVRNMEQVVMIPSLLRDVQLSGPGGSVQDGAPDLYTYFTMLKSICVEVDHGLLPREEWQAKVAGNETSEAENDAAETEEAEEDRISEELDLEAQFHLHFCSLHHILTHLTRKAQEVTRKYQEMTGQVL [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=2.65 [Source organism]=Mus musculus [Accession]=MF7000293 [Entry] [Entry number]=484 [Entry name]=Coiled coil domain of SAS-6 (C. elegans) [PDB ID]=4gkw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:23064147). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O62479 [UniProt boundaries chain A]=250-407 [UniProt coverage chain A]=32% [Name chain A]=Spindle assembly abnormal protein 6 [UniProt sequence chain A]=MTSKIALFDQTLIASLLQPLSLNQPDFKAYKTKVKLKISEQRNETSGEKELKFEISRSDDFEFLFSETLNNEKYQILARDHDLTVDFDAFPKVIIQHLLCKNIVKNLEEDGEVDARKKAGYHSIADPGKPTEINIILDAEKNFCSFELFSKTPISKGKIFSIKLHAVRGDHLISHLLKICSSQAVKLSTFYKSADELASLRQKCGDLEKQVEKLSGVKEEFEEMSEKFKELEDEVELVKEERENIRLLVEDKEDEVADLKQDTESLQKQLEENQEELEIVGNMLREEQGKVDQLQKRNVAHQKEIGKLRAELGTAQRNLEKADQLLKRNSQQQNQQSLDMRKLGELEADLKEKDSMVESLTETIGILRKELENEKLKAAENMDSFEKLSMENENLKEKIAHYRAQRFSPAPSGLPGLQTGLTNRLTPSFKPVLGPHTPYGANLNSRTPFRDNTTLNFQNSTIATPHAFRFNSQLIADETTGSSVTNTPPAQR [Source organism chain A]=Caenorhabditis elegans [UniProt ID chain B]=O62479 [UniProt boundaries chain B]=250-407 [UniProt coverage chain B]=32% [Name chain B]=Spindle assembly abnormal protein 6 [UniProt sequence chain B]=MTSKIALFDQTLIASLLQPLSLNQPDFKAYKTKVKLKISEQRNETSGEKELKFEISRSDDFEFLFSETLNNEKYQILARDHDLTVDFDAFPKVIIQHLLCKNIVKNLEEDGEVDARKKAGYHSIADPGKPTEINIILDAEKNFCSFELFSKTPISKGKIFSIKLHAVRGDHLISHLLKICSSQAVKLSTFYKSADELASLRQKCGDLEKQVEKLSGVKEEFEEMSEKFKELEDEVELVKEERENIRLLVEDKEDEVADLKQDTESLQKQLEENQEELEIVGNMLREEQGKVDQLQKRNVAHQKEIGKLRAELGTAQRNLEKADQLLKRNSQQQNQQSLDMRKLGELEADLKEKDSMVESLTETIGILRKELENEKLKAAENMDSFEKLSMENENLKEKIAHYRAQRFSPAPSGLPGLQTGLTNRLTPSFKPVLGPHTPYGANLNSRTPFRDNTTLNFQNSTIATPHAFRFNSQLIADETTGSSVTNTPPAQR [Source organism chain B]=Caenorhabditis elegans [ExpTech]=X-ray [Resolution]=3.30 [Source organism]=Caenorhabditis elegans [Accession]=MF7000294 [Entry] [Entry number]=485 [Entry name]=Coiled coil domain of Beclin 1 [PDB ID]=3q8t [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:22314358). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q91XJ1 [UniProt boundaries chain A]=174-264 [UniProt coverage chain A]=20% [Name chain A]=Beclin-1 [UniProt sequence chain A]=MEGSKASSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGESQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEMLEQMNEGDSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSAPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=Q91XJ1 [UniProt boundaries chain B]=174-264 [UniProt coverage chain B]=20% [Name chain B]=Beclin-1 [UniProt sequence chain B]=MEGSKASSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGESQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEMLEQMNEGDSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSAPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK [Source organism chain B]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Rattus norvegicus [Accession]=MF7000295 [Entry] [Entry number]=486 [Entry name]=HTH-type transcriptional regulator SkgA [PDB ID]=7cla [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=At least a subpart of the sructure, helices 6 and 7 are disordered in isolation based on earlier publications. The longest helix, H5 forms a coiled coil between the two monomers (PMID:33454020). Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P0CAV4 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=54% [Name chain A]=HTH-type transcriptional regulator SkgA [UniProt sequence chain A]=MSVYTVKQMARLSGVSVRALHHYDAIGLLKPRAVGANGYRYYDRQDLLRLQQILFHRALETPLKDIQAALDQPGFDLAAALRAQRERLAAQAERYARLVDVVDRTLADLEGDETMDDKHLFEGFDPEKQARHEAWLVEHYGDEATRRIADAKAGMKSWGKKDWSQFQEEAKAIEHDLAKALTQGLPVDSAPVTAIMRRHWAWVGRSWNREPTPDAFAGLGHLYQANPEFTARYEAIAPGLTEYFSEAMRAFARGR [Source organism chain A]= [UniProt ID chain A-2]=P0CAV4 [UniProt boundaries chain A-2]=1-138 [UniProt coverage chain A-2]=54% [Name chain A-2]=HTH-type transcriptional regulator SkgA [UniProt sequence chain A-2]=MSVYTVKQMARLSGVSVRALHHYDAIGLLKPRAVGANGYRYYDRQDLLRLQQILFHRALETPLKDIQAALDQPGFDLAAALRAQRERLAAQAERYARLVDVVDRTLADLEGDETMDDKHLFEGFDPEKQARHEAWLVEHYGDEATRRIADAKAGMKSWGKKDWSQFQEEAKAIEHDLAKALTQGLPVDSAPVTAIMRRHWAWVGRSWNREPTPDAFAGLGHLYQANPEFTARYEAIAPGLTEYFSEAMRAFARGR [Source organism chain A-2]= [ExpTech]=X-ray [Resolution]=2.50 [Source organism]= [Accession]=MF7000296 [Entry] [Entry number]=487 [Entry name]=Coiled coil dimerization domain of intracellular MLA immune receptors [PDB ID]=3qfl [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:21402358). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q8GSK4 [UniProt boundaries chain A]=7-120 [UniProt coverage chain A]=11% [Name chain A]=CC-NBS-LRR resistance protein MLA13 [UniProt sequence chain A]=MDIVTGAISNLIPKLGELLTEEFKLHKGVKKNIEDLGKELESMNAALIKIGEVPREQLDSQDKLWADEVRELSYVIEDVVDKFLVQVDGIKSDDNNNKFKGLMKRTTELLKKVKHKHGIAHAIKDIQEQLQKVADRRDRNKVFVPHPTRTIAIDPCLRALYAEATELVGIYGKRDQGLMRLLSMEGDDASNKRLKKVSIVGFGGLGKTTLARAVYEKIKGDFDCRAFVPVGQNPDMKKVLRDILIDLGNPHSDLAMLDANQLIKKLHEFLENKRYLVIIDDIWDEKLWEGINFAFSNRNNLGSRLITTTRIVSVSNSCCSSDGDSVYQMEPLSVDDSRMLFYKRIFPDENACINEFEQVSRDILKKCGGVPLAIITIASALAGDQKMKPKCEWDILLRSLGSGLTEDNSLEEMRRILSFSYSNLPSNLKTCLLYLCVYPEDSMISRDKLIWKWVAEGFVHHENQGNSLYLLGLNYFNQLINRSMIQPIYNYSGEAYACRVHDMVLDLICNLSNEAKFVNLLDGTGNSMSSQSNCRRLSLQKRNEDHQARPFTDIKSMSRVRSITIFPSAIEVMPSLSRFDVLRVLDLSRCNLGENSSMQLNLKGVGHLTHLRYLGLEGTNISKLPAEIGKLQFLEVLDLENNHNLKELPSTVCNFRRLIYLNLVGCQVVPPVGVLQNLTSIEVLSGILVSLNIIAQELGNLKRLRELNILFNDGSLDLYEGFVKSLCNLHHIESLIIGCNSRETSSFELMDLLGERWVPPVHFREFVSSMPSQLSALRGWIKRDPSHLSNLSELILTSVKEVQQDDVVIIGALSSLRRLCIKSTYQTQRLLVIPADGFRCIVGFHLDCGSATQILFEPGALPRAESVVISLGVRVAKEDGNRGFDLGLQGNLLSLRRDVFVSIYCGGARVGEAKEAEAAVRRALDAHPSHPPIYFEMRPHIAKGAHDDDLCEERRRTDF [Source organism chain A]=Hordeum vulgare [UniProt ID chain A-2]=Q8GSK4 [UniProt boundaries chain A-2]=7-120 [UniProt coverage chain A-2]=11% [Name chain A-2]=CC-NBS-LRR resistance protein MLA13 [UniProt sequence chain A-2]=MDIVTGAISNLIPKLGELLTEEFKLHKGVKKNIEDLGKELESMNAALIKIGEVPREQLDSQDKLWADEVRELSYVIEDVVDKFLVQVDGIKSDDNNNKFKGLMKRTTELLKKVKHKHGIAHAIKDIQEQLQKVADRRDRNKVFVPHPTRTIAIDPCLRALYAEATELVGIYGKRDQGLMRLLSMEGDDASNKRLKKVSIVGFGGLGKTTLARAVYEKIKGDFDCRAFVPVGQNPDMKKVLRDILIDLGNPHSDLAMLDANQLIKKLHEFLENKRYLVIIDDIWDEKLWEGINFAFSNRNNLGSRLITTTRIVSVSNSCCSSDGDSVYQMEPLSVDDSRMLFYKRIFPDENACINEFEQVSRDILKKCGGVPLAIITIASALAGDQKMKPKCEWDILLRSLGSGLTEDNSLEEMRRILSFSYSNLPSNLKTCLLYLCVYPEDSMISRDKLIWKWVAEGFVHHENQGNSLYLLGLNYFNQLINRSMIQPIYNYSGEAYACRVHDMVLDLICNLSNEAKFVNLLDGTGNSMSSQSNCRRLSLQKRNEDHQARPFTDIKSMSRVRSITIFPSAIEVMPSLSRFDVLRVLDLSRCNLGENSSMQLNLKGVGHLTHLRYLGLEGTNISKLPAEIGKLQFLEVLDLENNHNLKELPSTVCNFRRLIYLNLVGCQVVPPVGVLQNLTSIEVLSGILVSLNIIAQELGNLKRLRELNILFNDGSLDLYEGFVKSLCNLHHIESLIIGCNSRETSSFELMDLLGERWVPPVHFREFVSSMPSQLSALRGWIKRDPSHLSNLSELILTSVKEVQQDDVVIIGALSSLRRLCIKSTYQTQRLLVIPADGFRCIVGFHLDCGSATQILFEPGALPRAESVVISLGVRVAKEDGNRGFDLGLQGNLLSLRRDVFVSIYCGGARVGEAKEAEAAVRRALDAHPSHPPIYFEMRPHIAKGAHDDDLCEERRRTDF [Source organism chain A-2]=Hordeum vulgare [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Hordeum vulgare [Accession]=MF7000297 [Entry] [Entry number]=488 [Entry name]=Liprin-beta2 [PDB ID]=3qh9 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:21462929). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q8ND30 [UniProt boundaries chain A]=198-263 [UniProt coverage chain A]=7% [Name chain A]=Liprin-beta-2 [UniProt sequence chain A]=MASDASHALEAALEQMDGIIAGTKTGADLSDGTCEPGLASPASYMNPFPVLHLIEDLRLALEMLELPQERAALLSQIPGPTAAYIKEWFEESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPEGGFSKWNATNKDPEELFKQEMPPRCSSPTVGPPPLPQKSLETRAQKKLSCSLEDLRSESVDKCMDGNQPFPVLEPKDSPFLAEHKYPTLPGKLSGATPNGEAAKSPPTICQPDATGSSLLRLRDTESGWDDTAVVNDLSSTSSGTESGPQSPLTPDGKRNPKGIKKFWGKIRRTQSGNFYTDTLGMAEFRRGGLRATAGPRLSRTRDSKGQKSDANAPFAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAINTKQEEKSALLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLHVNKFNPHCLHRRPADESNLSPSEVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALIGPEAEQEKREKMASPAYTPLTTTAKVRPRKLGFSHFGNIRKKKFDESTDYICPMEPSDGVSDSHRVYSGYRGLSPLDAPELDGLDQVGQIS [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q8ND30 [UniProt boundaries chain A-2]=198-263 [UniProt coverage chain A-2]=7% [Name chain A-2]=Liprin-beta-2 [UniProt sequence chain A-2]=MASDASHALEAALEQMDGIIAGTKTGADLSDGTCEPGLASPASYMNPFPVLHLIEDLRLALEMLELPQERAALLSQIPGPTAAYIKEWFEESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPEGGFSKWNATNKDPEELFKQEMPPRCSSPTVGPPPLPQKSLETRAQKKLSCSLEDLRSESVDKCMDGNQPFPVLEPKDSPFLAEHKYPTLPGKLSGATPNGEAAKSPPTICQPDATGSSLLRLRDTESGWDDTAVVNDLSSTSSGTESGPQSPLTPDGKRNPKGIKKFWGKIRRTQSGNFYTDTLGMAEFRRGGLRATAGPRLSRTRDSKGQKSDANAPFAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAINTKQEEKSALLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLHVNKFNPHCLHRRPADESNLSPSEVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALIGPEAEQEKREKMASPAYTPLTTTAKVRPRKLGFSHFGNIRKKKFDESTDYICPMEPSDGVSDSHRVYSGYRGLSPLDAPELDGLDQVGQIS [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.01 [Source organism]=Homo sapiens [Accession]=MF7000298 [Entry] [Entry number]=490 [Entry name]=SD2 domain (Drosophila Shroom) [PDB ID]=3thf [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:22493320). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=A1Z9P3 [UniProt boundaries chain A]=1396-1570 [UniProt coverage chain A]=11% [Name chain A]=Protein Shroom [UniProt sequence chain A]=MKMRNHKENGNGSEMGESTKSLAKMEPENNNKISVVSVSKLLLKDSNGANSRSSNSNASFSSASVAGSVQDDLPHHNSSSSQLGQQHGSSLDQCGLTQAGLEEYNNRSSSYYDQTAFHHQKQPSYAQSEGYHSYVSSSDSTSATPFLDKLRQESDLLSRQSHHWSENDLSSVCSNSVAPSPIPLLARQSHSHSHSHAHSHSNSHGHSHGHAHSASSSSSSNNNSNGSATNNNNNNSSESTSSTETLKWLGSMSDISEASHATGYSAISESVSSSQRIVHSSRVPTPKRHHSESVLYLHNNEEQGDSSPTASNSSQMMISEEANGEESPPSVQPLRIQHRHSPSYPPVHTSMVLHHFQQQQQQQQDYQHPSRHHTNQSTLSTQSSLLELASPTEKPRSLMGQSHSMGDLQQKNPHQNPMLGRSAGQQHKSSISVTISSSEAVVTIAPQPPAGKPSKLQLSLGKSEALSCSTPNMGEQSPTNSIDSYRSNHRLFPVSTYTEPVHSNTSQYVQHPKPQFSSGLHKSAKLPVITPAGATVQPTWHSVAERINDFERSQLGEPPKFAYLEPTKTHRLSNPALKALQKNAVQSYVERQQQQQKEEQQLLRPHSQSYQACHVERKSLPNNLSPIMVGLPTGSNSASTRDCSSPTPPPPPRRSGSLLPNLLRRSSSASDYAEFRELHQAQGQVKGPSIRNISNAEKISFNDCGMPPPPPPPRGRLAVPTRRTSSATEYAPMRDKLLLQQAAALAHQQHHPQQHRHAQPPHVPPERPPKHPNLRVPSPELPPPPQSELDISYTFDEPLPPPPPPEVLQPRPPPSPNRRNCFAGASTRRTTYEAPPPTAIVAAKVPPLVPKKPTSLQHKHLANGGGGSRKRPHHATPQPILENVASPVAPPPPLLPRARSTAHDNVIASNLESNQQKRSNSKASYLPRQSLEKLNNTDPDHGIYKLTLTSNEDLVAHTKPSYGVTGKLPNNLPDVLPLGVKLHQQPKLQPGSPNGDANVTLRYGSNNNLTGNSPTVAPPPYYGGGQRYSTPVLGQGYGKSSKPVTPQQYTRSQSYDVKHTSAVTMPTMSQSHVDLKQAAHDLETTLEEVLPTATPTPTPTPTPTPPRLSPASSHSDCSLSTSSLECTINPIATPIPKPEAHIFRAEVISTTLNTNPLTTPPKPAMNRQESLRENIEKITQLQSVLMSAHLCDASLLGGYTTPLITSPTASFANEPLMTPPLPPSPPPPLEPEEEEEQEENDVHDKQPEIEELQLMQRSELVLMVNPKPSTTDMACQTDELEDRDTDLEAAREEHQTRTTLQPRQRQPIELDYEQMSRELVKLLPPGDKIADILTPKICKPTSQYVSNLYNPDVPLRLAKRDVGTSTLMRMKSITSSAEIRVVSVELQLAEPSEEPTNLIKQKMDELIKHLNQKIVSLKREQQTISEECSANDRLGQDLFAKLAEKVRPSEASKFRTHVDAVGNITSLLLSLSERLAQTESSLETRQQERGALESKRDLLYEQMEEAQRLKSDIERRGVSIAGLLAKNLSADMCADYDYFINMKAKLIADARDLAVRIKGSEEQLSSLSDALVQSDC [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=A1Z9P3 [UniProt boundaries chain B]=1397-1570 [UniProt coverage chain B]=11% [Name chain B]=Protein Shroom [UniProt sequence chain B]=MKMRNHKENGNGSEMGESTKSLAKMEPENNNKISVVSVSKLLLKDSNGANSRSSNSNASFSSASVAGSVQDDLPHHNSSSSQLGQQHGSSLDQCGLTQAGLEEYNNRSSSYYDQTAFHHQKQPSYAQSEGYHSYVSSSDSTSATPFLDKLRQESDLLSRQSHHWSENDLSSVCSNSVAPSPIPLLARQSHSHSHSHAHSHSNSHGHSHGHAHSASSSSSSNNNSNGSATNNNNNNSSESTSSTETLKWLGSMSDISEASHATGYSAISESVSSSQRIVHSSRVPTPKRHHSESVLYLHNNEEQGDSSPTASNSSQMMISEEANGEESPPSVQPLRIQHRHSPSYPPVHTSMVLHHFQQQQQQQQDYQHPSRHHTNQSTLSTQSSLLELASPTEKPRSLMGQSHSMGDLQQKNPHQNPMLGRSAGQQHKSSISVTISSSEAVVTIAPQPPAGKPSKLQLSLGKSEALSCSTPNMGEQSPTNSIDSYRSNHRLFPVSTYTEPVHSNTSQYVQHPKPQFSSGLHKSAKLPVITPAGATVQPTWHSVAERINDFERSQLGEPPKFAYLEPTKTHRLSNPALKALQKNAVQSYVERQQQQQKEEQQLLRPHSQSYQACHVERKSLPNNLSPIMVGLPTGSNSASTRDCSSPTPPPPPRRSGSLLPNLLRRSSSASDYAEFRELHQAQGQVKGPSIRNISNAEKISFNDCGMPPPPPPPRGRLAVPTRRTSSATEYAPMRDKLLLQQAAALAHQQHHPQQHRHAQPPHVPPERPPKHPNLRVPSPELPPPPQSELDISYTFDEPLPPPPPPEVLQPRPPPSPNRRNCFAGASTRRTTYEAPPPTAIVAAKVPPLVPKKPTSLQHKHLANGGGGSRKRPHHATPQPILENVASPVAPPPPLLPRARSTAHDNVIASNLESNQQKRSNSKASYLPRQSLEKLNNTDPDHGIYKLTLTSNEDLVAHTKPSYGVTGKLPNNLPDVLPLGVKLHQQPKLQPGSPNGDANVTLRYGSNNNLTGNSPTVAPPPYYGGGQRYSTPVLGQGYGKSSKPVTPQQYTRSQSYDVKHTSAVTMPTMSQSHVDLKQAAHDLETTLEEVLPTATPTPTPTPTPTPPRLSPASSHSDCSLSTSSLECTINPIATPIPKPEAHIFRAEVISTTLNTNPLTTPPKPAMNRQESLRENIEKITQLQSVLMSAHLCDASLLGGYTTPLITSPTASFANEPLMTPPLPPSPPPPLEPEEEEEQEENDVHDKQPEIEELQLMQRSELVLMVNPKPSTTDMACQTDELEDRDTDLEAAREEHQTRTTLQPRQRQPIELDYEQMSRELVKLLPPGDKIADILTPKICKPTSQYVSNLYNPDVPLRLAKRDVGTSTLMRMKSITSSAEIRVVSVELQLAEPSEEPTNLIKQKMDELIKHLNQKIVSLKREQQTISEECSANDRLGQDLFAKLAEKVRPSEASKFRTHVDAVGNITSLLLSLSERLAQTESSLETRQQERGALESKRDLLYEQMEEAQRLKSDIERRGVSIAGLLAKNLSADMCADYDYFINMKAKLIADARDLAVRIKGSEEQLSSLSDALVQSDC [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Drosophila melanogaster [Accession]=MF7000300 [Entry] [Entry number]=491 [Entry name]=FosB/JunD bZIP domain [PDB ID]=5vpa [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=bZIP transcription factor [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:28981703). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110006,MF2110009,MF7000301,MF7000302,MF7000303 [UniProt ID chain A]=P53539 [UniProt boundaries chain A]=164-217 [UniProt coverage chain A]=15% [Name chain A]=Protein FosB [UniProt sequence chain A]=MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPVVDPYDMPGTSYSTPGMSGYSSGGASGSGGPSTSGTTSGPGPARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSAPAKEDGFSWLLPPPPPPPLPFQTSQDAPPNLTASLFTHSEVQVLGDPFPVVNPSYTSSFVLTCPEVSAFAGAQRTSGSDQPSDPLNSPSLLAL [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P17535 [UniProt boundaries chain B]=275-332 [UniProt coverage chain B]=16% [Name chain B]=Transcription factor JunD [UniProt sequence chain B]=METPFYGDEALSGLGGGASGSGGSFASPGRLFPGAPPTAAAGSMMKKDALTLSLSEQVAAALKPAAAPPPTPLRADGAPSAAPPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSSQFLYPKVAASEEQEFAEGFVKALEDLHKQNQLGAGAAAAAAAAAAGGPSGTATGSAPPGELAPAAAAPEAPVYANLSSYAGGAGGAGGAATVAFAAEPVPFPPPPPPGALGPPRLAALKDEPQTVPDVPSFGESPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQKVLSHVNSGCQLLPQHQVPAY [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.83 [Source organism]=Homo sapiens [Accession]=MF7000301 [Entry] [Entry number]=492 [Entry name]=FosB/JunD bZIP domain [PDB ID]=7ucc [Chains]=J,F [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=bZIP transcription factor [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:36039764). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain F]=N/A [Evidence chain J]=N/A [Similar structures]=MF2110006,MF2110009,MF7000301,MF7000302,MF7000303 [UniProt ID chain F]=P53539 [UniProt boundaries chain F]=154-217 [UniProt coverage chain F]=18% [Name chain F]=Protein FosB [UniProt sequence chain F]=MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPVVDPYDMPGTSYSTPGMSGYSSGGASGSGGPSTSGTTSGPGPARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSAPAKEDGFSWLLPPPPPPPLPFQTSQDAPPNLTASLFTHSEVQVLGDPFPVVNPSYTSSFVLTCPEVSAFAGAQRTSGSDQPSDPLNSPSLLAL [Source organism chain F]=Homo sapiens [UniProt ID chain J]=P17535 [UniProt boundaries chain J]=266-332 [UniProt coverage chain J]=19% [Name chain J]=Transcription factor JunD [UniProt sequence chain J]=METPFYGDEALSGLGGGASGSGGSFASPGRLFPGAPPTAAAGSMMKKDALTLSLSEQVAAALKPAAAPPPTPLRADGAPSAAPPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSSQFLYPKVAASEEQEFAEGFVKALEDLHKQNQLGAGAAAAAAAAAAGGPSGTATGSAPPGELAPAAAAPEAPVYANLSSYAGGAGGAGGAATVAFAAEPVPFPPPPPPGALGPPRLAALKDEPQTVPDVPSFGESPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQKVLSHVNSGCQLLPQHQVPAY [Source organism chain J]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.94 [Source organism]=Homo sapiens [Accession]=MF7000302 [Entry] [Entry number]=493 [Entry name]=FosB/JunD bZIP domain (modified) [PDB ID]=7ucd [Chains]=J,F [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=bZIP transcription factor [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:36039764). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain F]=N/A [Evidence chain J]=N/A [Similar structures]=MF2110006,MF2110009,MF7000301,MF7000302,MF7000303 [UniProt ID chain F]=P53539 [UniProt boundaries chain F]=154-217 [UniProt coverage chain F]=18% [Name chain F]=Protein FosB [UniProt sequence chain F]=MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPVVDPYDMPGTSYSTPGMSGYSSGGASGSGGPSTSGTTSGPGPARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSAPAKEDGFSWLLPPPPPPPLPFQTSQDAPPNLTASLFTHSEVQVLGDPFPVVNPSYTSSFVLTCPEVSAFAGAQRTSGSDQPSDPLNSPSLLAL [Source organism chain F]=Homo sapiens [UniProt ID chain J]=P17535 [UniProt boundaries chain J]=266-332 [UniProt coverage chain J]=19% [Name chain J]=Transcription factor JunD [UniProt sequence chain J]=METPFYGDEALSGLGGGASGSGGSFASPGRLFPGAPPTAAAGSMMKKDALTLSLSEQVAAALKPAAAPPPTPLRADGAPSAAPPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSSQFLYPKVAASEEQEFAEGFVKALEDLHKQNQLGAGAAAAAAAAAAGGPSGTATGSAPPGELAPAAAAPEAPVYANLSSYAGGAGGAGGAATVAFAAEPVPFPPPPPPGALGPPRLAALKDEPQTVPDVPSFGESPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQKVLSHVNSGCQLLPQHQVPAY [Source organism chain J]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.21 [Source organism]=Homo sapiens [Accession]=MF7000303 [Entry] [Entry number]=494 [Entry name]=HGbRL's Globin Domain [PDB ID]=3wfw [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Globin [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The dimer structure is highly intertwined, a domain swapped dimer, with helices from the different subunits being stabilized by helices from the other subunit. Loop EF is straightened into part of the α-helical conformation, and the elongated helices from both subunits form an antiparallel pair. Instead of being sandwiched between helices E and F from a single globin subunit, a haem group in N-HGbRL is sandwiched by two subunits. A single N-HGbRL globin fold, denoted subunit A*, is therefore made up of helices A–E from one subunit and helices F–H from the other. In other words, both the proximal and distal sites of a single globin fold are constituted mainly by two separate subunits, representing the first ever site-swapping example in the globin family (PMID:26094577). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000304,MF7000305 [UniProt ID chain A]=B3DUZ1 [UniProt boundaries chain A]=1-133 [UniProt coverage chain A]=48% [Name chain A]=Hemoglobin-like flavoprotein fused to Roadblock/LC7 domain [UniProt sequence chain A]=MTREEIKMIQKSWLRVIDKMDEAGLLFYRRLFDVEPKVRPLFKIDIEKQGRKLMDVLNWIVLNLQDIDAALDAARELARRHVKYGVKAEHYPVVGHTLIWTLRKMIGSEWTKQLEQLWTQAYEALAQVMIEEHKKIQSFEYLIRYLEQELSEVINSVIAAFPEIVGIAISTTQGATVSRCSSESYSNIIGSVVSSTLGHAQRLCEAAAAGRLEEIKITGSMLHLYIRQAGSDAAIGVLYPSQTAEGIISLLIRSAALKIQSLLSSFRLKEVNPG [Source organism chain A]=V4)) [UniProt ID chain A-2]=B3DUZ1 [UniProt boundaries chain A-2]=1-133 [UniProt coverage chain A-2]=48% [Name chain A-2]=Hemoglobin-like flavoprotein fused to Roadblock/LC7 domain [UniProt sequence chain A-2]=MTREEIKMIQKSWLRVIDKMDEAGLLFYRRLFDVEPKVRPLFKIDIEKQGRKLMDVLNWIVLNLQDIDAALDAARELARRHVKYGVKAEHYPVVGHTLIWTLRKMIGSEWTKQLEQLWTQAYEALAQVMIEEHKKIQSFEYLIRYLEQELSEVINSVIAAFPEIVGIAISTTQGATVSRCSSESYSNIIGSVVSSTLGHAQRLCEAAAAGRLEEIKITGSMLHLYIRQAGSDAAIGVLYPSQTAEGIISLLIRSAALKIQSLLSSFRLKEVNPG [Source organism chain A-2]=V4)) [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=V4)) [Accession]=MF7000304 [Entry] [Entry number]=495 [Entry name]=HGbRL's Globin Domain with Imidazole [PDB ID]=3wfx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Globin [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disorder of the monomeric forms. The dimer structure is highly intertwined, a domain swapped dimer, with helices from the different subunits being stabilized by helices from the other subunit. Loop EF is straightened into part of the α-helical conformation, and the elongated helices from both subunits form an antiparallel pair. Instead of being sandwiched between helices E and F from a single globin subunit, a haem group in N-HGbRL is sandwiched by two subunits. A single N-HGbRL globin fold, denoted subunit A*, is therefore made up of helices A–E from one subunit and helices F–H from the other. In other words, both the proximal and distal sites of a single globin fold are constituted mainly by two separate subunits, representing the first ever site-swapping example in the globin family (PMID:26094577). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000304,MF7000305 [UniProt ID chain A]=B3DUZ1 [UniProt boundaries chain A]=1-133 [UniProt coverage chain A]=48% [Name chain A]=Hemoglobin-like flavoprotein fused to Roadblock/LC7 domain [UniProt sequence chain A]=MTREEIKMIQKSWLRVIDKMDEAGLLFYRRLFDVEPKVRPLFKIDIEKQGRKLMDVLNWIVLNLQDIDAALDAARELARRHVKYGVKAEHYPVVGHTLIWTLRKMIGSEWTKQLEQLWTQAYEALAQVMIEEHKKIQSFEYLIRYLEQELSEVINSVIAAFPEIVGIAISTTQGATVSRCSSESYSNIIGSVVSSTLGHAQRLCEAAAAGRLEEIKITGSMLHLYIRQAGSDAAIGVLYPSQTAEGIISLLIRSAALKIQSLLSSFRLKEVNPG [Source organism chain A]=V4)) [UniProt ID chain B]=B3DUZ1 [UniProt boundaries chain B]=1-133 [UniProt coverage chain B]=48% [Name chain B]=Hemoglobin-like flavoprotein fused to Roadblock/LC7 domain [UniProt sequence chain B]=MTREEIKMIQKSWLRVIDKMDEAGLLFYRRLFDVEPKVRPLFKIDIEKQGRKLMDVLNWIVLNLQDIDAALDAARELARRHVKYGVKAEHYPVVGHTLIWTLRKMIGSEWTKQLEQLWTQAYEALAQVMIEEHKKIQSFEYLIRYLEQELSEVINSVIAAFPEIVGIAISTTQGATVSRCSSESYSNIIGSVVSSTLGHAQRLCEAAAAGRLEEIKITGSMLHLYIRQAGSDAAIGVLYPSQTAEGIISLLIRSAALKIQSLLSSFRLKEVNPG [Source organism chain B]=V4)) [ExpTech]=X-ray [Resolution]=1.94 [Source organism]=V4)) [Accession]=MF7000305 [Entry] [Entry number]=496 [Entry name]=Hikeshi (receptor of Hsp70) (F97A mutant) [PDB ID]=3wvz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Hikeshi-like [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability of the monomeric forms. However, the dimeric state was confirmed by SEC and claimed to be the functional unit of the protein. The hydrophobic core provided a dimer interface, resulting in stabilization of the rigid dimer arrangement. The driving force for dimerization via the CTD was attributed to the exclusion of solvent via multiple hydrophobic contacts within two pairs of antiparallel helices, comprised of 2 and 4 from each monomer (PMID:25760597). Additionally, the turn– 3–turn– 9 segment (residues 156–173) connecting helices 2 and 4 of each monomer showed a domain crossover and was intimately intertwined (PMID:25760597). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000306,MF7000307 [UniProt ID chain A]=Q53FT3 [UniProt boundaries chain A]=1-195 [UniProt coverage chain A]=98% [Name chain A]=Protein Hikeshi [UniProt sequence chain A]=MFGCLVAGRLVQTAAQQVAEDKFVFDLPDYESINHVVVFMLGTIPFPEGMGGSVYFSYPDSNGMPVWQLLGFVTNGKPSAIFKISGLKSGEGSQHPFGAMNIVRTPSVAQIGISVELLDSMAQQTPVGNAAVSSVDSFTQFTQKMLDNFYNFASSFAVSQAQMTPSPSEMFIPANVVLKWYENFQRRLAQNPLFWKT [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q53FT3 [UniProt boundaries chain B]=1-196 [UniProt coverage chain B]=99% [Name chain B]=Protein Hikeshi [UniProt sequence chain B]=MFGCLVAGRLVQTAAQQVAEDKFVFDLPDYESINHVVVFMLGTIPFPEGMGGSVYFSYPDSNGMPVWQLLGFVTNGKPSAIFKISGLKSGEGSQHPFGAMNIVRTPSVAQIGISVELLDSMAQQTPVGNAAVSSVDSFTQFTQKMLDNFYNFASSFAVSQAQMTPSPSEMFIPANVVLKWYENFQRRLAQNPLFWKT [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.88 [Source organism]=Homo sapiens [Accession]=MF7000306 [Entry] [Entry number]=497 [Entry name]=Hikeshi (receptor of Hsp70) [PDB ID]=3ww0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Hikeshi-like [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability of the monomeric forms. However, the dimeric state was confirmed by SEC and claimed to be the functional unit of the protein. The hydrophobic core provided a dimer interface, resulting in stabilization of the rigid dimer arrangement. The driving force for dimerization via the CTD was attributed to the exclusion of solvent via multiple hydrophobic contacts within two pairs of antiparallel helices, comprised of 2 and 4 from each monomer (PMID:25760597). Additionally, the turn– 3–turn– 9 segment (residues 156–173) connecting helices 2 and 4 of each monomer showed a domain crossover and was intimately intertwined (PMID:25760597). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000306,MF7000307 [UniProt ID chain A]=Q53FT3 [UniProt boundaries chain A]=1-197 [UniProt coverage chain A]=100% [Name chain A]=Protein Hikeshi [UniProt sequence chain A]=MFGCLVAGRLVQTAAQQVAEDKFVFDLPDYESINHVVVFMLGTIPFPEGMGGSVYFSYPDSNGMPVWQLLGFVTNGKPSAIFKISGLKSGEGSQHPFGAMNIVRTPSVAQIGISVELLDSMAQQTPVGNAAVSSVDSFTQFTQKMLDNFYNFASSFAVSQAQMTPSPSEMFIPANVVLKWYENFQRRLAQNPLFWKT [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q53FT3 [UniProt boundaries chain B]=1-196 [UniProt coverage chain B]=99% [Name chain B]=Protein Hikeshi [UniProt sequence chain B]=MFGCLVAGRLVQTAAQQVAEDKFVFDLPDYESINHVVVFMLGTIPFPEGMGGSVYFSYPDSNGMPVWQLLGFVTNGKPSAIFKISGLKSGEGSQHPFGAMNIVRTPSVAQIGISVELLDSMAQQTPVGNAAVSSVDSFTQFTQKMLDNFYNFASSFAVSQAQMTPSPSEMFIPANVVLKWYENFQRRLAQNPLFWKT [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Homo sapiens [Accession]=MF7000307 [Entry] [Entry number]=498 [Entry name]=Coiled coil domain of TRIM25 [PDB ID]=4ltb [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:24550273). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q14258 [UniProt boundaries chain A]=190-360 [UniProt coverage chain A]=27% [Name chain A]=E3 ubiquitin/ISG15 ligase TRIM25 [UniProt sequence chain A]=MAELCPLAEELSCSICLEPFKEPVTTPCGHNFCGSCLNETWAVQGSPYLCPQCRAVYQARPQLHKNTVLCNVVEQFLQADLAREPPADVWTPPARASAPSPNAQVACDHCLKEAAVKTCLVCMASFCQEHLQPHFDSPAFQDHPLQPPVRDLLRRKCSQHNRLREFFCPEHSECICHICLVEHKTCSPASLSQASADLEATLRHKLTVMYSQINGASRALDDVRNRQQDVRMTANRKVEQLQQEYTEMKALLDASETTSTRKIKEEEKRVNSKFDTIYQILLKKKSEIQTLKEEIEQSLTKRDEFEFLEKASKLRGISTKPVYIPEVELNHKLIKGIHQSTIDLKNELKQCIGRLQEPTPSSGDPGEHDPASTHKSTRPVKKVSKEEKKSKKPPPVPALPSKLPTFGAPEQLVDLKQAGLEAAAKATSSHPNSTSLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVASVAEMPQNYRPHPQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPESRLGRNSASWCVEWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLMYKFRVDFTEALYPAFWVFSAGATLSICSPK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q14258 [UniProt boundaries chain B]=190-360 [UniProt coverage chain B]=27% [Name chain B]=E3 ubiquitin/ISG15 ligase TRIM25 [UniProt sequence chain B]=MAELCPLAEELSCSICLEPFKEPVTTPCGHNFCGSCLNETWAVQGSPYLCPQCRAVYQARPQLHKNTVLCNVVEQFLQADLAREPPADVWTPPARASAPSPNAQVACDHCLKEAAVKTCLVCMASFCQEHLQPHFDSPAFQDHPLQPPVRDLLRRKCSQHNRLREFFCPEHSECICHICLVEHKTCSPASLSQASADLEATLRHKLTVMYSQINGASRALDDVRNRQQDVRMTANRKVEQLQQEYTEMKALLDASETTSTRKIKEEEKRVNSKFDTIYQILLKKKSEIQTLKEEIEQSLTKRDEFEFLEKASKLRGISTKPVYIPEVELNHKLIKGIHQSTIDLKNELKQCIGRLQEPTPSSGDPGEHDPASTHKSTRPVKKVSKEEKKSKKPPPVPALPSKLPTFGAPEQLVDLKQAGLEAAAKATSSHPNSTSLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVASVAEMPQNYRPHPQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPESRLGRNSASWCVEWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLMYKFRVDFTEALYPAFWVFSAGATLSICSPK [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.59 [Source organism]=Homo sapiens [Accession]=MF7000308 [Entry] [Entry number]=499 [Entry name]=Coiled coil 1 domain of actin-binding protein SCAB1 [PDB ID]=4djg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:22356912). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O48791 [UniProt boundaries chain A]=103-151 [UniProt coverage chain A]=9% [Name chain A]=Stomatal closure-related actin-binding protein 1 [UniProt sequence chain A]=MTRVTRDFRDSLQRDGVPAVSADVKFASSRFPNYRIGANDQIFDVKDDPKVMSMKEVVARETAQLMDQQKRLSVRDLAHKFEKGLAAAAKLSEEAKLKEATSLEKHVLLKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDEERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAEKSKHFLQLQKKLAMCRKSEENISLVYEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGSKKELISGATKSVYAPEPFDVGRVLHADIIYDGHSLSLSTVGKIDPAAGLGSYVEALVRKHDVDFNVVVTQMSGEDHTSESIHLFHVGKMRIKLCKGKTVIAKEYYSSAMQLCGVRGGGNAAAQALYWQAKKGVSFVIAFESERERNAAIMLARRFACDCNVTLAGPEDRTETGQSP [Source organism chain A]=Arabidopsis thaliana [UniProt ID chain B]=O48791 [UniProt boundaries chain B]=100-146 [UniProt coverage chain B]=9% [Name chain B]=Stomatal closure-related actin-binding protein 1 [UniProt sequence chain B]=MTRVTRDFRDSLQRDGVPAVSADVKFASSRFPNYRIGANDQIFDVKDDPKVMSMKEVVARETAQLMDQQKRLSVRDLAHKFEKGLAAAAKLSEEAKLKEATSLEKHVLLKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDEERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAEKSKHFLQLQKKLAMCRKSEENISLVYEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGSKKELISGATKSVYAPEPFDVGRVLHADIIYDGHSLSLSTVGKIDPAAGLGSYVEALVRKHDVDFNVVVTQMSGEDHTSESIHLFHVGKMRIKLCKGKTVIAKEYYSSAMQLCGVRGGGNAAAQALYWQAKKGVSFVIAFESERERNAAIMLARRFACDCNVTLAGPEDRTETGQSP [Source organism chain B]=Arabidopsis thaliana [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Arabidopsis thaliana [Accession]=MF7000309 [Entry] [Entry number]=500 [Entry name]=N-terminal of HU protein [PDB ID]=4dky [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=IHF-like DNA-binding domain [Sequence domain]=IHF-like DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding from dimers to unfolded monomers proved experimentally (PMID:15066175). High stability of the dimer (PMID:15063721). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000052,MF7000051,MF7000024,MF7000050,MF7000310,MF7000311,MF7000026,MF7000025 [UniProt ID chain A]=A5U6Z7 [UniProt boundaries chain A]=1-97 [UniProt coverage chain A]=45% [Name chain A]=DNA-binding protein HupB [UniProt sequence chain A]=MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVSGAQRLPAEGPAVKRGVGASAAKKVAKKAPAKKATKAAKKAATKAPARKAATKAPAKKAATKAPAKKAVKATKSPAKKVTKAVKKTAVKASVRKAATKAPAKKAAAKRPATKAPAKKATARRGRK [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=A5U6Z7 [UniProt boundaries chain A-2]=1-98 [UniProt coverage chain A-2]=45% [Name chain A-2]=DNA-binding protein HupB [UniProt sequence chain A-2]=MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVSGAQRLPAEGPAVKRGVGASAAKKVAKKAPAKKATKAAKKAATKAPARKAATKAPAKKAATKAPAKKAVKATKSPAKKVTKAVKKTAVKASVRKAATKAPAKKAAAKRPATKAPAKKATARRGRK [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.48 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000310 [Entry] [Entry number]=501 [Entry name]=N-terminal of HU protein [PDB ID]=4pt4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=IHF-like DNA-binding domain [Sequence domain]=IHF-like DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding from dimers to unfolded monomers proved experimentally (PMID:15066175). High stability of the dimer (PMID:15063721). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000052,MF7000051,MF7000024,MF7000050,MF7000310,MF7000311,MF7000026,MF7000025 [UniProt ID chain A]=A5U6Z7 [UniProt boundaries chain A]=1-99 [UniProt coverage chain A]=46% [Name chain A]=DNA-binding protein HupB [UniProt sequence chain A]=MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVSGAQRLPAEGPAVKRGVGASAAKKVAKKAPAKKATKAAKKAATKAPARKAATKAPAKKAATKAPAKKAVKATKSPAKKVTKAVKKTAVKASVRKAATKAPAKKAAAKRPATKAPAKKATARRGRK [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=A5U6Z7 [UniProt boundaries chain B]=1-97 [UniProt coverage chain B]=45% [Name chain B]=DNA-binding protein HupB [UniProt sequence chain B]=MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVSGAQRLPAEGPAVKRGVGASAAKKVAKKAPAKKATKAAKKAATKAPARKAATKAPAKKAATKAPAKKAVKATKSPAKKVTKAVKKTAVKASVRKAATKAPAKKAAAKRPATKAPAKKATARRGRK [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.04 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000311 [Entry] [Entry number]=502 [Entry name]=C-terminal of Mad1 [PDB ID]=4dzo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=N-terminal coiled coil dimerization subdomain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Mad1 CTD is a homodimer and contains a coiled coil stem and a globular head. The N-terminal segments of two αA helices (one from each monomer) form the stem. αC and the C-terminal end of αA mediate the dimerization of the globular head through coiled coil formation (PMID:22493223). Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9Y6D9 [UniProt boundaries chain A]=598-716 [UniProt coverage chain A]=16% [Name chain A]=Mitotic spindle assembly checkpoint protein MAD1 [UniProt sequence chain A]=MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9Y6D9 [UniProt boundaries chain B]=597-718 [UniProt coverage chain B]=16% [Name chain B]=Mitotic spindle assembly checkpoint protein MAD1 [UniProt sequence chain B]=MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.76 [Source organism]=Homo sapiens [Accession]=MF7000312 [Entry] [Entry number]=503 [Entry name]=PadR-like transcriptional regulator (Bacillus cereus ATCC 14579) [PDB ID]=4esb [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q818P3 [UniProt boundaries chain A]=3-105 [UniProt coverage chain A]=98% [Name chain A]=Transcriptional regulator, PadR family [UniProt sequence chain A]=MHSQMLKGVLEGCILYIISQEEVYGYELSTKLNKHGFTFVSEGSIYPLLLRMQKEKLIEGTLKASSLGPKRKYYHITDKGLEQLEEFKQSWGMVSTTVNNLLQGE [Source organism chain A]=15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) [UniProt ID chain A-2]=Q818P3 [UniProt boundaries chain A-2]=3-105 [UniProt coverage chain A-2]=98% [Name chain A-2]=Transcriptional regulator, PadR family [UniProt sequence chain A-2]=MHSQMLKGVLEGCILYIISQEEVYGYELSTKLNKHGFTFVSEGSIYPLLLRMQKEKLIEGTLKASSLGPKRKYYHITDKGLEQLEEFKQSWGMVSTTVNNLLQGE [Source organism chain A-2]=15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) [Accession]=MF7000313 [Entry] [Entry number]=504 [Entry name]=PadR-like transcriptional regulator (Listeria monocytogenes) [PDB ID]=7wjp [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=A0A1D2INR9 [UniProt boundaries chain A]=5-105 [UniProt coverage chain A]=91% [Name chain A]=PadR family transcriptional regulator [UniProt sequence chain A]=MEVNPQFKKGVLELCCLFLIQKKDCYGYELANQVSKYIEVAEGAIYPVLRRLVKEEYCSTYLVESNEGPSRKYYQLTVKGEIYLNELISEWNNFTDSVAKLLTEGEAVNE [Source organism chain A]=Listeria monocytogenes [UniProt ID chain A-2]=A0A1D2INR9 [UniProt boundaries chain A-2]=5-105 [UniProt coverage chain A-2]=91% [Name chain A-2]=PadR family transcriptional regulator [UniProt sequence chain A-2]=MEVNPQFKKGVLELCCLFLIQKKDCYGYELANQVSKYIEVAEGAIYPVLRRLVKEEYCSTYLVESNEGPSRKYYQLTVKGEIYLNELISEWNNFTDSVAKLLTEGEAVNE [Source organism chain A-2]=Listeria monocytogenes [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Listeria monocytogenes [Accession]=MF7000314 [Entry] [Entry number]=505 [Entry name]=PadR-like transcriptional regulator (Bacteroides fragilis NCTC 9343) [PDB ID]=5h20 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q5LC36 [UniProt boundaries chain A]=4-106 [UniProt coverage chain A]=92% [Name chain A]=PadR-family transcriptional regulatory protein [UniProt sequence chain A]=MNVDNVKSQMRKGMLEYCIMLLLHKEPAYASDIIQKLKEARLIVVEGTLYPLLTRLKNDDLLSYEWVESTQGPPRKYYKLTGKGESFLGELEASWKELNETVNHIANRESI [Source organism chain A]=/ LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2) [UniProt ID chain A-2]=Q5LC36 [UniProt boundaries chain A-2]=4-106 [UniProt coverage chain A-2]=92% [Name chain A-2]=PadR-family transcriptional regulatory protein [UniProt sequence chain A-2]=MNVDNVKSQMRKGMLEYCIMLLLHKEPAYASDIIQKLKEARLIVVEGTLYPLLTRLKNDDLLSYEWVESTQGPPRKYYKLTGKGESFLGELEASWKELNETVNHIANRESI [Source organism chain A-2]=/ LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2) [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=/ LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2) [Accession]=MF7000315 [Entry] [Entry number]=506 [Entry name]=PadR-family transcriptional regulator Rv3488 (Mycobacterium tuberculosis) [PDB ID]=5zhc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=I6X7F9 [UniProt boundaries chain A]=1-96 [UniProt coverage chain A]=89% [Name chain A]=Transcriptional regulator Rv3488 [UniProt sequence chain A]=MREFQRAAVRLHILHHAADNEVHGAWLTQELSRHGYRVSPGTLYPTLHRLEADGLLVSEQRVVDGRARRVYRATPAGRAALTEDRRALEELAREVLGGQSHTAGNGT [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=I6X7F9 [UniProt boundaries chain B]=1-96 [UniProt coverage chain B]=89% [Name chain B]=Transcriptional regulator Rv3488 [UniProt sequence chain B]=MREFQRAAVRLHILHHAADNEVHGAWLTQELSRHGYRVSPGTLYPTLHRLEADGLLVSEQRVVDGRARRVYRATPAGRAALTEDRRALEELAREVLGGQSHTAGNGT [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.97 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000316 [Entry] [Entry number]=507 [Entry name]=PadR-family transcriptional regulator Rv3488 (Mycobacterium tuberculosis) [PDB ID]=5zhv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=I6X7F9 [UniProt boundaries chain A]=1-96 [UniProt coverage chain A]=89% [Name chain A]=Transcriptional regulator Rv3488 [UniProt sequence chain A]=MREFQRAAVRLHILHHAADNEVHGAWLTQELSRHGYRVSPGTLYPTLHRLEADGLLVSEQRVVDGRARRVYRATPAGRAALTEDRRALEELAREVLGGQSHTAGNGT [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=I6X7F9 [UniProt boundaries chain B]=1-96 [UniProt coverage chain B]=89% [Name chain B]=Transcriptional regulator Rv3488 [UniProt sequence chain B]=MREFQRAAVRLHILHHAADNEVHGAWLTQELSRHGYRVSPGTLYPTLHRLEADGLLVSEQRVVDGRARRVYRATPAGRAALTEDRRALEELAREVLGGQSHTAGNGT [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000317 [Entry] [Entry number]=508 [Entry name]=PadR-family transcriptional regulator Rv3488 (Mycobacterium tuberculosis) [PDB ID]=5zi8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=I6X7F9 [UniProt boundaries chain A]=1-101 [UniProt coverage chain A]=94% [Name chain A]=Transcriptional regulator Rv3488 [UniProt sequence chain A]=MREFQRAAVRLHILHHAADNEVHGAWLTQELSRHGYRVSPGTLYPTLHRLEADGLLVSEQRVVDGRARRVYRATPAGRAALTEDRRALEELAREVLGGQSHTAGNGT [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=I6X7F9 [UniProt boundaries chain B]=1-99 [UniProt coverage chain B]=92% [Name chain B]=Transcriptional regulator Rv3488 [UniProt sequence chain B]=MREFQRAAVRLHILHHAADNEVHGAWLTQELSRHGYRVSPGTLYPTLHRLEADGLLVSEQRVVDGRARRVYRATPAGRAALTEDRRALEELAREVLGGQSHTAGNGT [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000318 [Entry] [Entry number]=509 [Entry name]=Ferric uptake regulator S1 [PDB ID]=6d57 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and dimerization domain [Sequence domain]=Ferric uptake regulator family [Evidence level]=Indirect evidence [Evidence text]=The protein assembles into a biological dimer in which each monomer has two domains, the DNA-binding domain and the dimerization domain, as other ferric uptake regulators (PMID:29739988). Dimeric in solution according to its FPLC profile (PMID:16925555). The dimerization domain is a strong candidate for MSF due to large interface and beta sheet augmentation between the monomers. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000830,MF7000831,MF7000832,MF7000833,MF7000834,MF7000320,MF7000319 [UniProt ID chain A]=A0A1E7PHN7 [UniProt boundaries chain A]=3-149 [UniProt coverage chain A]=93% [Name chain A]=Ferric uptake regulation protein [UniProt sequence chain A]=MLIENVEYDVLLERFKKILRQGGLKYTKQREVLLKTLYHSDTHYTPESLYMEIKQAEPDLNVGIATVYRTLNLLEEAEMVTSISFGSAGKKYELANKPHHDHMICKNCGKIIEFENPIIERQQALIAKEHGFKLTGHLMQLYGVCGDCNNQKAKVKI [Source organism chain A]=Campylobacter jejuni [UniProt ID chain B]=A0A1E7PHN7 [UniProt boundaries chain B]=1-154 [UniProt coverage chain B]=98% [Name chain B]=Ferric uptake regulation protein [UniProt sequence chain B]=MLIENVEYDVLLERFKKILRQGGLKYTKQREVLLKTLYHSDTHYTPESLYMEIKQAEPDLNVGIATVYRTLNLLEEAEMVTSISFGSAGKKYELANKPHHDHMICKNCGKIIEFENPIIERQQALIAKEHGFKLTGHLMQLYGVCGDCNNQKAKVKI [Source organism chain B]=Campylobacter jejuni [ExpTech]=X-ray [Resolution]=1.81 [Source organism]=Campylobacter jejuni [Accession]=MF7000319 [Entry] [Entry number]=510 [Entry name]=Ferric uptake regulator S1 [PDB ID]=4ets [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and dimerization domain [Sequence domain]=Ferric uptake regulator family [Evidence level]=Indirect evidence [Evidence text]=The protein assembles into a biological dimer in which each monomer has two domains, the DNA-binding domain and the dimerization domain, as other ferric uptake regulators (PMID:29739988). Dimeric in solution according to its FPLC profile (PMID:16925555). The dimerization domain is a strong candidate for MSF due to large interface and beta sheet augmentation between the monomers. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000830,MF7000831,MF7000832,MF7000833,MF7000834,MF7000320,MF7000319 [UniProt ID chain A]=P0C631 [UniProt boundaries chain A]=4-149 [UniProt coverage chain A]=92% [Name chain A]=Ferric uptake regulation protein [UniProt sequence chain A]=MLIENVEYDVLLERFKKILRQGGLKYTKQREVLLKTLYHSDTHYTPESLYMEIKQAEPDLNVGIATVYRTLNLLEEAEMVTSISFGSAGKKYELANKPHHDHMICKNCGKIIEFENPIIERQQALIAKEHGFKLTGHLMQLYGVCGDCNNQKAKVKI [Source organism chain A]=NCTC 11168) [UniProt ID chain B]=P0C631 [UniProt boundaries chain B]=2-154 [UniProt coverage chain B]=97% [Name chain B]=Ferric uptake regulation protein [UniProt sequence chain B]=MLIENVEYDVLLERFKKILRQGGLKYTKQREVLLKTLYHSDTHYTPESLYMEIKQAEPDLNVGIATVYRTLNLLEEAEMVTSISFGSAGKKYELANKPHHDHMICKNCGKIIEFENPIIERQQALIAKEHGFKLTGHLMQLYGVCGDCNNQKAKVKI [Source organism chain B]=NCTC 11168) [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=NCTC 11168) [Accession]=MF7000320 [Entry] [Entry number]=511 [Entry name]=AtRbcX1 (Arabidopsis thaliana) [PDB ID]=4gr2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Chaperonin-like RbcX [Sequence domain]=Chaperonin-like RbcX [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. However, RbcX is a dimer in solution (PMID:17574029) and its biologically relevant form is the homodimer (a monomeric form with this fold is not known PMID:23295968, PMID:21821880). The structure is highly intertwined with the interface being extended and hydrophobic between the two four-helix-bundle cores and by the exchange of the C-terminal parts of the long a4 helices between the two subunits (PMID:21821880). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000851,MF7000852,MF7000853,MF7000854,MF7000855,MF7000321 [UniProt ID chain A]=Q94AU9 [UniProt boundaries chain A]=54-163 [UniProt coverage chain A]=63% [Name chain A]=Chaperonin-like RBCX protein 1, chloroplastic [UniProt sequence chain A]=MESSSSLLHHSYLSYLNPKFGKRPLVSYPLMQSSRKCKQTRICSNKMYVPGFGEASPEAKAAKHLHDFFTYVAVRIVSAQLESYNPEAYMELREFLDTNSVSDGDKFCATLMRRSSRHMNLALRILEVRSAYCKNDFEWDNMKRLAFKNVDDSNTRLMREYVLETSHVETDSDK [Source organism chain A]=Arabidopsis thaliana [UniProt ID chain B]=Q94AU9 [UniProt boundaries chain B]=49-166 [UniProt coverage chain B]=67% [Name chain B]=Chaperonin-like RBCX protein 1, chloroplastic [UniProt sequence chain B]=MESSSSLLHHSYLSYLNPKFGKRPLVSYPLMQSSRKCKQTRICSNKMYVPGFGEASPEAKAAKHLHDFFTYVAVRIVSAQLESYNPEAYMELREFLDTNSVSDGDKFCATLMRRSSRHMNLALRILEVRSAYCKNDFEWDNMKRLAFKNVDDSNTRLMREYVLETSHVETDSDK [Source organism chain B]=Arabidopsis thaliana [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Arabidopsis thaliana [Accession]=MF7000321 [Entry] [Entry number]=512 [Entry name]=FosB (Bacillus cereus) [PDB ID]=4jh1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.55 [Source organism]=Bacillus cereus [Accession]=MF7000322 [Entry] [Entry number]=513 [Entry name]=FosB (Bacillus cereus) [PDB ID]=8g7f [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=2.04 [Source organism]=Bacillus cereus [Accession]=MF7000323 [Entry] [Entry number]=515 [Entry name]=Dimerization domain of Hsc70-interacting protein [PDB ID]=4j8c [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. Extensive helix packing within the short, all-helical dimerization domain. Monomers most likely not folded on their own (PMID:23812373). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P50503 [UniProt boundaries chain A]=1-44 [UniProt coverage chain A]=11% [Name chain A]=Hsc70-interacting protein [UniProt sequence chain A]=MDPRKVSELRAFVKMCRQDPSVLHTEEMRFLREWVESMGGKVPPATHKAKSEENTKEEKRDKTTEDNIKTEEPSSEESDLEIDNEGVIEADTDAPQEMGDENAEITEAMMDEANEKKGAAIDALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWEEAARDLALACKLDYDEDASAMLREVQPRAQKIAEHRRKYERKREEREIKERIERVKKAREEHEKAQREEEARRQSGSQFGSFPGGFPGGMPGNFPGGMPGMGGAMPGMAGMPGLNEILSDPEVLAAMQDPEVMVAFQDVAQNPSNMSKYQNNPKVMNLISKLSAKFGGHS [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P50503 [UniProt boundaries chain B]=1-44 [UniProt coverage chain B]=11% [Name chain B]=Hsc70-interacting protein [UniProt sequence chain B]=MDPRKVSELRAFVKMCRQDPSVLHTEEMRFLREWVESMGGKVPPATHKAKSEENTKEEKRDKTTEDNIKTEEPSSEESDLEIDNEGVIEADTDAPQEMGDENAEITEAMMDEANEKKGAAIDALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWEEAARDLALACKLDYDEDASAMLREVQPRAQKIAEHRRKYERKREEREIKERIERVKKAREEHEKAQREEEARRQSGSQFGSFPGGFPGGMPGNFPGGMPGMGGAMPGMAGMPGLNEILSDPEVLAAMQDPEVMVAFQDVAQNPSNMSKYQNNPKVMNLISKLSAKFGGHS [Source organism chain B]=Rattus norvegicus [ExpTech]=X-ray [Resolution]=1.10 [Source organism]=Rattus norvegicus [Accession]=MF7000325 [Entry] [Entry number]=518 [Entry name]=C-terminal of RasGRP1 [PDB ID]=4l9u [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:23908768). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O95267 [UniProt boundaries chain A]=745-793 [UniProt coverage chain A]=6% [Name chain A]=RAS guanyl-releasing protein 1 [UniProt sequence chain A]=MGTLGKAREAPRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPGLCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEINKVLGEMTELLSSSRNYDNYRRAYGECTDFKIPILGVHLKDLISLYEAMPDYLEDGKVNVHKLLALYNHISELVQLQEVAPPLEANKDLVHLLTLSLDLYYTEDEIYELSYAREPRNHRAPPLTPSKPPVVVDWASGVSPKPDPKTISKHVQRMVDSVFKNYDHDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRDEITAYFMRASSIYSKLGLGFPHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFECKKRAKNPVAPTENNTSVGPVSNLCSLGAKDLLHAPEEGPFTFPNGEAVEHGEESKDRTIMLMGVSSQKISLRLKRAVAHKATQTESQPWIGSEGPSGPFVLSSPRKTAQDTLYVLPSPTSPCPSPVLVRKRAFVKWENKDSLIKSKEELRHLRLPTYQELEQEINTLKADNDALKIQLKYAQKKIESLQLEKSNHVLAQMEQGDCS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O95267 [UniProt boundaries chain B]=745-786 [UniProt coverage chain B]=5% [Name chain B]=RAS guanyl-releasing protein 1 [UniProt sequence chain B]=MGTLGKAREAPRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPGLCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEINKVLGEMTELLSSSRNYDNYRRAYGECTDFKIPILGVHLKDLISLYEAMPDYLEDGKVNVHKLLALYNHISELVQLQEVAPPLEANKDLVHLLTLSLDLYYTEDEIYELSYAREPRNHRAPPLTPSKPPVVVDWASGVSPKPDPKTISKHVQRMVDSVFKNYDHDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRDEITAYFMRASSIYSKLGLGFPHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFECKKRAKNPVAPTENNTSVGPVSNLCSLGAKDLLHAPEEGPFTFPNGEAVEHGEESKDRTIMLMGVSSQKISLRLKRAVAHKATQTESQPWIGSEGPSGPFVLSSPRKTAQDTLYVLPSPTSPCPSPVLVRKRAFVKWENKDSLIKSKEELRHLRLPTYQELEQEINTLKADNDALKIQLKYAQKKIESLQLEKSNHVLAQMEQGDCS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Homo sapiens [Accession]=MF7000328 [Entry] [Entry number]=519 [Entry name]=Cytosolic domain of the Plant Ethylene Receptor 1 (ETR1) [PDB ID]=4mt8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:25451923). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q38846 [UniProt boundaries chain A]=308-406 [UniProt coverage chain A]=16% [Name chain A]=Ethylene response sensor 1 [UniProt sequence chain A]=MESCDCFETHVNQDDLLVKYQYISDALIALAYFSIPLELIYFVQKSAFFPYKWVLMQFGAFIILCGATHFINLWMFFMHSKAVAIVMTIAKVSCAVVSCATALMLVHIIPDLLSVKNRELFLKKKADELDREMGLILTQEETGRHVRMLTHGIRRTLDRHTILRTTLVELGKTLCLEECALWMPSQSGLYLQLSHTLSHKIQVGSSVPINLPIINELFNSAQAMHIPHSCPLAKIGPPVGRYSPPEVVSVRVPLLHLSNFQGSDWSDLSGKGYAIMVLILPTDGARKWRDHELELVENVADQVAVALSHAAILEESMHARDQLMEQNFALDKARQEAEMAVHARNDFLAVMNHEMRTPMHAIISLSSLLLETELSPEQRVMIETILKSSNLVATLISDVLDLSRLEDGSLLLENEPFSLQAIFEEVISLIKPIASVKKLSTNLILSADLPTYAIGDEKRLMQTILNIMGNAVKFTKEGYISIIASIMKPESLQELPSPEFFPVLSDSHFYLCVQVKDTGCGIHTQDIPLLFTKFVQPRTGTQRNHSGGGLGLALCKRFVGLMGGYMWIESEGLEKGCTASFIIRLGICNGPSSSSGSMALHLAAKSQTRPWNW [Source organism chain A]=Arabidopsis thaliana [UniProt ID chain B]=Q38846 [UniProt boundaries chain B]=312-407 [UniProt coverage chain B]=15% [Name chain B]=Ethylene response sensor 1 [UniProt sequence chain B]=MESCDCFETHVNQDDLLVKYQYISDALIALAYFSIPLELIYFVQKSAFFPYKWVLMQFGAFIILCGATHFINLWMFFMHSKAVAIVMTIAKVSCAVVSCATALMLVHIIPDLLSVKNRELFLKKKADELDREMGLILTQEETGRHVRMLTHGIRRTLDRHTILRTTLVELGKTLCLEECALWMPSQSGLYLQLSHTLSHKIQVGSSVPINLPIINELFNSAQAMHIPHSCPLAKIGPPVGRYSPPEVVSVRVPLLHLSNFQGSDWSDLSGKGYAIMVLILPTDGARKWRDHELELVENVADQVAVALSHAAILEESMHARDQLMEQNFALDKARQEAEMAVHARNDFLAVMNHEMRTPMHAIISLSSLLLETELSPEQRVMIETILKSSNLVATLISDVLDLSRLEDGSLLLENEPFSLQAIFEEVISLIKPIASVKKLSTNLILSADLPTYAIGDEKRLMQTILNIMGNAVKFTKEGYISIIASIMKPESLQELPSPEFFPVLSDSHFYLCVQVKDTGCGIHTQDIPLLFTKFVQPRTGTQRNHSGGGLGLALCKRFVGLMGGYMWIESEGLEKGCTASFIIRLGICNGPSSSSGSMALHLAAKSQTRPWNW [Source organism chain B]=Arabidopsis thaliana [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Arabidopsis thaliana [Accession]=MF7000329 [Entry] [Entry number]=520 [Entry name]=MST1-RASSF5 SARAH heterodimer [PDB ID]=4oh8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:25004971). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q13043 [UniProt boundaries chain A]=438-480 [UniProt coverage chain A]=8% [Name chain A]=Serine/threonine-protein kinase 4 [UniProt sequence chain A]=METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVRSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGANTMIEHDDTLPSQLGTMVINAEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q8WWW0 [UniProt boundaries chain B]=367-412 [UniProt coverage chain B]=11% [Name chain B]=Ras association domain-containing protein 5 [UniProt sequence chain B]=MAMASPAIGQRPYPLLLDPEPPRYLQSLSGPELPPPPPDRSSRLCVPAPLSTAPGAREGRSARRAARGNLEPPPRASRPARPLRPGLQQRLRRRPGAPRPRDVRSIFEQPQDPRVPAERGEGHCFAELVLPGGPGWCDLCGREVLRQALRCTNCKFTCHPECRSLIQLDCSQQEGLSRDRPSPESTLTVTFSQNVCKPVEETQRPPTLQEIKQKIDSYNTREKNCLGMKLSEDGTYTGFIKVHLKLRRPVTVPAGIRPQSIYDAIKEVNLAATTDKRTSFYLPLDAIKQLHISSTTTVSEVIQGLLKKFMVVDNPQKFALFKRIHKDGQVLFQKLSIADRPLYLRLLAGPDTEVLSFVLKENETGEVEWDAFSIPELQNFLTILEKEEQDKIQQVQKKYDKFRQKLEEALRESQGKPG [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.28 [Source organism]=Homo sapiens [Accession]=MF7000330 [Entry] [Entry number]=521 [Entry name]=MST2 SARAH homodimer complex [PDB ID]=4oh9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:25004971). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q13188 [UniProt boundaries chain A]=436-484 [UniProt coverage chain A]=9% [Name chain A]=Serine/threonine-protein kinase 3 [UniProt sequence chain A]=MEQPPAPKSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLIEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEEEENSDEDELDSHTMVKTSVESVGTMRATSTMSEGAQTMIEHNSTMLESDLGTMVINSEDEEEEDGTMKRNATSPQVQRPSFMDYFDKQDFKNKSHENCNQNMHEPFPMSKNVFPDNWKVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAKKRRQQNF [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q13188 [UniProt boundaries chain B]=436-484 [UniProt coverage chain B]=9% [Name chain B]=Serine/threonine-protein kinase 3 [UniProt sequence chain B]=MEQPPAPKSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLIEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEEEENSDEDELDSHTMVKTSVESVGTMRATSTMSEGAQTMIEHNSTMLESDLGTMVINSEDEEEEDGTMKRNATSPQVQRPSFMDYFDKQDFKNKSHENCNQNMHEPFPMSKNVFPDNWKVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAKKRRQQNF [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Homo sapiens [Accession]=MF7000388 [Entry] [Entry number]=522 [Entry name]=SCO4226 (Streptomyces coelicolor A3(2)) [PDB ID]=4oi3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Nickel responsive protein SCO4226-like [Evidence level]=Indirect evidence [Evidence text]=There is beta sheet augmentation between the SCO4226 monomers, so it seems that dimer is the obligate form of the protein and the monomers would be unstable in solution. The overall structure of SCO4226 adopts a ferredoxin-like fold with an α+β structure: five β-strands (β1-5) packing against two α-helices (α1-2). The N-terminal four β-strands β1-4 of one subunit form an antiparallel β-sheet, whereas the C-terminal β5 swaps to the corresponding β-sheet (β1′-4′) of the symmetric subunit, completing an extended antiparallel β-sheet of five strands. These two extended β-sheets face against each other to form a dimer interface, which possesses a hydrophobic core sealed by two hydrophilic laterals. The hydrophobic core is formed by residues Met5, Trp41, Tyr50, Leu52, and Val78 from both subunits (PMID:25285530). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000332,MF7000333 [UniProt ID chain A]=Q9FCE4 [UniProt boundaries chain A]=2-82 [UniProt coverage chain A]=98% [Name chain A]=SCO4226 family nickel-binding protein [UniProt sequence chain A]=MAHFMDVHRGMHGITSDQLHQAHQADLAVEKDENVHFEQAWADPASGTIYCLSEGPSAEAVQRVHERAGHKADEIHEVPLSA [Source organism chain A]=Streptomyces coelicolor [UniProt ID chain B]=Q9FCE4 [UniProt boundaries chain B]=2-82 [UniProt coverage chain B]=98% [Name chain B]=SCO4226 family nickel-binding protein [UniProt sequence chain B]=MAHFMDVHRGMHGITSDQLHQAHQADLAVEKDENVHFEQAWADPASGTIYCLSEGPSAEAVQRVHERAGHKADEIHEVPLSA [Source organism chain B]=Streptomyces coelicolor [ExpTech]=X-ray [Resolution]=1.30 [Source organism]=Streptomyces coelicolor [Accession]=MF7000332 [Entry] [Entry number]=523 [Entry name]=SCO4226 (Streptomyces coelicolor A3(2)) [PDB ID]=4oi6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Nickel responsive protein SCO4226-like [Evidence level]=Indirect evidence [Evidence text]=There is beta sheet augmentation between the SCO4226 monomers, so it seems that dimer is the obligate form of the protein and the monomers would be unstable in solution. The overall structure of SCO4226 adopts a ferredoxin-like fold with an α+β structure: five β-strands (β1-5) packing against two α-helices (α1-2). The N-terminal four β-strands β1-4 of one subunit form an antiparallel β-sheet, whereas the C-terminal β5 swaps to the corresponding β-sheet (β1′-4′) of the symmetric subunit, completing an extended antiparallel β-sheet of five strands. These two extended β-sheets face against each other to form a dimer interface, which possesses a hydrophobic core sealed by two hydrophilic laterals. The hydrophobic core is formed by residues Met5, Trp41, Tyr50, Leu52, and Val78 from both subunits (PMID:25285530). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000332,MF7000333 [UniProt ID chain A]=Q9FCE4 [UniProt boundaries chain A]=2-82 [UniProt coverage chain A]=98% [Name chain A]=SCO4226 family nickel-binding protein [UniProt sequence chain A]=MAHFMDVHRGMHGITSDQLHQAHQADLAVEKDENVHFEQAWADPASGTIYCLSEGPSAEAVQRVHERAGHKADEIHEVPLSA [Source organism chain A]=Streptomyces coelicolor [UniProt ID chain B]=Q9FCE4 [UniProt boundaries chain B]=2-82 [UniProt coverage chain B]=98% [Name chain B]=SCO4226 family nickel-binding protein [UniProt sequence chain B]=MAHFMDVHRGMHGITSDQLHQAHQADLAVEKDENVHFEQAWADPASGTIYCLSEGPSAEAVQRVHERAGHKADEIHEVPLSA [Source organism chain B]=Streptomyces coelicolor [ExpTech]=X-ray [Resolution]=2.04 [Source organism]=Streptomyces coelicolor [Accession]=MF7000333 [Entry] [Entry number]=524 [Entry name]=Domain-swapped lectin dimer (Mycobacterium smegmatis) [PDB ID]=4okc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bulb-type lectin domain [Subclass]=Homodimeric lectin [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Extensive unprecedented domain swapping in dimer formation, the swapping involves 4 of the 12 strands in each subunit (PMID:24957055). The association between the two subunits of mannose-binding lectin from garlic bulbs was shown to be highly reversible and can be defined as a two-state process in which the folded dimer is converted directly into the unfolded monomers (PMID: 11401577). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=A0QYH7 [UniProt boundaries chain A]=1-105 [UniProt coverage chain A]=50% [Name chain A]=Mannose-binding lectin [UniProt sequence chain A]=MGDTLTAGQKLERGGSLQSGNGAYTLTLQDDGNLVLYARDKAVWSTGTNGQDVVRAEVQTDGNFVLYTAEKPVWHTDTKGKKEVKLVLQDDRNLVLYAKDGPAWSSKTDTTEPPPPAPEPEKEAEVAPAAAEEAAPAPVAEPAPAEPAPAAPPPAPPAPRTYTVVSGDTLWAIAERFYGDGSKYQQIADASGIANPDLIHPGQVLTIP [Source organism chain A]=smegmatis) [UniProt ID chain B]=A0QYH7 [UniProt boundaries chain B]=1-105 [UniProt coverage chain B]=50% [Name chain B]=Mannose-binding lectin [UniProt sequence chain B]=MGDTLTAGQKLERGGSLQSGNGAYTLTLQDDGNLVLYARDKAVWSTGTNGQDVVRAEVQTDGNFVLYTAEKPVWHTDTKGKKEVKLVLQDDRNLVLYAKDGPAWSSKTDTTEPPPPAPEPEKEAEVAPAAAEEAAPAPVAEPAPAEPAPAAPPPAPPAPRTYTVVSGDTLWAIAERFYGDGSKYQQIADASGIANPDLIHPGQVLTIP [Source organism chain B]=smegmatis) [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=smegmatis) [Accession]=MF7000334 [Entry] [Entry number]=525 [Entry name]=FHMPCDH [PDB ID]=4om8 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=It is a dimer. Dissociation cannot be detected by differential scanning calorimetry (PMID:35041856). The helical dimerization domain is very tightly packed. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q988C8 [UniProt boundaries chain A]=1-309 [UniProt coverage chain A]=100% [Name chain A]=5-formyl-3-hydroxy-2-methylpyridine 4-carboxylate 5-dehydrogenase [UniProt sequence chain A]=MIRNIAIIGLGTMGPGMAARLARGGLQVVAYDVAPAAIERARSMLSVAETVLDALGIALPSAGVGTVRFTDDIGDAVSGADLVIENVPENISIKADVYRTIDGLIGQDTIVASDTSGIPITKLQAHISYPERMVGMHWSNPPHIIPMIEVIAGEKTAPQTVATIRDLIRSIGLLPVVVKKDVPGFVENRVLYALLREAVDLVERGVIDPEDLDTCVSWGIGYKIAVIGPMALLDMAGLDIYKSVSSFLNADLSNRDDVAPMVLEKTSASKFGIKSGEGMFCYTPEQTKALQAERARKLVAVRRILEGRE [Source organism chain A]= [UniProt ID chain A-2]=Q988C8 [UniProt boundaries chain A-2]=1-309 [UniProt coverage chain A-2]=100% [Name chain A-2]=5-formyl-3-hydroxy-2-methylpyridine 4-carboxylate 5-dehydrogenase [UniProt sequence chain A-2]=MIRNIAIIGLGTMGPGMAARLARGGLQVVAYDVAPAAIERARSMLSVAETVLDALGIALPSAGVGTVRFTDDIGDAVSGADLVIENVPENISIKADVYRTIDGLIGQDTIVASDTSGIPITKLQAHISYPERMVGMHWSNPPHIIPMIEVIAGEKTAPQTVATIRDLIRSIGLLPVVVKKDVPGFVENRVLYALLREAVDLVERGVIDPEDLDTCVSWGIGYKIAVIGPMALLDMAGLDIYKSVSSFLNADLSNRDDVAPMVLEKTSASKFGIKSGEGMFCYTPEQTKALQAERARKLVAVRRILEGRE [Source organism chain A-2]= [ExpTech]=X-ray [Resolution]=1.55 [Source organism]= [Accession]=MF7000335 [Entry] [Entry number]=528 [Entry name]=SYCE3 [PDB ID]=4r3q [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Synaptonemal complex central element protein 3 [Evidence level]=Indirect evidence [Evidence text]=The authors claim that the extensive hydrophobic and hydrogen bonding interactions within the 4-helix bundle indicate highly stable dimer formation. SYCE3 is also seen in the dimeric form in solution and in cells by several methods (PMID:25394919). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000338,MF7000972 [UniProt ID chain A]=B5KM66 [UniProt boundaries chain A]=13-85 [UniProt coverage chain A]=82% [Name chain A]=Synaptonemal complex central element protein 3 [UniProt sequence chain A]=MADSDPGERSYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFLNCKEEMEKNWQELLTETKRKQ [Source organism chain A]=Mus musculus [UniProt ID chain B]=B5KM66 [UniProt boundaries chain B]=12-85 [UniProt coverage chain B]=84% [Name chain B]=Synaptonemal complex central element protein 3 [UniProt sequence chain B]=MADSDPGERSYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFLNCKEEMEKNWQELLTETKRKQ [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Mus musculus [Accession]=MF7000338 [Entry] [Entry number]=530 [Entry name]=L27 domain of Discs Large 1 [PDB ID]=4rp4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=L27 domains [Subclass]=L27_1 type [Sequence domain]=L27_1 [Evidence level]=Direct evidence [Evidence text]=The interacting chains form half of a heterotetrameric L27 complex (a dimer of dimers) (PMID:16147993). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110024,MF7000341,MF7000342 [UniProt ID chain A]=P31007 [UniProt boundaries chain A]=5-94 [UniProt coverage chain A]=9% [Name chain A]=Disks large 1 tumor suppressor protein [UniProt sequence chain A]=MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIFKSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWEKDGQAVKIADFIKSSNLNRNCAYEFNNDASSNQTNQSALNQNPIANNVSAQAQAEALSRTFKSELEEILNQRMRIESDTENAKEPTVEQQQKQQQAQQRSSRSPQQQNPQQQQGSKSRSGSQTVNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIYITKLISGGAAAADGRLSINDIIVSVNDVSVVDVPHASAVDALKKAGNVVKLHVKRKRGTATTPAAGSAAGDARDSAASGPKVIEIDLVKGGKGLGFSIAGGIGNQHIPGDNGIYVTKLMDGGAAQVDGRLSIGDKLIAVRTNGSEKNLENVTHELAVATLKSITDKVTLIIGKTQHLTTSASGGGGGGLSSGQQLSQSQSQLATSQSQSQVHQQQHATPMVNSQSTEPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGPQGLGFNIVGGEDGQGIYVSFILAGGPADLGSELKRGDQLLSVNNVNLTHATHEEAAQALKTSGGVVTLLAQYRPEEYNRFEARIQELKQQAALGAGGSGTLLRTTQKRSLYVRALFDYDPNRDDGLPSRGLPFKHGDILHVTNASDDEWWQARRVLGDNEDEQIGIVPSKRRWERKMRARDRSVKFQGHAAANNNLDKQSTLDRKKKNFTFSRKFPFMKSRDEKNEDGSDQEPFMLCYTQDDANAEGASEENVLSYEAVQRLSINYTRPVIILGPLKDRINDDLISEYPDKFGSCVPHTTRPKREYEVDGRDYHFVSSREQMERDIQNHLFIEAGQYNDNLYGTSVASVREVAEKGKHCILDVSGNAIKRLQVAQLYPVAVFIKPKSVDSVMEMNRRMTEEQAKKTYERAIKMEQEFGEYFTGVVQGDTIEEIYSKVKSMIWSQSGPTIWVPSKESL [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=P31007 [UniProt boundaries chain B]=5-95 [UniProt coverage chain B]=9% [Name chain B]=Disks large 1 tumor suppressor protein [UniProt sequence chain B]=MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIFKSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWEKDGQAVKIADFIKSSNLNRNCAYEFNNDASSNQTNQSALNQNPIANNVSAQAQAEALSRTFKSELEEILNQRMRIESDTENAKEPTVEQQQKQQQAQQRSSRSPQQQNPQQQQGSKSRSGSQTVNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIYITKLISGGAAAADGRLSINDIIVSVNDVSVVDVPHASAVDALKKAGNVVKLHVKRKRGTATTPAAGSAAGDARDSAASGPKVIEIDLVKGGKGLGFSIAGGIGNQHIPGDNGIYVTKLMDGGAAQVDGRLSIGDKLIAVRTNGSEKNLENVTHELAVATLKSITDKVTLIIGKTQHLTTSASGGGGGGLSSGQQLSQSQSQLATSQSQSQVHQQQHATPMVNSQSTEPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGPQGLGFNIVGGEDGQGIYVSFILAGGPADLGSELKRGDQLLSVNNVNLTHATHEEAAQALKTSGGVVTLLAQYRPEEYNRFEARIQELKQQAALGAGGSGTLLRTTQKRSLYVRALFDYDPNRDDGLPSRGLPFKHGDILHVTNASDDEWWQARRVLGDNEDEQIGIVPSKRRWERKMRARDRSVKFQGHAAANNNLDKQSTLDRKKKNFTFSRKFPFMKSRDEKNEDGSDQEPFMLCYTQDDANAEGASEENVLSYEAVQRLSINYTRPVIILGPLKDRINDDLISEYPDKFGSCVPHTTRPKREYEVDGRDYHFVSSREQMERDIQNHLFIEAGQYNDNLYGTSVASVREVAEKGKHCILDVSGNAIKRLQVAQLYPVAVFIKPKSVDSVMEMNRRMTEEQAKKTYERAIKMEQEFGEYFTGVVQGDTIEEIYSKVKSMIWSQSGPTIWVPSKESL [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=1.42 [Source organism]=Drosophila melanogaster [Accession]=MF7000341 [Entry] [Entry number]=531 [Entry name]=L27 domain of Discs Large 2 [PDB ID]=4rp5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=L27 domains [Subclass]=L27_1 type [Sequence domain]=L27_1 [Evidence level]=Direct evidence [Evidence text]=The interacting chains form half of a heterotetrameric L27 complex (a dimer of dimers) (PMID:16147993). L27 complexes formed by Lin-2 and Lin-7 proteins were shown to function as obligate heterodimers/tetramers undergoing a cooperative unfolding transition. Circular dichroism studies reveal that the individual monomers are largely unfolded outside the complex form (PMID:12110687). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110024,MF7000341,MF7000342 [UniProt ID chain A]=P31007 [UniProt boundaries chain A]=1-94 [UniProt coverage chain A]=9% [Name chain A]=Disks large 1 tumor suppressor protein [UniProt sequence chain A]=MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIFKSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWEKDGQAVKIADFIKSSNLNRNCAYEFNNDASSNQTNQSALNQNPIANNVSAQAQAEALSRTFKSELEEILNQRMRIESDTENAKEPTVEQQQKQQQAQQRSSRSPQQQNPQQQQGSKSRSGSQTVNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIYITKLISGGAAAADGRLSINDIIVSVNDVSVVDVPHASAVDALKKAGNVVKLHVKRKRGTATTPAAGSAAGDARDSAASGPKVIEIDLVKGGKGLGFSIAGGIGNQHIPGDNGIYVTKLMDGGAAQVDGRLSIGDKLIAVRTNGSEKNLENVTHELAVATLKSITDKVTLIIGKTQHLTTSASGGGGGGLSSGQQLSQSQSQLATSQSQSQVHQQQHATPMVNSQSTEPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGPQGLGFNIVGGEDGQGIYVSFILAGGPADLGSELKRGDQLLSVNNVNLTHATHEEAAQALKTSGGVVTLLAQYRPEEYNRFEARIQELKQQAALGAGGSGTLLRTTQKRSLYVRALFDYDPNRDDGLPSRGLPFKHGDILHVTNASDDEWWQARRVLGDNEDEQIGIVPSKRRWERKMRARDRSVKFQGHAAANNNLDKQSTLDRKKKNFTFSRKFPFMKSRDEKNEDGSDQEPFMLCYTQDDANAEGASEENVLSYEAVQRLSINYTRPVIILGPLKDRINDDLISEYPDKFGSCVPHTTRPKREYEVDGRDYHFVSSREQMERDIQNHLFIEAGQYNDNLYGTSVASVREVAEKGKHCILDVSGNAIKRLQVAQLYPVAVFIKPKSVDSVMEMNRRMTEEQAKKTYERAIKMEQEFGEYFTGVVQGDTIEEIYSKVKSMIWSQSGPTIWVPSKESL [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=P31007 [UniProt boundaries chain B]=5-94 [UniProt coverage chain B]=9% [Name chain B]=Disks large 1 tumor suppressor protein [UniProt sequence chain B]=MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIFKSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWEKDGQAVKIADFIKSSNLNRNCAYEFNNDASSNQTNQSALNQNPIANNVSAQAQAEALSRTFKSELEEILNQRMRIESDTENAKEPTVEQQQKQQQAQQRSSRSPQQQNPQQQQGSKSRSGSQTVNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIYITKLISGGAAAADGRLSINDIIVSVNDVSVVDVPHASAVDALKKAGNVVKLHVKRKRGTATTPAAGSAAGDARDSAASGPKVIEIDLVKGGKGLGFSIAGGIGNQHIPGDNGIYVTKLMDGGAAQVDGRLSIGDKLIAVRTNGSEKNLENVTHELAVATLKSITDKVTLIIGKTQHLTTSASGGGGGGLSSGQQLSQSQSQLATSQSQSQVHQQQHATPMVNSQSTEPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGPQGLGFNIVGGEDGQGIYVSFILAGGPADLGSELKRGDQLLSVNNVNLTHATHEEAAQALKTSGGVVTLLAQYRPEEYNRFEARIQELKQQAALGAGGSGTLLRTTQKRSLYVRALFDYDPNRDDGLPSRGLPFKHGDILHVTNASDDEWWQARRVLGDNEDEQIGIVPSKRRWERKMRARDRSVKFQGHAAANNNLDKQSTLDRKKKNFTFSRKFPFMKSRDEKNEDGSDQEPFMLCYTQDDANAEGASEENVLSYEAVQRLSINYTRPVIILGPLKDRINDDLISEYPDKFGSCVPHTTRPKREYEVDGRDYHFVSSREQMERDIQNHLFIEAGQYNDNLYGTSVASVREVAEKGKHCILDVSGNAIKRLQVAQLYPVAVFIKPKSVDSVMEMNRRMTEEQAKKTYERAIKMEQEFGEYFTGVVQGDTIEEIYSKVKSMIWSQSGPTIWVPSKESL [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Drosophila melanogaster [Accession]=MF7000342 [Entry] [Entry number]=532 [Entry name]=MerR (Priestia megaterium) [PDB ID]=4ua1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=DNA-binding HTH domain and helical dimerization domain [Sequence domain]=MerR-type HTH domain transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=A substantial part of the structure is a coiled coil dimerization region. Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815). There is an N-terminal MerR-type HTH DNA-binding domain and a C-terminal coiled coil dimerization region. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000343,MF7000344 [UniProt ID chain A]=Q799U3 [UniProt boundaries chain A]=3-131 [UniProt coverage chain A]=97% [Name chain A]=Mercuric resistance operon regulatory protein [UniProt sequence chain A]=MKFRIGELADKCGVNKETIRYYERLGLIPEPERTEKGYRMYSQQTVDRLHFIKRMQELGFTLNEIDKLLGVVDRDEAKCRDMYDFTILKIEDIQRKIEDLKRIERMLMDLKERCPENKDIYECPIIETLMKK [Source organism chain A]=Priestia megaterium [UniProt ID chain B]=Q799U3 [UniProt boundaries chain B]=3-131 [UniProt coverage chain B]=97% [Name chain B]=Mercuric resistance operon regulatory protein [UniProt sequence chain B]=MKFRIGELADKCGVNKETIRYYERLGLIPEPERTEKGYRMYSQQTVDRLHFIKRMQELGFTLNEIDKLLGVVDRDEAKCRDMYDFTILKIEDIQRKIEDLKRIERMLMDLKERCPENKDIYECPIIETLMKK [Source organism chain B]=Priestia megaterium [ExpTech]=X-ray [Resolution]=2.56 [Source organism]=Priestia megaterium [Accession]=MF7000343 [Entry] [Entry number]=533 [Entry name]=Transcription activator Tn501 MerR [PDB ID]=5crl [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=DNA-binding HTH domain and helical dimerization domain [Sequence domain]=MerR-type HTH domain transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=A substantial part of the structure is a coiled coil dimerization region. Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815). There is an N-terminal MerR-type HTH DNA-binding domain and a C-terminal coiled coil dimerization region. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000343,MF7000344 [UniProt ID chain A]=P0A183 [UniProt boundaries chain A]=6-133 [UniProt coverage chain A]=88% [Name chain A]=Mercuric resistance operon regulatory protein [UniProt sequence chain A]=MENNLENLTIGVFAKAAGVNVETIRFYQRKGLLLEPDKPYGSIRRYGEADVTRVRFVKSAQRLGFSLDEIAELLRLEDGTHCEEASSLAEHKLKDVREKMADLARMEAVLSELVCACHARRGNVSCPLIASLQGGASLAGSAMP [Source organism chain A]=Pseudomonas aeruginosa [UniProt ID chain B]=P0A183 [UniProt boundaries chain B]=7-134 [UniProt coverage chain B]=88% [Name chain B]=Mercuric resistance operon regulatory protein [UniProt sequence chain B]=MENNLENLTIGVFAKAAGVNVETIRFYQRKGLLLEPDKPYGSIRRYGEADVTRVRFVKSAQRLGFSLDEIAELLRLEDGTHCEEASSLAEHKLKDVREKMADLARMEAVLSELVCACHARRGNVSCPLIASLQGGASLAGSAMP [Source organism chain B]=Pseudomonas aeruginosa [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Pseudomonas aeruginosa [Accession]=MF7000344 [Entry] [Entry number]=534 [Entry name]=N-terminal domain of GpsB [PDB ID]=4ug1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=DivIVA protein [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:26575090). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000229,MF7000345 [UniProt ID chain A]=Q8Y614 [UniProt boundaries chain A]=1-68 [UniProt coverage chain A]=60% [Name chain A]=Cell cycle protein GpsB [UniProt sequence chain A]=MTSEQFEYHLTGKEILEKEFKTGLRGYSPEDVDEFLDMVIKDYSTFTQEIEALQAENIRLVQELDNAPLRTSTQPAPTFQAAAQPAGTTNFDILKRLSNLEKHVFGNKLDDNE [Source organism chain A]=Listeria monocytogenes serovar 1/2a [UniProt ID chain B]=Q8Y614 [UniProt boundaries chain B]=1-71 [UniProt coverage chain B]=62% [Name chain B]=Cell cycle protein GpsB [UniProt sequence chain B]=MTSEQFEYHLTGKEILEKEFKTGLRGYSPEDVDEFLDMVIKDYSTFTQEIEALQAENIRLVQELDNAPLRTSTQPAPTFQAAAQPAGTTNFDILKRLSNLEKHVFGNKLDDNE [Source organism chain B]=Listeria monocytogenes serovar 1/2a [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Listeria monocytogenes serovar 1/2a [Accession]=MF7000345 [Entry] [Entry number]=535 [Entry name]=TAF8/TAF10 heterodimer [PDB ID]=4wv4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=As observed in other histone fold domain (HFD) interactions, the two opposing aromatic residues Y68 of TAF8 and F162 of TAF10 at the crossover of the α2 helices contact each other via hydrophobic stacking interactions and categorize the complex to the H3/H4 family of HFD-containing proteins (PMID:PMID:25586196). There is also disorder evidence for the TAF10 region in DisProt:DP03622. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q12962 [UniProt boundaries chain A]=113-212 [UniProt coverage chain A]=45% [Name chain A]=Transcription initiation factor TFIID subunit 10 [UniProt sequence chain A]=MSCSGSGADPEAAPASAASAPGPAPPVSAPAALPSSTAAENKASPAGTAGGPGAGAAAGGTGPLAARAGEPAERRGAAPVSAGGAAPPEGAISNGVYVLPSAANGDVKPVVSSTPLVDFLMQLEDYTPTIPDAVTGYYLNRAGFEASDPRIIRLISLAAQKFISDIANDALQHCKMKGTASGSSRSKSKDRKYTLTMEDLTPALSEYGINVKKPHYFT [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q7Z7C8 [UniProt boundaries chain B]=28-120 [UniProt coverage chain B]=30% [Name chain B]=Transcription initiation factor TFIID subunit 8 [UniProt sequence chain B]=MADAAATAGAGGSGTRSGSKQSTNPADNYHLARRRTLQVVVSSLLTEAGFESAEKASVETLTEMLQSYISEIGRSAKSYCEHTARTQPTLSDIVVTLVEMGFNVDTLPAYAKRSQRMVITAPPVTNQPVTPKALTAGQNRPHPPHIPSHFPEFPDPHTYIKTPTYREPVSDYQVLREKAASQRRDVERALTRFMAKTGETQSLFKDDVSTFPLIAARPFTIPYLTALLPSELEMQQMEETDSSEQDEQTDTENLALHISMEDSGAEKENTSVLQQNPSLSGSRNGEENIIDNPYLRPVKKPKIRRKKSLS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.91 [Source organism]=Homo sapiens [Accession]=MF7000346 [Entry] [Entry number]=536 [Entry name]=Dimerization domain of SAS-5 (C. elegans) [PDB ID]=4ynh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Interlocked helices are arranged in an antiparallel fashion. Novel globular dimeric Implico domain, with high thermal stability. Heat denaturation after point mutations implies disordered monomeric state (PMID:26023830). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q20010 [UniProt boundaries chain A]=210-264 [UniProt coverage chain A]=13% [Name chain A]=Spindle assembly abnormal protein 5 [UniProt sequence chain A]=MNNYDDLPCSIYFKKPTVQEFVDQPRVFEDSEVPAFQEVLQLPQERTKPPVPSTQPIVAAVEVAKKKSCLSAPKPRKEPPSHPALRQKTVAFGKTVNVSQTVEGTSRNSKKVLASTMSAQNTTTTEEQAAENWRDAMKTELQTIRTEIQEETARRQEELNAQNLVKMQELMSNFFQKITIPKQQAIEPVEKDKENFHESPRQSRQQKPASKIASAREVIKRDGVIPPEALTIIEQRLRSDPMFRQQIDNVLADAECDANRAAYSPPPPMSEVRYGSGVNPALMRETLTVERSIRYDNGLASIDSRQWTNERRDNRAPDSYRTYEPDQPCHSLYQKGQSISYYPSEAAGKTTARNNRTGYYVEDSSDHEEDVVVNKRGQNYHEQAVPETPAERERRIREKYARRK [Source organism chain A]=Caenorhabditis elegans [UniProt ID chain B]=Q20010 [UniProt boundaries chain B]=210-263 [UniProt coverage chain B]=13% [Name chain B]=Spindle assembly abnormal protein 5 [UniProt sequence chain B]=MNNYDDLPCSIYFKKPTVQEFVDQPRVFEDSEVPAFQEVLQLPQERTKPPVPSTQPIVAAVEVAKKKSCLSAPKPRKEPPSHPALRQKTVAFGKTVNVSQTVEGTSRNSKKVLASTMSAQNTTTTEEQAAENWRDAMKTELQTIRTEIQEETARRQEELNAQNLVKMQELMSNFFQKITIPKQQAIEPVEKDKENFHESPRQSRQQKPASKIASAREVIKRDGVIPPEALTIIEQRLRSDPMFRQQIDNVLADAECDANRAAYSPPPPMSEVRYGSGVNPALMRETLTVERSIRYDNGLASIDSRQWTNERRDNRAPDSYRTYEPDQPCHSLYQKGQSISYYPSEAAGKTTARNNRTGYYVEDSSDHEEDVVVNKRGQNYHEQAVPETPAERERRIREKYARRK [Source organism chain B]=Caenorhabditis elegans [ExpTech]=X-ray [Resolution]=1.00 [Source organism]=Caenorhabditis elegans [Accession]=MF7000347 [Entry] [Entry number]=537 [Entry name]=YdiE [PDB ID]=4ynx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=The authors claim that the monomeric structure seems highly unlikely in solution (PMID:26144239). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P0ACX9 [UniProt boundaries chain A]=24-63 [UniProt coverage chain A]=63% [Name chain A]=Uncharacterized protein YdiE [UniProt sequence chain A]=MRYTDSRKLTPETDANHKTASPQPIRRISSQTLLGPDGKLIIDHDGQEYLLRKTQAGKLLLTK [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0ACX9 [UniProt boundaries chain B]=22-63 [UniProt coverage chain B]=66% [Name chain B]=Uncharacterized protein YdiE [UniProt sequence chain B]=MRYTDSRKLTPETDANHKTASPQPIRRISSQTLLGPDGKLIIDHDGQEYLLRKTQAGKLLLTK [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Escherichia coli [Accession]=MF7000348 [Entry] [Entry number]=538 [Entry name]=C-terminal of Bicaudal D1 (mouse) [PDB ID]=4ytd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Protein bicaudal D [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:25796327). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000349,MF7000350,MF7000351 [UniProt ID chain A]=Q8BR07 [UniProt boundaries chain A]=711-803 [UniProt coverage chain A]=11% [Name chain A]=Protein bicaudal D homolog 1 [UniProt sequence chain A]=MAAEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYINLSDSHISISVDGLKFAEDGSEPNNDDKMNGHIHGPLGKLNGDYRTPTTRKGESLHPVSDLFSELNISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSKEIKAELDCEKGRNSAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQLYHHVCLCNNETPNRVMLDYYRQSRVTRSGSLKGPDDPRGLLSPRLSRRGVSSPVESRTSSEPVSKENTETSKEPSPTKTPTISPVITAPPSSPVLDTSDIRKEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKLGKSKIGSPKIVSSLLPPYRHSAHN [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q8BR07 [UniProt boundaries chain B]=711-808 [UniProt coverage chain B]=11% [Name chain B]=Protein bicaudal D homolog 1 [UniProt sequence chain B]=MAAEEALKTVDQYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDGLKQELEQLREAFGQSFSIHRKVAEDGETREETLLQESASKEAYYLNKILEMQNELKQSRAVVTNVQAENERLSAVVQELKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYINLSDSHISISVDGLKFAEDGSEPNNDDKMNGHIHGPLGKLNGDYRTPTTRKGESLHPVSDLFSELNISEIQKLKQQLIQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQNSKEIKAELDCEKGRNSAEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTEEKTKYESKIQMYDEQVTNLEKTSKESGEKMAHMEKELQKMTGIANENHNTLNTAQDELVTFSEELAQLYHHVCLCNNETPNRVMLDYYRQSRVTRSGSLKGPDDPRGLLSPRLSRRGVSSPVESRTSSEPVSKENTETSKEPSPTKTPTISPVITAPPSSPVLDTSDIRKEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKLGKSKIGSPKIVSSLLPPYRHSAHN [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Mus musculus [Accession]=MF7000349 [Entry] [Entry number]=539 [Entry name]=C-terminal of Bicaudal D2 (human) [PDB ID]=6ofp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Protein bicaudal D [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:31306018). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000349,MF7000350,MF7000351 [UniProt ID chain A]=Q8TD16 [UniProt boundaries chain A]=715-801 [UniProt coverage chain A]=10% [Name chain A]=Protein bicaudal D homolog 2 [UniProt sequence chain A]=MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTPKKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREGQGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRAKAAPKTKPATPSL [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q8TD16 [UniProt boundaries chain B]=715-802 [UniProt coverage chain B]=10% [Name chain B]=Protein bicaudal D homolog 2 [UniProt sequence chain B]=MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTPKKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREGQGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRAKAAPKTKPATPSL [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.01 [Source organism]=Homo sapiens [Accession]=MF7000350 [Entry] [Entry number]=540 [Entry name]=C-terminal of Bicaudal D2, F684I mutant (Drosophila melanogaster) [PDB ID]=6tzw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Protein bicaudal D [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:32378283). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000349,MF7000350,MF7000351 [UniProt ID chain A]=P16568 [UniProt boundaries chain A]=666-740 [UniProt coverage chain A]=9% [Name chain A]=Protein bicaudal D [UniProt sequence chain A]=MSSASNNGPSADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTNKTGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREAKYALKKELDGHLNRESMYHISNLAYSIRSNMEDNASNNSDGEEENLALKRLEADLSTELKSPDGTKCDLFSEIHLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKKQIDVKEQGKEGGQKKDELEQQLRALISQYANWFTLSAKEIDGLKTDIAELQKGLNYTDATTTLRNEVTNLKNKLLATEQKSLDLQSDVQTLTHISQNAGQSLGSARSTLVALSDDLAQLYHLVCTVNGETPTRVLLDHKTDDMSFENDSLTAIQSQFKSDVFIAKPQIVEDLQGLADSVEIKKYVDTVSDQIKYLKTAVEHTIDMNKHKIRSEGGDALEKVNTEEMEELQEQIVKLKSLLSVKREQIGTLRNVLKSNKQTAEVALTNLKSKYENEKIIVSDTMSKLRNELRLLKEDAATFSSLRAMFAARCEEYVTQVDDLNRQLEAAEEEKKTLNQLLRLAVQQKLALTQRLEEMEMDREMRHVRRPMPAQRGTSGKSSFSTRPSSRNPASSNANPF [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=P16568 [UniProt boundaries chain B]=684-741 [UniProt coverage chain B]=7% [Name chain B]=Protein bicaudal D [UniProt sequence chain B]=MSSASNNGPSADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTNKTGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREAKYALKKELDGHLNRESMYHISNLAYSIRSNMEDNASNNSDGEEENLALKRLEADLSTELKSPDGTKCDLFSEIHLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKKQIDVKEQGKEGGQKKDELEQQLRALISQYANWFTLSAKEIDGLKTDIAELQKGLNYTDATTTLRNEVTNLKNKLLATEQKSLDLQSDVQTLTHISQNAGQSLGSARSTLVALSDDLAQLYHLVCTVNGETPTRVLLDHKTDDMSFENDSLTAIQSQFKSDVFIAKPQIVEDLQGLADSVEIKKYVDTVSDQIKYLKTAVEHTIDMNKHKIRSEGGDALEKVNTEEMEELQEQIVKLKSLLSVKREQIGTLRNVLKSNKQTAEVALTNLKSKYENEKIIVSDTMSKLRNELRLLKEDAATFSSLRAMFAARCEEYVTQVDDLNRQLEAAEEEKKTLNQLLRLAVQQKLALTQRLEEMEMDREMRHVRRPMPAQRGTSGKSSFSTRPSSRNPASSNANPF [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Drosophila melanogaster [Accession]=MF7000351 [Entry] [Entry number]=541 [Entry name]=Dimerization Domain of Sds3 [PDB ID]=4zqa [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:26124119). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q8BR65 [UniProt boundaries chain A]=90-172 [UniProt coverage chain A]=25% [Name chain A]=Sin3 histone deacetylase corepressor complex component SDS3 [UniProt sequence chain A]=MSAAGLLAPAPAPAAAPAAPEYYPEDEEELESAEDDERSCRGRESDEDTEDASETDLAKHDEEDYVEMKEQMYQDKLASLKRQLQQLQEGTLQEYQKRMKKLDQQYRERIRNAELFLQLETEQVERNYIKEKKAAVKEFEDKKVELKENLIAELEEKKKMIENEKLTMELTGDSMEVKPIMTRKLRRRPNDPVPIPDKRRKPAPAQLNYLLTDEQIMEDLRTLNKLKSPKRPASPSSPEHLPATPAESPAQRFEARIEDGKLYYDKRWYHKSQAIYLESKDNQKLSCVISSVGANEIWVRKTSDSTKMRIYVGQLQRGLFVIRRRSAA [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=Q8BR65 [UniProt boundaries chain A-2]=90-172 [UniProt coverage chain A-2]=25% [Name chain A-2]=Sin3 histone deacetylase corepressor complex component SDS3 [UniProt sequence chain A-2]=MSAAGLLAPAPAPAAAPAAPEYYPEDEEELESAEDDERSCRGRESDEDTEDASETDLAKHDEEDYVEMKEQMYQDKLASLKRQLQQLQEGTLQEYQKRMKKLDQQYRERIRNAELFLQLETEQVERNYIKEKKAAVKEFEDKKVELKENLIAELEEKKKMIENEKLTMELTGDSMEVKPIMTRKLRRRPNDPVPIPDKRRKPAPAQLNYLLTDEQIMEDLRTLNKLKSPKRPASPSSPEHLPATPAESPAQRFEARIEDGKLYYDKRWYHKSQAIYLESKDNQKLSCVISSVGANEIWVRKTSDSTKMRIYVGQLQRGLFVIRRRSAA [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Mus musculus [Accession]=MF7000352 [Entry] [Entry number]=542 [Entry name]=PC4 homolog BPSL1147 [PDB ID]=5a4n [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=PC4-like fold [Sequence domain]=Transcriptional Coactivator p15 (PC4) [Evidence level]=Direct evidence [Evidence text]=In PC4 fold dimers there is beta sheet augmentation as well as coiled coil formation by helices from the two different monomers. The interface is quite large and there are many inter-chain hydrogen bonds and salt bridges, most of them are formed by conserved residues (PMID:22948907, PMID:24029071). The guanidine hydrochloride induced unfolding of PC4 (monitored using fluorescence) was best fitted to a two-state model (PMID:34534740). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000282,MF7000281,MF7000915,MF7000353 [UniProt ID chain A]=Q63VU8 [UniProt boundaries chain A]=6-73 [UniProt coverage chain A]=90% [Name chain A]=Transcriptional coactivator p15 (PC4) C-terminal domain-containing protein [UniProt sequence chain A]=MSAYDSGKTIADVQKSATQRIRISHRWYRGRRYVDVRLVVVDRDGDFVPTRQGISIRPELLAQVIQGLLLASREG [Source organism chain A]=Burkholderia pseudomallei [UniProt ID chain B]=Q63VU8 [UniProt boundaries chain B]=6-73 [UniProt coverage chain B]=90% [Name chain B]=Transcriptional coactivator p15 (PC4) C-terminal domain-containing protein [UniProt sequence chain B]=MSAYDSGKTIADVQKSATQRIRISHRWYRGRRYVDVRLVVVDRDGDFVPTRQGISIRPELLAQVIQGLLLASREG [Source organism chain B]=Burkholderia pseudomallei [ExpTech]=X-ray [Resolution]=1.96 [Source organism]=Burkholderia pseudomallei [Accession]=MF7000353 [Entry] [Entry number]=544 [Entry name]=N-terminal domain of H-NS family protein TurB [PDB ID]=5b52 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:27709616). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q88GF9 [UniProt boundaries chain A]=4-60 [UniProt coverage chain A]=47% [Name chain A]=H-NS family protein MvaT [UniProt sequence chain A]=MSRLAEFRAAEKALQEQMAQLEALKKDAGLKREIEFEQKLVGLMKSYDKSLRDIIAILDPKAVARASSTPPKQQRRPRVVKVYQNPHTGERIETKGGNHRGLKAWKEQYGAATVESWVR [Source organism chain A]=/ KT2440) [UniProt ID chain B]=Q88GF9 [UniProt boundaries chain B]=3-61 [UniProt coverage chain B]=49% [Name chain B]=H-NS family protein MvaT [UniProt sequence chain B]=MSRLAEFRAAEKALQEQMAQLEALKKDAGLKREIEFEQKLVGLMKSYDKSLRDIIAILDPKAVARASSTPPKQQRRPRVVKVYQNPHTGERIETKGGNHRGLKAWKEQYGAATVESWVR [Source organism chain B]=/ KT2440) [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=/ KT2440) [Accession]=MF7000355 [Entry] [Entry number]=545 [Entry name]=Coiled coil domain of GEMC1 [PDB ID]=5c9n [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:26527144). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=A6NCL1 [UniProt boundaries chain A]=69-132 [UniProt coverage chain A]=19% [Name chain A]=Geminin coiled-coil domain-containing protein 1 [UniProt sequence chain A]=MNTILPCQDQYFVGGQSYNCPYSTTTSESSVDVSTETWVSFWAAGLLDNRELQQAPQAQESFSDSNFPLPDLCSWEEAQLSSQLYRNKQLQDTLVQKEEELARLHEENNHLRQYLNSALVKCLEEKAKKLLSSDEFSKAYGKFRKGKRKSKEQRYSPAEIPHPKNAKRNLSSEFANCEEQAGPPVDPWVLQTLGLKDLDTIDDTSSANYSALASHPRRVASTFSQFPDDAVDYKNIPREDMPIDYRGDRTTPLHSTATHGEDFHILSQLSNPPVGLKTLPYYTAHVSPNKTEMAFSTSLSPHCNVKTHSFHQGQAFVRRDEEGGWKFTWVPKQS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=A6NCL1 [UniProt boundaries chain B]=69-129 [UniProt coverage chain B]=18% [Name chain B]=Geminin coiled-coil domain-containing protein 1 [UniProt sequence chain B]=MNTILPCQDQYFVGGQSYNCPYSTTTSESSVDVSTETWVSFWAAGLLDNRELQQAPQAQESFSDSNFPLPDLCSWEEAQLSSQLYRNKQLQDTLVQKEEELARLHEENNHLRQYLNSALVKCLEEKAKKLLSSDEFSKAYGKFRKGKRKSKEQRYSPAEIPHPKNAKRNLSSEFANCEEQAGPPVDPWVLQTLGLKDLDTIDDTSSANYSALASHPRRVASTFSQFPDDAVDYKNIPREDMPIDYRGDRTTPLHSTATHGEDFHILSQLSNPPVGLKTLPYYTAHVSPNKTEMAFSTSLSPHCNVKTHSFHQGQAFVRRDEEGGWKFTWVPKQS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Homo sapiens [Accession]=MF7000356 [Entry] [Entry number]=547 [Entry name]=Kinesin-3 KIF13A NC-CC1, mutant [PDB ID]=5djn [Chains]=C,A [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:26680000). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain C]=N/A [Similar structures]=None [UniProt ID chain A]=F8VQ75 [UniProt boundaries chain A]=362-439 [UniProt coverage chain A]=4% [Name chain A]=Kinesin family member 13A [UniProt sequence chain A]=MSDTKVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPPSNTKQGERKPPKVFAFDYCFWSMDESNTTKYAGQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFQRIALEQNESQTFKVEVSYMEIYNEKVRDLLDPKGSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGKGKNKFVPYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNEDPNAKVIRELREEVEKLREQLSQAEAMKAPELKEKLEESEKLIKELTVTWEEKLRKTEAIAQERQRQLESMGISLETSGIKVGDDKCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCEIDIAADGDITLTPKENARSCVNGTLVCSTTQLWHGDRILWGNNHFFRINLPKRKRRDWLKDFERETSSAEHDLDAASEASSEPDYNYEFAQMEVIMKTLNSNDPVQNVVQVLEKQYLEEKRTALEEQRLMYERELEQLRQQLSPERQPPSSASDRLAYSSQTAQQKVTQWAEERDELFRQSLAKLREQLVKANTLVREANFLAEEMSKLTDYQVTLQIPAANLSANRKRGAIVSEPAIQARRKGKGTQVWTIEKLENKLIDMRDLYQEWKENVPEAKRLYGKRGDPFYEAQENHNLIGVANVFLECLFCDVKLQYAVPIISQQGEVAGRLHVEVTRITGTIPERMAEDDSSENSSESGSLEVVDSSGEVIHRVKKLTCRVIIKEATGLPISLSNFVFCQYTFWDQCESTVAAPVVDPDVPSPQSKDAQYTVTFSHCKDYVVTVTEEFLEFISDGALAIEVWGHRCAGNGSPIWEVDSLHAKTRTLHDRWNEVTRRIEVWISILELNELGDYAAVELHQAKDVNTGGVFQLRQGHSRRVQVTVKPVQHSGTLPLMVEAILSVSIGCVTARSTKLQRGLDSYQEEDLNCVRERWSDALIKRREYLDEQIKKVSNKKEKTEDDMEREARLVEQWVGLTEERNAVLVPAPGSGIPGAPADWVPPPGMETHIPVLFLDLNADDLSANEQLVGPHASGVNSILPKEHGSQFFYLPIIKHSDDEVSATASWDSSVHDSLHLNRVTPQNERIYLIVKTTVQLSHPAAMELVLRKRIAANIYNKQSFTQSLKRRISLINICYSCGVTYEIVSNIPKATEEIEDRETLALLAARSENEGTLDGETYIEKYTRGVLQVENILSLERLRQAVTVKEALSTKARHIRRSLSTPNVHNVSSSRPDLSGFDEDDKGWPENQLDVSDYSSSYQDVACYGTLPRDSPRRSKEGCPSENPHALTVSPFKAFSPQPPKFFKPLMPVKEEHKKRLALEARPLLSQEDSEEEENELEALSRKLMLTQPYVPVEFADFSVYNASLENREWSSSKADLTDSRALEKAVSRSPTTSSLTSGYFSHSASNATLSDMAVPSSDSSDQLAVSTKEVECAEPPGPSLAPDVRPASNQELTEVGRGSGKDETIAVPLEENSALPKGTPSPQSIPEESSRMPCRTASCSELDVGPSKDGHQAREFCPGEVTIEHTTNILEDHSFTEFMGVSDGKDFDGLADCSVGEPSRRRALTNETDHKGIPERPPDADRLHPKIENDQEATATR [Source organism chain A]=Mus musculus [UniProt ID chain C]=F8VQ75 [UniProt boundaries chain C]=360-441 [UniProt coverage chain C]=4% [Name chain C]=Kinesin family member 13A [UniProt sequence chain C]=MSDTKVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPPSNTKQGERKPPKVFAFDYCFWSMDESNTTKYAGQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFQRIALEQNESQTFKVEVSYMEIYNEKVRDLLDPKGSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGKGKNKFVPYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNEDPNAKVIRELREEVEKLREQLSQAEAMKAPELKEKLEESEKLIKELTVTWEEKLRKTEAIAQERQRQLESMGISLETSGIKVGDDKCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCEIDIAADGDITLTPKENARSCVNGTLVCSTTQLWHGDRILWGNNHFFRINLPKRKRRDWLKDFERETSSAEHDLDAASEASSEPDYNYEFAQMEVIMKTLNSNDPVQNVVQVLEKQYLEEKRTALEEQRLMYERELEQLRQQLSPERQPPSSASDRLAYSSQTAQQKVTQWAEERDELFRQSLAKLREQLVKANTLVREANFLAEEMSKLTDYQVTLQIPAANLSANRKRGAIVSEPAIQARRKGKGTQVWTIEKLENKLIDMRDLYQEWKENVPEAKRLYGKRGDPFYEAQENHNLIGVANVFLECLFCDVKLQYAVPIISQQGEVAGRLHVEVTRITGTIPERMAEDDSSENSSESGSLEVVDSSGEVIHRVKKLTCRVIIKEATGLPISLSNFVFCQYTFWDQCESTVAAPVVDPDVPSPQSKDAQYTVTFSHCKDYVVTVTEEFLEFISDGALAIEVWGHRCAGNGSPIWEVDSLHAKTRTLHDRWNEVTRRIEVWISILELNELGDYAAVELHQAKDVNTGGVFQLRQGHSRRVQVTVKPVQHSGTLPLMVEAILSVSIGCVTARSTKLQRGLDSYQEEDLNCVRERWSDALIKRREYLDEQIKKVSNKKEKTEDDMEREARLVEQWVGLTEERNAVLVPAPGSGIPGAPADWVPPPGMETHIPVLFLDLNADDLSANEQLVGPHASGVNSILPKEHGSQFFYLPIIKHSDDEVSATASWDSSVHDSLHLNRVTPQNERIYLIVKTTVQLSHPAAMELVLRKRIAANIYNKQSFTQSLKRRISLINICYSCGVTYEIVSNIPKATEEIEDRETLALLAARSENEGTLDGETYIEKYTRGVLQVENILSLERLRQAVTVKEALSTKARHIRRSLSTPNVHNVSSSRPDLSGFDEDDKGWPENQLDVSDYSSSYQDVACYGTLPRDSPRRSKEGCPSENPHALTVSPFKAFSPQPPKFFKPLMPVKEEHKKRLALEARPLLSQEDSEEEENELEALSRKLMLTQPYVPVEFADFSVYNASLENREWSSSKADLTDSRALEKAVSRSPTTSSLTSGYFSHSASNATLSDMAVPSSDSSDQLAVSTKEVECAEPPGPSLAPDVRPASNQELTEVGRGSGKDETIAVPLEENSALPKGTPSPQSIPEESSRMPCRTASCSELDVGPSKDGHQAREFCPGEVTIEHTTNILEDHSFTEFMGVSDGKDFDGLADCSVGEPSRRRALTNETDHKGIPERPPDADRLHPKIENDQEATATR [Source organism chain C]=Mus musculus [ExpTech]=X-ray [Resolution]=2.82 [Source organism]=Mus musculus [Accession]=MF7000358 [Entry] [Entry number]=548 [Entry name]=CC1-FHA tandem of Kinesin-3 KIF13A [PDB ID]=5djo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Coiled coil dimerization and FHA domains [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=A substantial part of the structure is a coiled coil dimerization region (PMID:26680000). Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815).The complex structure contains an extended coiled coil dimerization subdomain, the "stalk", and folded FHA domains, "the head". [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9EQW7 [UniProt boundaries chain A]=387-544 [UniProt coverage chain A]=9% [Name chain A]=Kinesin-like protein KIF13A [UniProt sequence chain A]=MSDTKVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPPSNTKQGERKPPKVFAFDYCFWSMDESNTTKYAGQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFQRIALEQNESQTFKVEVSYMEIYNEKVRDLLDPKGSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGKGKNKFVPYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNEDPNAKVIRELREEVEKLREQLSKAEAMKPPELKEKLEESEKLIKELTVTWEEKLRKTEAIAQERQRQLESMGISLETSGIKVGDDKCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCEIDIAADGDITLTPKENARSCVNGTLVCNTTQLWHGDRILWGNNHFFRINLPKRKRRDWLKDFERETSSAEHDLDAASEASSEPDYNYEFAQMEVIMKTLNSNDPVQNVVQVLEKQYLEEKRTALEEQRLMYERELEQLRQQLSPERQPPSSASDRLAYSSQTAQQKVTQWAEERDELFRQSLAKLREQLVKANTLVREANFLAEEMSKLTDYQVTLQIPAANLSANRKRGAIVSEPAIQARRKGKGTQVWTIEKLENKLIDMRDLYQEWKENVPEAKRLYGKRGDPFYEAQENHNLIGVANVFLECLFCDVKLQYAVPIISQQGEVAGRLHVEVTRITGTIPERMAEDDSSENSSESGSLEVVDSSGEVIHRVKKLTCRVIIKEATGLPISLSNFVFCQYTFWDQCESTVAAPVVDPDVPSPQSKDAQYTVTFSHCKDYVVTVTEEFLEFISDGALAIEVWGHRCAGNGSPIWEVDSLHAKTRTLHDRWNEVTRRIEVWISILELNELGDYAAVELHQAKDVNTGGVFQLRQGHSRRVQVTVKPVQHSGTLPLMVEAILSVSIGCVTARSTKLQRGLDSYQEEDLNCVRERWSDALIKRREYLDEQIKKVSNKKEKTEDDMEREARLVEQWVGLTEERNAVLVPAPGSGIPGAPADWVPPPGMETHIPVLFLDLNADDLSANEQLVGPHASGVNSILPKEHGSQFFYLPIIKHSDDEVSATASWDSSVHDSLHLNRVTPQNERIYLIVKTTVQLSHPAAMELVLRKRIAANIYNKQSFTQSLKRRISLINICYSCGVTYEIVSNIPKATEEIEDRETLALLAARSENEGTLDGETYIEKYTRGVLQVENILSLERLRQAVTVKEALSTKARHIRRSLSTPNVHNVSSSRPDLSGFDEDDKGWPENQLDVSDYSSSYQDVACYGTLPRDSPRRSKEGCPSENPHALTVSPFKAFSPQPPKFFKPLMPVKEEHKKRLALEARPLLSQEDSEEEENELEALSRKLMLTQPYVPVEFADFSVYNASLENREWSSSKADLTDSRALEKAVSRSPTTSSLTSGYFSHSASNATLSDMAVPSSDSSDQLAVSTKEVECAEPPGPSLAPDVRRASNQELTEVGRGSGKDETIAVPLEENSALPKGTPSPQSIPEESSRMPCRTASCSELDVGPSKDGHQAREFCPGEVTIEHTTNILEDHSFTEFMGVSDGKDFDGLADCSVGEPSRRRALTNETDHKGIPERPPDADRLHPKIENDQEATATR [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9EQW7 [UniProt boundaries chain B]=386-544 [UniProt coverage chain B]=9% [Name chain B]=Kinesin-like protein KIF13A [UniProt sequence chain B]=MSDTKVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPPSNTKQGERKPPKVFAFDYCFWSMDESNTTKYAGQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFQRIALEQNESQTFKVEVSYMEIYNEKVRDLLDPKGSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGKGKNKFVPYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNEDPNAKVIRELREEVEKLREQLSKAEAMKPPELKEKLEESEKLIKELTVTWEEKLRKTEAIAQERQRQLESMGISLETSGIKVGDDKCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCEIDIAADGDITLTPKENARSCVNGTLVCNTTQLWHGDRILWGNNHFFRINLPKRKRRDWLKDFERETSSAEHDLDAASEASSEPDYNYEFAQMEVIMKTLNSNDPVQNVVQVLEKQYLEEKRTALEEQRLMYERELEQLRQQLSPERQPPSSASDRLAYSSQTAQQKVTQWAEERDELFRQSLAKLREQLVKANTLVREANFLAEEMSKLTDYQVTLQIPAANLSANRKRGAIVSEPAIQARRKGKGTQVWTIEKLENKLIDMRDLYQEWKENVPEAKRLYGKRGDPFYEAQENHNLIGVANVFLECLFCDVKLQYAVPIISQQGEVAGRLHVEVTRITGTIPERMAEDDSSENSSESGSLEVVDSSGEVIHRVKKLTCRVIIKEATGLPISLSNFVFCQYTFWDQCESTVAAPVVDPDVPSPQSKDAQYTVTFSHCKDYVVTVTEEFLEFISDGALAIEVWGHRCAGNGSPIWEVDSLHAKTRTLHDRWNEVTRRIEVWISILELNELGDYAAVELHQAKDVNTGGVFQLRQGHSRRVQVTVKPVQHSGTLPLMVEAILSVSIGCVTARSTKLQRGLDSYQEEDLNCVRERWSDALIKRREYLDEQIKKVSNKKEKTEDDMEREARLVEQWVGLTEERNAVLVPAPGSGIPGAPADWVPPPGMETHIPVLFLDLNADDLSANEQLVGPHASGVNSILPKEHGSQFFYLPIIKHSDDEVSATASWDSSVHDSLHLNRVTPQNERIYLIVKTTVQLSHPAAMELVLRKRIAANIYNKQSFTQSLKRRISLINICYSCGVTYEIVSNIPKATEEIEDRETLALLAARSENEGTLDGETYIEKYTRGVLQVENILSLERLRQAVTVKEALSTKARHIRRSLSTPNVHNVSSSRPDLSGFDEDDKGWPENQLDVSDYSSSYQDVACYGTLPRDSPRRSKEGCPSENPHALTVSPFKAFSPQPPKFFKPLMPVKEEHKKRLALEARPLLSQEDSEEEENELEALSRKLMLTQPYVPVEFADFSVYNASLENREWSSSKADLTDSRALEKAVSRSPTTSSLTSGYFSHSASNATLSDMAVPSSDSSDQLAVSTKEVECAEPPGPSLAPDVRRASNQELTEVGRGSGKDETIAVPLEENSALPKGTPSPQSIPEESSRMPCRTASCSELDVGPSKDGHQAREFCPGEVTIEHTTNILEDHSFTEFMGVSDGKDFDGLADCSVGEPSRRRALTNETDHKGIPERPPDADRLHPKIENDQEATATR [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.74 [Source organism]=Mus musculus [Accession]=MF7000359 [Entry] [Entry number]=549 [Entry name]=Microtubule-binding domain of CEP135 [PDB ID]=5fcn [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=CEP135 [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:27477386). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000360,MF7000361 [UniProt ID chain B]=Q66GS9 [UniProt boundaries chain B]=82-132 [UniProt coverage chain B]=4% [Name chain B]=Centrosomal protein of 135 kDa [UniProt sequence chain B]=MTTAVERKYINIRKRLDQLGYRQTLTVECLPLVEKLFSDLVHTTESLRQSKLSAVKAEKESANFDFVLEPYKLENARLSRENNELYLELMKLREHSDQHVKELKTSLKKCARETADLKFLNNQYAHKLKLLEKESKAKNERIQQLQEKNLHAVVQTPGGKKRSIAFRRQRMQIDEPVPPSEVSSYPVPQPDDPYIADLLQVADNRIQELQQEVHQLQEKLAMMESGVRDYSKQIELREREIERLSVALDGGRSPDVLSLESRNKTNEKLIAHLNIQVDFLQQANKDLEKRIRELMETKETVTSEVVNLSNKNEKLCQELTEIDQLAQQLERHKEEVLETADKELGEAKKEIKRKLSEMQDLEETMAKLQLELNLCQKEKERLSDELLVKSDLETVVHQLEQEKQRLSKKVESFAVTERQLTLEVERMRLEHGIKRRDRSPSRLDTFLKGIEEERDYYKKELERLQHIIQRRSCSTSYSAREKSSIFRTPEKGDYNSEIHQITRERDELQRMLERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQTTAPHNIVSLMEKEKELALSDLRRIMAEKEALREKLEHIEEVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLATNRDKEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTERYERERAIQEMRRHGLATPPLSSTLRSPSHSPEHRNV [Source organism chain B]=Homo sapiens [UniProt ID chain A]=Q66GS9 [UniProt boundaries chain A]=82-133 [UniProt coverage chain A]=4% [Name chain A]=Centrosomal protein of 135 kDa [UniProt sequence chain A]=MTTAVERKYINIRKRLDQLGYRQTLTVECLPLVEKLFSDLVHTTESLRQSKLSAVKAEKESANFDFVLEPYKLENARLSRENNELYLELMKLREHSDQHVKELKTSLKKCARETADLKFLNNQYAHKLKLLEKESKAKNERIQQLQEKNLHAVVQTPGGKKRSIAFRRQRMQIDEPVPPSEVSSYPVPQPDDPYIADLLQVADNRIQELQQEVHQLQEKLAMMESGVRDYSKQIELREREIERLSVALDGGRSPDVLSLESRNKTNEKLIAHLNIQVDFLQQANKDLEKRIRELMETKETVTSEVVNLSNKNEKLCQELTEIDQLAQQLERHKEEVLETADKELGEAKKEIKRKLSEMQDLEETMAKLQLELNLCQKEKERLSDELLVKSDLETVVHQLEQEKQRLSKKVESFAVTERQLTLEVERMRLEHGIKRRDRSPSRLDTFLKGIEEERDYYKKELERLQHIIQRRSCSTSYSAREKSSIFRTPEKGDYNSEIHQITRERDELQRMLERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQTTAPHNIVSLMEKEKELALSDLRRIMAEKEALREKLEHIEEVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLATNRDKEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTERYERERAIQEMRRHGLATPPLSSTLRSPSHSPEHRNV [Source organism chain A]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF7000360 [Entry] [Entry number]=550 [Entry name]=Microtubule-binding domain of CEP135 [PDB ID]=5ng4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=CEP135 [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:30135143). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000360,MF7000361 [UniProt ID chain A]=Q66GS9 [UniProt boundaries chain A]=82-134 [UniProt coverage chain A]=4% [Name chain A]=Centrosomal protein of 135 kDa [UniProt sequence chain A]=MTTAVERKYINIRKRLDQLGYRQTLTVECLPLVEKLFSDLVHTTESLRQSKLSAVKAEKESANFDFVLEPYKLENARLSRENNELYLELMKLREHSDQHVKELKTSLKKCARETADLKFLNNQYAHKLKLLEKESKAKNERIQQLQEKNLHAVVQTPGGKKRSIAFRRQRMQIDEPVPPSEVSSYPVPQPDDPYIADLLQVADNRIQELQQEVHQLQEKLAMMESGVRDYSKQIELREREIERLSVALDGGRSPDVLSLESRNKTNEKLIAHLNIQVDFLQQANKDLEKRIRELMETKETVTSEVVNLSNKNEKLCQELTEIDQLAQQLERHKEEVLETADKELGEAKKEIKRKLSEMQDLEETMAKLQLELNLCQKEKERLSDELLVKSDLETVVHQLEQEKQRLSKKVESFAVTERQLTLEVERMRLEHGIKRRDRSPSRLDTFLKGIEEERDYYKKELERLQHIIQRRSCSTSYSAREKSSIFRTPEKGDYNSEIHQITRERDELQRMLERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQTTAPHNIVSLMEKEKELALSDLRRIMAEKEALREKLEHIEEVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLATNRDKEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTERYERERAIQEMRRHGLATPPLSSTLRSPSHSPEHRNV [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q66GS9 [UniProt boundaries chain B]=82-127 [UniProt coverage chain B]=4% [Name chain B]=Centrosomal protein of 135 kDa [UniProt sequence chain B]=MTTAVERKYINIRKRLDQLGYRQTLTVECLPLVEKLFSDLVHTTESLRQSKLSAVKAEKESANFDFVLEPYKLENARLSRENNELYLELMKLREHSDQHVKELKTSLKKCARETADLKFLNNQYAHKLKLLEKESKAKNERIQQLQEKNLHAVVQTPGGKKRSIAFRRQRMQIDEPVPPSEVSSYPVPQPDDPYIADLLQVADNRIQELQQEVHQLQEKLAMMESGVRDYSKQIELREREIERLSVALDGGRSPDVLSLESRNKTNEKLIAHLNIQVDFLQQANKDLEKRIRELMETKETVTSEVVNLSNKNEKLCQELTEIDQLAQQLERHKEEVLETADKELGEAKKEIKRKLSEMQDLEETMAKLQLELNLCQKEKERLSDELLVKSDLETVVHQLEQEKQRLSKKVESFAVTERQLTLEVERMRLEHGIKRRDRSPSRLDTFLKGIEEERDYYKKELERLQHIIQRRSCSTSYSAREKSSIFRTPEKGDYNSEIHQITRERDELQRMLERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQTTAPHNIVSLMEKEKELALSDLRRIMAEKEALREKLEHIEEVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLATNRDKEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTERYERERAIQEMRRHGLATPPLSSTLRSPSHSPEHRNV [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.14 [Source organism]=Homo sapiens [Accession]=MF7000361 [Entry] [Entry number]=552 [Entry name]=Bacteriophage AP205 coat protein [PDB ID]=5fs4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Leviviridae coat protein fold [Sequence domain]=AP205 coat protein [Evidence level]=Direct evidence [Evidence text]=Functionally, the coat protein does not exist as a monomer but engages in very strong dimeric interactions (PMID:27591890). Intertwined dimer with beta sheet augmentation between the monomers. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000364,MF7000363 [UniProt ID chain A]=Q9AZ42 [UniProt boundaries chain A]=1-130 [UniProt coverage chain A]=99% [Name chain A]=Coat protein [UniProt sequence chain A]=MANKPMQPITSTANKIVWSDPTRLSTTFSASLLRQRVKVGIAELNNVSGQYVSVYKRPAPKPEGCADACVIMPNENQSIRTVISGSAENLATLKAEWETHKRNVDTLFASGNAGLGFLDPTAAIVSSDTTA [Source organism chain A]=Acinetobacter phage AP205 [UniProt ID chain B]=Q9AZ42 [UniProt boundaries chain B]=1-130 [UniProt coverage chain B]=99% [Name chain B]=Coat protein [UniProt sequence chain B]=MANKPMQPITSTANKIVWSDPTRLSTTFSASLLRQRVKVGIAELNNVSGQYVSVYKRPAPKPEGCADACVIMPNENQSIRTVISGSAENLATLKAEWETHKRNVDTLFASGNAGLGFLDPTAAIVSSDTTA [Source organism chain B]=Acinetobacter phage AP205 [ExpTech]=X-ray [Resolution]=1.73 [Source organism]=Acinetobacter phage AP205 [Accession]=MF7000363 [Entry] [Entry number]=553 [Entry name]=Acinetobacter phage 205 (AP205) coat protein [PDB ID]=5jzr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Leviviridae coat protein fold [Sequence domain]=AP205 coat protein [Evidence level]=Direct evidence [Evidence text]=Functionally, the coat protein does not exist as a monomer but engages in very strong dimeric interactions (PMID:27591890). Intertwined dimer with beta sheet augmentation between the monomers. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000364,MF7000363 [UniProt ID chain A]=Q9AZ42 [UniProt boundaries chain A]=1-131 [UniProt coverage chain A]=100% [Name chain A]=Coat protein [UniProt sequence chain A]=MANKPMQPITSTANKIVWSDPTRLSTTFSASLLRQRVKVGIAELNNVSGQYVSVYKRPAPKPEGCADACVIMPNENQSIRTVISGSAENLATLKAEWETHKRNVDTLFASGNAGLGFLDPTAAIVSSDTTA [Source organism chain A]=Acinetobacter phage AP205 [UniProt ID chain B]=Q9AZ42 [UniProt boundaries chain B]=1-131 [UniProt coverage chain B]=100% [Name chain B]=Coat protein [UniProt sequence chain B]=MANKPMQPITSTANKIVWSDPTRLSTTFSASLLRQRVKVGIAELNNVSGQYVSVYKRPAPKPEGCADACVIMPNENQSIRTVISGSAENLATLKAEWETHKRNVDTLFASGNAGLGFLDPTAAIVSSDTTA [Source organism chain B]=Acinetobacter phage AP205 [ExpTech]=Solid state NMR [Resolution]=N/A [Source organism]=Acinetobacter phage AP205 [Accession]=MF7000364 [Entry] [Entry number]=555 [Entry name]=Hit1p-Rsa1p complex (Saccharomyces cerevisiae) [PDB ID]=2mjf [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Pac-Hit fold domain + enclosed helix [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Large relative interaction surface. Intricate interaction of Rsa1p with Hit1p. Thus helix α1′ of the Rsa1p320−334 forms the architectural base for the heterodimeric complex (PMID:25170085). The amino acids involved in the interaction are required for both the stability and solubility of both partners (PMID:25170085). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q08932 [UniProt boundaries chain A]=317-352 [UniProt coverage chain A]=9% [Name chain A]=Ribosome assembly 1 protein [UniProt sequence chain A]=MNYNNFENSKGDGHSRLPKPTYSGTLSDGYDESKIKRQKTDSAFNAAYSPHMYPNSPYYEGSWNTGYTPQLHHVAPHNQYFHPIQPSTQYNYTSPPNYTENYIPPVHQNISYAPALNLQKWPSSYCENTQALKNDKDYQTSISYEDVAIPTVKEIQLIEKNRGKDTFMNEISPVPSSKDQASAEPTEIPRKDPELANSNAEDDHNNLGLEDDDRDEQLESEGLGKVVLVPGTSIALITDEDVKKWREERKKMWLLKISNNKQKHMQEMGIKEDELKSQPSIFKESRKEKQFIQSIQNQVQRGNPKIDLNLKLIQREFANENSQLLDFIRELGDVGLLEYELSQQEKDVLFGSSEDNNKNHYKPNYKNRKPNLSRANFTRNK [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P46973 [UniProt boundaries chain B]=70-164 [UniProt coverage chain B]=57% [Name chain B]=Protein HIT1 [UniProt sequence chain B]=MVSSAVKCGICRGVDGKYKCPKCGVRYCSLKCYKDAAKHVHKESEQPRAGTEANVEVVNNDKIINSSLAMNKTLKTKAFDDIYQNSAELQELLKYNTVKFHLAKVYRILSSTVNDGSSGKMNSDLQKELAVNYLNTLRYGGIHYNEAIEEFCQILLDKLNAVKK [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000366 [Entry] [Entry number]=556 [Entry name]=MIS12 complex Head2 subdomain (DSN1-NSL1) [PDB ID]=5lsi [Chains]=E,D [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. Large relative interaction surface. The partners form helical hairpins that interact in a four-helix bundle, together forming the Head2 domain (PMID:27881301). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain D]=N/A [Evidence chain E]=N/A [Similar structures]=None [UniProt ID chain D]=Q9H410 [UniProt boundaries chain D]=116-197 [UniProt coverage chain D]=23% [Name chain D]=Kinetochore-associated protein DSN1 homolog [UniProt sequence chain D]=MTSVTRSEIIDEKGPVMSKTHDHQLESSLSPVEVFAKTSASLEMNQGVSEERIHLGSSPKKGGNCDLSHQERLQSKSLHLSPQEQSASYQDRRQSWRRASMKETNRRKSLHPIHQGITELSRSISVDLAESKRLGCLLLSSFQFSIQKLEPFLRDTKGFSLESFRAKASSLSEELKHFADGLETDGTLQKCFEDSNGKASDFSLEASVAEMKEYITKFSLERQTWDQLLLHYQQEAKEILSRGSTEAKITEVKVEPMTYLGSSQNEVLNTKPDYQKILQNQSKVFDCMELVMDELQGSVKQLQAFMDESTQCFQKVSVQLGKRSMQQLDPSPARKLLKLQLQNPPAIHGSGSGSCQ [Source organism chain D]=Homo sapiens [UniProt ID chain E]=Q96IY1 [UniProt boundaries chain E]=29-99 [UniProt coverage chain E]=25% [Name chain E]=Kinetochore-associated protein NSL1 homolog [UniProt sequence chain E]=MAGSPELVVLDPPWDKELAAGTESQALVSATPREDFRVRCTSKRAVTEMLQLCGRFVQKLGDALPEEIREPALRDAQWTFESAVQENISINGQAWQEASDNCFMDSDIKVLEDQFDEIIVDIATKRKQYPRKILECVIKTIKAKQEILKQYHPVVHPLDLKYDPDPAPHMENLKCRGETVAKEISEAMKSLPALIEQGEGFSQVLRMQPVIHLQRIHQEVFSSCHRKPDAKPENFITQIETTPTETASRKTSDMVLKRKQTKDCPQRKWYPLRPKKINLDT [Source organism chain E]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000367 [Entry] [Entry number]=558 [Entry name]=Prp19/Pso4 (spliceosome component) [PDB ID]=5m88 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=U-box domain and C-terminal coiled coil dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=A substantial part of the structure is a coiled coil dimerization region. Coiled coils are highly versatile folding units (PMID:11166216), showing cooperative binding and folding (PMID:9811815). There are two independently folded U-box domains and a coiled coil dimerization domain. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=G0SFY0 [UniProt boundaries chain A]=1-134 [UniProt coverage chain A]=27% [Name chain A]=Pre-mRNA-processing factor 19 [UniProt sequence chain A]=MLCALSGEIPEEPVVSKKTGVLFEKRLILKYLEEHNNIEPGTTEELDPETDLLPIKTSRVVRPRPPNFTSIPSLLKAFQDEWDALVLETYTTREQLARVREELATALYQHDAAVRVIARLTRERDEAREALARLTVTGAAPAAQNGEAMAVDSESLSEGLVEHVNEVQQQLMKTRKKRPIPQGWATADDVAALQQVAYTDLNVTQASSLDLENECAAVGGLDGKLDIYSVVANKVERTLDIGEPVTATEWTGTKVVIGTAKGWVKVYDAGRESATFQTHAGPVTGLAVHPGGRILASVGVDKSFVFYDLETGERVARGYADAALTTCAFHPDGNLFAAGTQTGHILVFHTTTLEQAESFPLGTPIQALAFSENGFWFAATGKGTSSVTIFDLRKSGAAAAVKELQTGEVLSISWDYTGQYLATGGGTGVTVQMYTKATKSWSEPVRLGMPVVGVKWGGEAKRLVVVSREGVVSVLGKKEE [Source organism chain A]= [UniProt ID chain B]=G0SFY0 [UniProt boundaries chain B]=1-134 [UniProt coverage chain B]=27% [Name chain B]=Pre-mRNA-processing factor 19 [UniProt sequence chain B]=MLCALSGEIPEEPVVSKKTGVLFEKRLILKYLEEHNNIEPGTTEELDPETDLLPIKTSRVVRPRPPNFTSIPSLLKAFQDEWDALVLETYTTREQLARVREELATALYQHDAAVRVIARLTRERDEAREALARLTVTGAAPAAQNGEAMAVDSESLSEGLVEHVNEVQQQLMKTRKKRPIPQGWATADDVAALQQVAYTDLNVTQASSLDLENECAAVGGLDGKLDIYSVVANKVERTLDIGEPVTATEWTGTKVVIGTAKGWVKVYDAGRESATFQTHAGPVTGLAVHPGGRILASVGVDKSFVFYDLETGERVARGYADAALTTCAFHPDGNLFAAGTQTGHILVFHTTTLEQAESFPLGTPIQALAFSENGFWFAATGKGTSSVTIFDLRKSGAAAAVKELQTGEVLSISWDYTGQYLATGGGTGVTVQMYTKATKSWSEPVRLGMPVVGVKWGGEAKRLVVVSREGVVSVLGKKEE [Source organism chain B]= [ExpTech]=X-ray [Resolution]=2.80 [Source organism]= [Accession]=MF7000369 [Entry] [Entry number]=559 [Entry name]=HLHLZ domain of TFEB [PDB ID]=7y62 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Basic helix-loop-helix (bHLH) [Sequence domain]=Helix-loop-helix DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294, PMID:9488706). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100009,MF2110021,MF2110023,MF2100010,MF7000192,MF7000402,MF7000403,MF7000444,MF7000371 [UniProt ID chain A]=P19484 [UniProt boundaries chain A]=248-319 [UniProt coverage chain A]=15% [Name chain A]=Transcription factor EB [UniProt sequence chain A]=MASRIGLRMQLMREQAQQEEQRERMQQQAVMHYMQQQQQQQQQQLGGPPTPAINTPVHFQSPPPVPGEVLKVQSYLENPTSYHLQQSQHQKVREYLSETYGNKFAAHISPAQGSPKPPPAASPGVRAGHVLSSSAGNSAPNSPMAMLHIGSNPERELDDVIDNIMRLDDVLGYINPEMQMPNTLPLSSSHLNVYSSDPQVTASLVGVTSSSCPADLTQKRELTDAESRALAKERQKKDNHNLIERRRRFNINDRIKELGMLIPKANDLDVRWNKGTILKASVDYIRRMQKDLQKSRELENHSRRLEMTNKQLWLRIQELEMQARVHGLPTTSPSGMNMAELAQQVVKQELPSEEGPGEALMLGAEVPDPEPLPALPPQAPLPLPTQPPSPFHHLDFSHSLSFGGREDEGPPGYPEPLAPGHGSPFPSLSKKDLDLMLLDDSLLPLASDPLLSTMSPEASKASSRRSSFSMEEGDVL [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P19484 [UniProt boundaries chain B]=248-319 [UniProt coverage chain B]=15% [Name chain B]=Transcription factor EB [UniProt sequence chain B]=MASRIGLRMQLMREQAQQEEQRERMQQQAVMHYMQQQQQQQQQQLGGPPTPAINTPVHFQSPPPVPGEVLKVQSYLENPTSYHLQQSQHQKVREYLSETYGNKFAAHISPAQGSPKPPPAASPGVRAGHVLSSSAGNSAPNSPMAMLHIGSNPERELDDVIDNIMRLDDVLGYINPEMQMPNTLPLSSSHLNVYSSDPQVTASLVGVTSSSCPADLTQKRELTDAESRALAKERQKKDNHNLIERRRRFNINDRIKELGMLIPKANDLDVRWNKGTILKASVDYIRRMQKDLQKSRELENHSRRLEMTNKQLWLRIQELEMQARVHGLPTTSPSGMNMAELAQQVVKQELPSEEGPGEALMLGAEVPDPEPLPALPPQAPLPLPTQPPSPFHHLDFSHSLSFGGREDEGPPGYPEPLAPGHGSPFPSLSKKDLDLMLLDDSLLPLASDPLLSTMSPEASKASSRRSSFSMEEGDVL [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000371 [Entry] [Entry number]=560 [Entry name]=C-terminal domain of ParB (Spo0J) [PDB ID]=5noc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=The dimer interface is formed via an intermolecular β-sheet and two domain-swapped C-terminal helices. Analytical ultracentrifugation, native MS and circular dichroism thermal melt scans further confirmed that the CTD was primarily dimeric in solution and measured a Tm of 68°C (PMID:29244022). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P26497 [UniProt boundaries chain A]=229-282 [UniProt coverage chain A]=19% [Name chain A]=Stage 0 sporulation protein J [UniProt sequence chain A]=MAKGLGKGINALFNQVDLSEETVEEIKIADLRPNPYQPRKHFDDEALAELKESVLQHGILQPLIVRKSLKGYDIVAGERRFRAAKLAGLDTVPAIVRELSEALMREIALLENLQREDLSPLEEAQAYDSLLKHLDLTQEQLAKRLGKSRPHIANHLRLLTLPENIQQLIAEGTLSMGHGRTLLGLKNKNKLEPLVQKVIAEQLNVRQLEQLIQQLNQNVPRETKKKEPVKDAVLKERESYLQNYFGTTVNIKRQKKKGKIEIEFFSNEDLDRILELLSERES [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P26497 [UniProt boundaries chain B]=229-282 [UniProt coverage chain B]=19% [Name chain B]=Stage 0 sporulation protein J [UniProt sequence chain B]=MAKGLGKGINALFNQVDLSEETVEEIKIADLRPNPYQPRKHFDDEALAELKESVLQHGILQPLIVRKSLKGYDIVAGERRFRAAKLAGLDTVPAIVRELSEALMREIALLENLQREDLSPLEEAQAYDSLLKHLDLTQEQLAKRLGKSRPHIANHLRLLTLPENIQQLIAEGTLSMGHGRTLLGLKNKNKLEPLVQKVIAEQLNVRQLEQLIQQLNQNVPRETKKKEPVKDAVLKERESYLQNYFGTTVNIKRQKKKGKIEIEFFSNEDLDRILELLSERES [Source organism chain B]=Bacillus subtilis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus subtilis [Accession]=MF7000373 [Entry] [Entry number]=561 [Entry name]=N-terminal coiled coil domain Ddc2 (S. cerevisiae) [PDB ID]=5omd [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:29033322). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q04377 [UniProt boundaries chain A]=73-132 [UniProt coverage chain A]=8% [Name chain A]=DNA damage checkpoint protein LCD1 [UniProt sequence chain A]=MRRETVGEFSSDDDDDILLELGTRPPRFTQIPPSSAALQTQIPTTLEVTTTTLNNKQSKNDNQLVNQLNKAQGEASMLRDKINFLNIEREKEKNIQAVKVNELQVKHLQELAKLKQELQKLEDEKKFLQMEARGKSKREVITNVKPPSTTLSTNTNTITPDSSSVAIEAKPQSPQSKKRKISDNLLKKNMVPLNPNRIIPDETSLFLESILLHQIIGADLSTIEILNRLKLDYITEFKFKNFVIAKGAPIGKSIVSLLLRCKKTLTLDRFIDTLLEDIAVLIKEISVHPNESKLAVPFLVALMYQIVQFRPSATHNLALKDCFLFICDLIRIYHHVLKVPIHESNMNLHVEPQIFQYELIDYLIISYSFDLLEGILRVLQSHPKQTYMEFFDENILKSFEFVYKLALTISYKPMVNVIFSAVEVVNIITSIILNMDNSSDLKSLISGSWWRDCITRLYALLEKEIKSGDVYNENVDTTTLHMSKYHDFFGLIRNIGDNELGGLISKLIYTDRLQSVPRVISKEDIGMDSDKFTAPIIGYKMEKWLLKLKDEVLNIFENLLMIYGDDATIVNGEMLIHSSKFLSREQALMIERYVGQDSPNLDLRCHLIEHTLTIIYRLWKDHFKQLREEQIKQVESQLIMSLWRFLVCQTETVTANEREMRDHRHLVDSLHDLTIKDQASYYEDAFEDLPEYIEEELKMQLNKRTGRIMQVKYDEKFQEMARTILESKSFDLTTLEEADSLYISMGL [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=Q04377 [UniProt boundaries chain A-2]=73-132 [UniProt coverage chain A-2]=8% [Name chain A-2]=DNA damage checkpoint protein LCD1 [UniProt sequence chain A-2]=MRRETVGEFSSDDDDDILLELGTRPPRFTQIPPSSAALQTQIPTTLEVTTTTLNNKQSKNDNQLVNQLNKAQGEASMLRDKINFLNIEREKEKNIQAVKVNELQVKHLQELAKLKQELQKLEDEKKFLQMEARGKSKREVITNVKPPSTTLSTNTNTITPDSSSVAIEAKPQSPQSKKRKISDNLLKKNMVPLNPNRIIPDETSLFLESILLHQIIGADLSTIEILNRLKLDYITEFKFKNFVIAKGAPIGKSIVSLLLRCKKTLTLDRFIDTLLEDIAVLIKEISVHPNESKLAVPFLVALMYQIVQFRPSATHNLALKDCFLFICDLIRIYHHVLKVPIHESNMNLHVEPQIFQYELIDYLIISYSFDLLEGILRVLQSHPKQTYMEFFDENILKSFEFVYKLALTISYKPMVNVIFSAVEVVNIITSIILNMDNSSDLKSLISGSWWRDCITRLYALLEKEIKSGDVYNENVDTTTLHMSKYHDFFGLIRNIGDNELGGLISKLIYTDRLQSVPRVISKEDIGMDSDKFTAPIIGYKMEKWLLKLKDEVLNIFENLLMIYGDDATIVNGEMLIHSSKFLSREQALMIERYVGQDSPNLDLRCHLIEHTLTIIYRLWKDHFKQLREEQIKQVESQLIMSLWRFLVCQTETVTANEREMRDHRHLVDSLHDLTIKDQASYYEDAFEDLPEYIEEELKMQLNKRTGRIMQVKYDEKFQEMARTILESKSFDLTTLEEADSLYISMGL [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000375 [Entry] [Entry number]=562 [Entry name]=Oligomerization domain of TPR [PDB ID]=5to5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Nucleoprotein TPR [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:28528776). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000376,MF7000377 [UniProt ID chain A]=P12270 [UniProt boundaries chain A]=2-142 [UniProt coverage chain A]=5% [Name chain A]=Nucleoprotein TPR [UniProt sequence chain A]=MAAVLQQVLERTELNKLPKSVQNKLEKFLADQQSEIDGLKGRHEKFKVESEQQYFEIEKRLSHSQERLVNETRECQSLRLELEKLNNQLKALTEKNKELEIAQDRNIAIQSQFTRTKEELEAEKRDLIRTNERLSQELEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVSVKYREKRLEQEKELLHSQNTWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVSRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVEELHKLLKEAGEANKAIQDHLLEVEQSKDQMEKEMLEKIGRLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKLENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSVKLEQAMKEIQRLQEDTDKANKQSSVLERDNRRMEIQVKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLVALRELGETREREEQETTSSKITELQLKLESALTELEQLRKSRQHQMQLVDSIVRQRDMYRILLSQTTGVAIPLHASSLDDVSLASTPKRPSTSQTVSTPAPVPVIESTEAIEAKAALKQLQEIFENYKKEKAENEKIQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLHERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLSSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTETNLHLNTKELLKNAQKEIATLKQHLSNMEVQVASQSSQRTGKGQPSNKEDVDDLVSQLRQTEEQVNDLKERLKTSTSNVEQYQAMVTSLEESLNKEKQVTEEVRKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRRAIESMEQQLSELKKTLSSVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMASVRQHLEETTQKAESQLLECKASWEERERMLKDEVSKCVCRCEDLEKQNRLLHDQIEKLSDKVVASVKEGVQGPLNVSLSEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQDLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQHLVSQQKDPDTEEYRKLLSEKEVHTKRIQQLTEEIGRLKAEIARSNASLTNNQNLIQSLKEDLNKVRTEKETIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQYEELKAQQDKVMETSAQSSGDHQEQHVSVQEMQELKETLNQAETKSKSLESQVENLQKTLSEKETEARNLQEQTVQLQSELSRLRQDLQDRTTQEEQLRQQITEKEEKTRKAIVAAKSKIAHLAGVKDQLTKENEELKQRNGALDQQKDELDVRITALKSQYEGRISRLERELREHQERHLEQRDEPQEPSNKVPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGSTSGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPANQELSSNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTIEASDQVSDDTVEMPLPKKLKSVTPVGTEEEVMAEESTDGEVETQVYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTTSSQDGQGKGDDVIVIDSDDEEEDDDENDGEHEDYEEDEEDDDDDEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGGEGNHRAADSQNSGEGNTGAAESSFSQEVSREQQPSSASERQAPRAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETATGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGVSHAMGGRGGINRGNIN [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P12270 [UniProt boundaries chain B]=3-142 [UniProt coverage chain B]=5% [Name chain B]=Nucleoprotein TPR [UniProt sequence chain B]=MAAVLQQVLERTELNKLPKSVQNKLEKFLADQQSEIDGLKGRHEKFKVESEQQYFEIEKRLSHSQERLVNETRECQSLRLELEKLNNQLKALTEKNKELEIAQDRNIAIQSQFTRTKEELEAEKRDLIRTNERLSQELEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVSVKYREKRLEQEKELLHSQNTWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVSRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVEELHKLLKEAGEANKAIQDHLLEVEQSKDQMEKEMLEKIGRLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKLENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSVKLEQAMKEIQRLQEDTDKANKQSSVLERDNRRMEIQVKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLVALRELGETREREEQETTSSKITELQLKLESALTELEQLRKSRQHQMQLVDSIVRQRDMYRILLSQTTGVAIPLHASSLDDVSLASTPKRPSTSQTVSTPAPVPVIESTEAIEAKAALKQLQEIFENYKKEKAENEKIQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLHERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLSSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTETNLHLNTKELLKNAQKEIATLKQHLSNMEVQVASQSSQRTGKGQPSNKEDVDDLVSQLRQTEEQVNDLKERLKTSTSNVEQYQAMVTSLEESLNKEKQVTEEVRKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRRAIESMEQQLSELKKTLSSVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMASVRQHLEETTQKAESQLLECKASWEERERMLKDEVSKCVCRCEDLEKQNRLLHDQIEKLSDKVVASVKEGVQGPLNVSLSEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQDLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQHLVSQQKDPDTEEYRKLLSEKEVHTKRIQQLTEEIGRLKAEIARSNASLTNNQNLIQSLKEDLNKVRTEKETIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQYEELKAQQDKVMETSAQSSGDHQEQHVSVQEMQELKETLNQAETKSKSLESQVENLQKTLSEKETEARNLQEQTVQLQSELSRLRQDLQDRTTQEEQLRQQITEKEEKTRKAIVAAKSKIAHLAGVKDQLTKENEELKQRNGALDQQKDELDVRITALKSQYEGRISRLERELREHQERHLEQRDEPQEPSNKVPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGSTSGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPANQELSSNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTIEASDQVSDDTVEMPLPKKLKSVTPVGTEEEVMAEESTDGEVETQVYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTTSSQDGQGKGDDVIVIDSDDEEEDDDENDGEHEDYEEDEEDDDDDEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGGEGNHRAADSQNSGEGNTGAAESSFSQEVSREQQPSSASERQAPRAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETATGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGVSHAMGGRGGINRGNIN [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Homo sapiens [Accession]=MF7000376 [Entry] [Entry number]=563 [Entry name]=Oligomerization domain of TPR [PDB ID]=5tvb [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Nucleoprotein TPR [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:28528776). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000376,MF7000377 [UniProt ID chain A]=P12270 [UniProt boundaries chain A]=3-142 [UniProt coverage chain A]=5% [Name chain A]=Nucleoprotein TPR [UniProt sequence chain A]=MAAVLQQVLERTELNKLPKSVQNKLEKFLADQQSEIDGLKGRHEKFKVESEQQYFEIEKRLSHSQERLVNETRECQSLRLELEKLNNQLKALTEKNKELEIAQDRNIAIQSQFTRTKEELEAEKRDLIRTNERLSQELEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVSVKYREKRLEQEKELLHSQNTWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVSRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVEELHKLLKEAGEANKAIQDHLLEVEQSKDQMEKEMLEKIGRLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKLENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSVKLEQAMKEIQRLQEDTDKANKQSSVLERDNRRMEIQVKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLVALRELGETREREEQETTSSKITELQLKLESALTELEQLRKSRQHQMQLVDSIVRQRDMYRILLSQTTGVAIPLHASSLDDVSLASTPKRPSTSQTVSTPAPVPVIESTEAIEAKAALKQLQEIFENYKKEKAENEKIQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLHERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLSSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTETNLHLNTKELLKNAQKEIATLKQHLSNMEVQVASQSSQRTGKGQPSNKEDVDDLVSQLRQTEEQVNDLKERLKTSTSNVEQYQAMVTSLEESLNKEKQVTEEVRKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRRAIESMEQQLSELKKTLSSVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMASVRQHLEETTQKAESQLLECKASWEERERMLKDEVSKCVCRCEDLEKQNRLLHDQIEKLSDKVVASVKEGVQGPLNVSLSEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQDLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQHLVSQQKDPDTEEYRKLLSEKEVHTKRIQQLTEEIGRLKAEIARSNASLTNNQNLIQSLKEDLNKVRTEKETIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQYEELKAQQDKVMETSAQSSGDHQEQHVSVQEMQELKETLNQAETKSKSLESQVENLQKTLSEKETEARNLQEQTVQLQSELSRLRQDLQDRTTQEEQLRQQITEKEEKTRKAIVAAKSKIAHLAGVKDQLTKENEELKQRNGALDQQKDELDVRITALKSQYEGRISRLERELREHQERHLEQRDEPQEPSNKVPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGSTSGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPANQELSSNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTIEASDQVSDDTVEMPLPKKLKSVTPVGTEEEVMAEESTDGEVETQVYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTTSSQDGQGKGDDVIVIDSDDEEEDDDENDGEHEDYEEDEEDDDDDEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGGEGNHRAADSQNSGEGNTGAAESSFSQEVSREQQPSSASERQAPRAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETATGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGVSHAMGGRGGINRGNIN [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P12270 [UniProt boundaries chain B]=3-142 [UniProt coverage chain B]=5% [Name chain B]=Nucleoprotein TPR [UniProt sequence chain B]=MAAVLQQVLERTELNKLPKSVQNKLEKFLADQQSEIDGLKGRHEKFKVESEQQYFEIEKRLSHSQERLVNETRECQSLRLELEKLNNQLKALTEKNKELEIAQDRNIAIQSQFTRTKEELEAEKRDLIRTNERLSQELEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVSVKYREKRLEQEKELLHSQNTWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVSRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVEELHKLLKEAGEANKAIQDHLLEVEQSKDQMEKEMLEKIGRLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKLENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSVKLEQAMKEIQRLQEDTDKANKQSSVLERDNRRMEIQVKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLVALRELGETREREEQETTSSKITELQLKLESALTELEQLRKSRQHQMQLVDSIVRQRDMYRILLSQTTGVAIPLHASSLDDVSLASTPKRPSTSQTVSTPAPVPVIESTEAIEAKAALKQLQEIFENYKKEKAENEKIQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLHERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLSSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTETNLHLNTKELLKNAQKEIATLKQHLSNMEVQVASQSSQRTGKGQPSNKEDVDDLVSQLRQTEEQVNDLKERLKTSTSNVEQYQAMVTSLEESLNKEKQVTEEVRKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRRAIESMEQQLSELKKTLSSVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMASVRQHLEETTQKAESQLLECKASWEERERMLKDEVSKCVCRCEDLEKQNRLLHDQIEKLSDKVVASVKEGVQGPLNVSLSEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQDLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQHLVSQQKDPDTEEYRKLLSEKEVHTKRIQQLTEEIGRLKAEIARSNASLTNNQNLIQSLKEDLNKVRTEKETIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQYEELKAQQDKVMETSAQSSGDHQEQHVSVQEMQELKETLNQAETKSKSLESQVENLQKTLSEKETEARNLQEQTVQLQSELSRLRQDLQDRTTQEEQLRQQITEKEEKTRKAIVAAKSKIAHLAGVKDQLTKENEELKQRNGALDQQKDELDVRITALKSQYEGRISRLERELREHQERHLEQRDEPQEPSNKVPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGSTSGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPANQELSSNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTIEASDQVSDDTVEMPLPKKLKSVTPVGTEEEVMAEESTDGEVETQVYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTTSSQDGQGKGDDVIVIDSDDEEEDDDENDGEHEDYEEDEEDDDDDEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGGEGNHRAADSQNSGEGNTGAAESSFSQEVSREQQPSSASERQAPRAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETATGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGVSHAMGGRGGINRGNIN [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.75 [Source organism]=Homo sapiens [Accession]=MF7000377 [Entry] [Entry number]=564 [Entry name]=RNF20 RING domain [PDB ID]=5trb [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, RING type [Sequence domain]=Zinc finger, C3HC4 type (RING finger) [Evidence level]=No contradicting information [Evidence text]=The BRE1 and BRE1A RING domains are both homodimers in solution as confirmed by size-exclusion chromatography and multi-angle laser light scattering (MALLS) (PMID:27569044, PMID:25864391). The extended dimerization interface consists of symmetric RING domain-RING domain interactions and a coiled- coil interaction between the N-terminal a-helices (PMID:25864391). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000974,MF7000378 [UniProt ID chain A]=Q5VTR2 [UniProt boundaries chain A]=907-975 [UniProt coverage chain A]=7% [Name chain A]=E3 ubiquitin-protein ligase BRE1A [UniProt sequence chain A]=MSGIGNKRAAGEPGTSMPPEKKAAVEDSGTTVETIKLGGVSSTEELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSGDNLIVEEAVQELNSFLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITINARKFEEMNAELEENKELAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRGTHQHQVELIERDEVSLHKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQEDANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSAKDKEKGKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKKENKKMADEDALRKIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDDANFKLMSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDMFNFKRAQEDISRLRRKLETTKKPDNVPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q5VTR2 [UniProt boundaries chain A-2]=907-975 [UniProt coverage chain A-2]=7% [Name chain A-2]=E3 ubiquitin-protein ligase BRE1A [UniProt sequence chain A-2]=MSGIGNKRAAGEPGTSMPPEKKAAVEDSGTTVETIKLGGVSSTEELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSGDNLIVEEAVQELNSFLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITINARKFEEMNAELEENKELAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRGTHQHQVELIERDEVSLHKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQEDANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSAKDKEKGKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKKENKKMADEDALRKIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDDANFKLMSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDMFNFKRAQEDISRLRRKLETTKKPDNVPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF7000378 [Entry] [Entry number]=565 [Entry name]=Coiled coil and marked-box domains of E2F4-DP1 [PDB ID]=5tuu [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Coiled coil and β-sandwich subdomains [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=A substantial part of the structure is a coiled coil dimerization region. Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815). The two transcription factor chains form an intertwined dimer with large relative interafce. The dependence on DP to complete the hydrophobic core explains why heterodimerization is necessary for E2F stability, DNA binding, and transcriptional activity (PMID:28439018). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q14186 [UniProt boundaries chain A]=199-339 [UniProt coverage chain A]=34% [Name chain A]=Transcription factor Dp-1 [UniProt sequence chain A]=MAKDAGLIEANGELKVFIDQNLSPGKGVVSLVAVHPSTVNPLGKQLLPKTFGQSNVNIAQQVVIGTPQRPAASNTLVVGSPHTPSTHFASQNQPSDSSPWSAGKRNRKGEKNGKGLRHFSMKVCEKVQRKGTTSYNEVADELVAEFSAADNHILPNESAYDQKNIRRRVYDALNVLMAMNIISKEKKEIKWIGLPTNSAQECQNLEVERQRRLERIKQKQSQLQELILQQIAFKNLVQRNRHAEQQASRPPPPNSVIHLPFIIVNTSKKTVIDCSISNDKFEYLFNFDNTFEIHDDIEVLKRMGMACGLESGSCSAEDLKMARSLVPKALEPYVTEMAQGTVGGVFITTAGSTSNGTRFSASDLTNGADGMLATSSNGSQYSGSRVETPVSYVGEDDEEDDDFNENDEDD [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q16254 [UniProt boundaries chain B]=91-196 [UniProt coverage chain B]=25% [Name chain B]=Transcription factor E2F4 [UniProt sequence chain B]=MAEAGPQAPPPPGTPSRHEKSLGLLTTKFVSLLQEAKDGVLDLKLAADTLAVRQKRRIYDITNVLEGIGLIEKKSKNSIQWKGVGPGCNTREIADKLIELKAEIEELQQREQELDQHKVWVQQSIRNVTEDVQNSCLAYVTHEDICRCFAGDTLLAIRAPSGTSLEVPIPEGLNGQKKYQIHLKSVSGPIEVLLVNKEAWSSPPVAVPVPPPEDLLQSPSAVSTPPPLPKPALAQSQEASRPNSPQLTPTAVPGSAEVQGMAGPAAEITVSGGPGTDSKDSGELSSLPLGPTTLDTRPLQSSALLDSSSSSSSSSSSSSNSNSSSSSGPNPSTSFEPIKADPTGVLELPKELSEIFDPTRECMSSELLEELMSSEVFAPLLRLSPPPGDHDYIYNLDESEGVCDLFDVPVLNL [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Homo sapiens [Accession]=MF7000379 [Entry] [Entry number]=568 [Entry name]=Kinetochore Mis12C subcomplex from Schizogenesis pombe [PDB ID]=5wwl [Chains]=M,N [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Helix bundles [Sequence domain]=Nnf1-Mis12 heterodimer [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. However, Mis12 and Nnf1 of MNC consist of six and five α-helices, respectively, which tightly pack against each other to form a “V”-shaped heterodimer. The V-shaped structure of MNC can be divided into two helix bundles. The N-terminal seven-helix bundle is composed of the helix α1–α3 of Mis12 and helix α1–α4 of Nnf1, while the helix α4–α6 of Mis12 and helix α5 of Nnf1 form a four-helix buddle at the C terminus. The buried surface area of the interface between Mis12 and Nnf1 is huge, containing nineteen hydrogen bonds, providing a strong interaction for the two subunits. Hydrophobic interactions and salt bridges also make significant contributions to stabilize the heterodimer (PMID:29180432). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain M]=N/A [Evidence chain N]=N/A [Similar structures]=MF7000383,MF7000382 [UniProt ID chain M]=Q9Y738 [UniProt boundaries chain M]=2-215 [UniProt coverage chain M]=82% [Name chain M]=Centromere protein mis12 [UniProt sequence chain M]=MLVELLEFTPLSFIDDVINITNQLLYKGVNGVDKAFSQTRFAKKAPQEIEEGLHKFEVLFESVVDRYYDGFEVYTLRNIFSYPPELKGYMRTFGKDVDYSITTEQDAAMDQAIQEAAEKLVVKMQLRRDLRMRLSRKREKKTEIEKHLERISFLNKVPENWQVTLPETTDFLLDQLGNLQHAVKRVVEASPTVHSREVDERITYLEKGYERLSNPIDQQKDFWSHHLSKLESTANTETANNIHKLLLSSEKDVGHTDEP [Source organism chain M]=Schizosaccharomyces pombe [UniProt ID chain N]=Q09858 [UniProt boundaries chain N]=2-140 [UniProt coverage chain N]=67% [Name chain N]=Kinetochore protein nnf1 [UniProt sequence chain N]=MTSRKEQLDAFLSRTLSETIAHIPLEKFAQCFPSMKKGKVIAVIHQQLIEFFEKSCKQEYANLIKERDLNKKLDMLDECIHDAEFRKLHGESEVDISNKQPQEILKAHLYSHKRELLDKLNQDLLDIDKENEGLSTQIAAEEKATEDCISRMQSLIQKLEKTVYGMNEKNLAKEAHDTLNDLLPYIQNPSSTWTNALNEQGNIER [Source organism chain N]=Schizosaccharomyces pombe [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Schizosaccharomyces pombe [Accession]=MF7000382 [Entry] [Entry number]=569 [Entry name]=Mis12/MIND complex (Kluyveromyces lactis) [PDB ID]=5t51 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Helix bundles [Sequence domain]=Nnf1-Mis12 heterodimer [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. However, Mis12 and Nnf1 of MNC consist of six and five α-helices, respectively, which tightly pack against each other to form a “V”-shaped heterodimer. The V-shaped structure of MNC can be divided into two helix bundles. The N-terminal seven-helix bundle is composed of the helix α1–α3 of Mis12 and helix α1–α4 of Nnf1, while the helix α4–α6 of Mis12 and helix α5 of Nnf1 form a four-helix buddle at the C terminus. The buried surface area of the interface between Mis12 and Nnf1 is huge, containing nineteen hydrogen bonds, providing a strong interaction for the two subunits. Hydrophobic interactions and salt bridges also make significant contributions to stabilize the heterodimer (PMID:29180432). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000383,MF7000382 [UniProt ID chain A]=Q6CLK3 [UniProt boundaries chain A]=3-98 [UniProt coverage chain A]=33% [Name chain A]=KLLA0F02343p [UniProt sequence chain A]=MTTPTMQSTSLLTEHLGYPPISLVDDIINAVNEIMYKCTNAMEKYLMQRNIIGKKDFSDEIKIGTAKLESLLENSVDKNFDKLELYVLRNILSIPSDLLEENRFRLLHHEKLVLTDSATRAHTDTSIEQKLQEIERQYQLNVMLRDRIQNTKELLTEVVQFKKKVIDLLRCDDNLTTALHELWDDLKPLDVAVKLITTRLKQIYLENEEFYSIDQVNRLVKRYNELRNTSIVRNGYIDKKSQHILDELHISVNSTQNNEDSTNTSIRSLQEDDPEIEHPDWSSMQKVI [Source organism chain A]=NRRL Y-1140 / WM37) [UniProt ID chain B]=Q6CPD1 [UniProt boundaries chain B]=13-102 [UniProt coverage chain B]=43% [Name chain B]=Kinetochore-associated protein [UniProt sequence chain B]=MSVDRYSGMEGTEHIRFQRLVQVCNKALEESIRKLQSWEKIHECFPNYGQTREGIENLTVCQQQVIKLWSNLSRVEFDAIFHERSIEEKLNQLDDLINKARSIDTSSSSKKLRKIDDLRPLELIEGNLQGAKESTLERINNKLQIIKESNEALETNLKDLNDNIFQELDQLQQVYDDMLNEKSMLPDETIKQAVSDMIIESRQTS [Source organism chain B]=NRRL Y-1140 / WM37) [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=NRRL Y-1140 / WM37) [Accession]=MF7000383 [Entry] [Entry number]=570 [Entry name]=Dpb4/Dpb3 complex [PDB ID]=5y26 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) and archaeal histone [Evidence level]=Direct evidence [Evidence text]=Data on the GdmCl-induced unfolding and refolding transitions of the dimer (monitored by stopped-flow far UV CD) fitted to a two-state model (PMID:15313621). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2130001,MF7000001,MF7000002,MF7000004,MF7000005,MF7000384,MF7000385 [UniProt ID chain A]=P87174 [UniProt boundaries chain A]=9-105 [UniProt coverage chain A]=46% [Name chain A]=DNA polymerase epsilon subunit D [UniProt sequence chain A]=MNQDKSKETSELDDLALPRSIIMRLVKGVLPEKSLVQKEALKAMINSATLFVSFLTSASGEIATNNNRKILMPQDVLNALDEIEYPEFSKTLKKHLEAYELALKEKRLKLPNVSDVDNRKKAKIDAHDTTPLDEEKDELEEERIAEDIAQNEVEQNIDDVEDLEEVNDTLDANAESPQIETIHLTDATGNPIEDSSESDSEESLQLNDSS [Source organism chain A]=Schizosaccharomyces pombe [UniProt ID chain B]=C6Y4D0 [UniProt boundaries chain B]=1-87 [UniProt coverage chain B]=100% [Name chain B]=DNA polymerase epsilon subunit C [UniProt sequence chain B]=MEKTYGKTVLPLSRVKRIIKQDEDVHYCSNASALLISVATELFVEKLATEAYQLAKLQKRKGIRYRDVEDVVRKDDQFEFLSDLFSI [Source organism chain B]=Schizosaccharomyces pombe [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Schizosaccharomyces pombe [Accession]=MF7000384 [Entry] [Entry number]=571 [Entry name]=Se-Met Dpb4/Dpb3 complex [PDB ID]=5y27 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Histone-like interactions [Subclass]=Histone-like complexes [Sequence domain]=Histone-like transcription factor (CBF/NF-Y) and archaeal histone [Evidence level]=Direct evidence [Evidence text]=Data on the GdmCl-induced unfolding and refolding transitions of the dimer (monitored by stopped-flow far UV CD) fitted to a two-state model (PMID:15313621). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2130001,MF7000001,MF7000002,MF7000004,MF7000005,MF7000384,MF7000385 [UniProt ID chain A]=P87174 [UniProt boundaries chain A]=9-106 [UniProt coverage chain A]=46% [Name chain A]=DNA polymerase epsilon subunit D [UniProt sequence chain A]=MNQDKSKETSELDDLALPRSIIMRLVKGVLPEKSLVQKEALKAMINSATLFVSFLTSASGEIATNNNRKILMPQDVLNALDEIEYPEFSKTLKKHLEAYELALKEKRLKLPNVSDVDNRKKAKIDAHDTTPLDEEKDELEEERIAEDIAQNEVEQNIDDVEDLEEVNDTLDANAESPQIETIHLTDATGNPIEDSSESDSEESLQLNDSS [Source organism chain A]=Schizosaccharomyces pombe [UniProt ID chain B]=C6Y4D0 [UniProt boundaries chain B]=1-87 [UniProt coverage chain B]=100% [Name chain B]=DNA polymerase epsilon subunit C [UniProt sequence chain B]=MEKTYGKTVLPLSRVKRIIKQDEDVHYCSNASALLISVATELFVEKLATEAYQLAKLQKRKGIRYRDVEDVVRKDDQFEFLSDLFSI [Source organism chain B]=Schizosaccharomyces pombe [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Schizosaccharomyces pombe [Accession]=MF7000385 [Entry] [Entry number]=572 [Entry name]=Beclin1-UVRAG complex [PDB ID]=5yr0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:29866835). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O88597 [UniProt boundaries chain A]=175-222 [UniProt coverage chain A]=10% [Name chain A]=Beclin-1 [UniProt sequence chain A]=MEGSKASSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQVRYAQIQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q8K245 [UniProt boundaries chain B]=231-274 [UniProt coverage chain B]=6% [Name chain B]=UV radiation resistance-associated protein [UniProt sequence chain B]=MSSCASLGGPVPLPPPGPSAALTSGAPARALHVELPSQQRRLRHLRNIAARNIVNRNGHQLLDTYFTLHLCDNEKIFKEFYRSEVIKNSLNPTWRSLDFGIMPDRLDTSVSCFVVKIWGGKEEAFQLLIEWKVYLDGLKYLGQQIHARNQNEIIFGLNDGYYGAPCEHKGHPNAQKNLLQVDQNCVRNSYDVFSLLRLHRAQCAIKQTQVTVQRLGKEIEEKLRLTSTSNELKKESECLRLKILVLRNELERQKKALGREVAFLHKQQMALQDKGSAFSTEHGKLQLQKDSLSELRKECTAKRELFLKTNAQLTIRCRQLLSELSYIYPIDLNENKDYFVCGVKLPNSEDFQAKDDGSIAVALGYTAHLVSMISFFLQVPLRYPIIHKGSRSTIKDNINDKLTEKEREFPLYPKGGEKLQFDYGVYLLNKNIAQLRYQHGLGTPDLRQTLPNLKNFMEHGLMVRCDRHHISNAIPVPKRQSSTFGGADGGFSAGIPSPDKVHRKRASSENERLQYKTPPPSYNSALTQPGVAMPTSGDSERKVAPLSSSLDTSLDFSKENKKAGVDLGSSVSGDHGNSDSGQEQGEALPGHLAAVNGTALPSEQAGPAGTLLPGSCHPAPSAELCCAVEQAEEIIGLEATGFTSGDQLEALSCIPVDSAVAVECDEQVLGEFEEFSRRIYALSENVSSFRRPRRSSDK [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Mus musculus [Accession]=MF7000386 [Entry] [Entry number]=574 [Entry name]=Salvador Hippo SARAH domain complex [PDB ID]=6bn1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=SARAH domain dimer [Sequence domain]=SARAH domain dimer [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:29519817). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000985,MF7000389 [UniProt ID chain A]=Q8T0S6 [UniProt boundaries chain A]=606-659 [UniProt coverage chain A]=8% [Name chain A]=Serine/threonine-protein kinase hippo [UniProt sequence chain A]=MSEPEVTSVVDMKSPNISSSCSFFKLKKLSEESLLQPPEKVFDIMYKLGEGSYGSVYKAVHKESSSIVAIKLVPVESDLHEIIKEISIMQQCDSPYVVRYYGSYFKQYDLWICMEYCGAGSVSDIMRLRKKTLTEDEIATILSDTLQGLVYLHLRRKIHRDIKAANILLNTEGYAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIEEIGYDCVADIWSLGITALEMAEGKPPYGEIHPMRAIFMIPQKPPPSFREPDRWSTEFIDFVSKCLVKEPDDRATATELLEHEFIRNAKHRSILKPMLEETCAIREQQRANRSFGGVLAASQAKSLATQENGMQQHITDNAFMEDPGTLVPEKFGEYQQSSASDATMIAHAEQGVDEGTLGPGGLRNLSKAAAPAAASSAASPLDMPAVDSGTMVELESNLGTMVINSDSDDSTTAKNNDDQKPRNRYRPQFLEHFDRKNAGDGRGDEKPIATEYSPAAAEQQQQQQQQQQQQQQDEQHLASGANDLNNWEHNMEMQFQQISAINQYGLQQHQQQQQVLMAYPLMNEQLIALNNQPNLLLSNAAPMGQQGIPAAAPAQPPPAYQNQHMHTQSHAYVEGEFEFLKFLTFDDLNQRLCNIDHEMELEIEQLNKKYNAKRQPIVDAMNAKRKRQQNINNNLIKI [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=Q9VCR6 [UniProt boundaries chain B]=531-600 [UniProt coverage chain B]=11% [Name chain B]=Scaffold protein salvador [UniProt sequence chain B]=MNYLTILLCNRKPTMLSRRNKEKSQHKEGVVGKYMKKDTPPDISVINVWSDQRAKKKSLQRCASTSPSCEFHPRSSSTSRNTYSCTDSQPDYYHARRAQSQMPLQQHSHSHPHSLPHPSHPHVRSHPPLPPHQFRASSNQLSQNSSNYVNFEQIERMRRQQSSPLLQTTSSPAPGAGGFQRSYSTTQRQHHPHLGGDSYDADQGLLSASYANMLQLPQRPHSPAHYAVPPQQQQHPQIHQQHASTPFGSTLRFDRAAMSIRERQPRYQPTSSPMQQQQQQQQQQQQQLQHTQLAAHLGGSYSSDSYPIYENPSRVISMRATQSQRSESPIYSNTTASSATLAVVPQHHHQGHLAVPSGSGGGSLSGSGRGGSSGSVRGASTSVQSLYVPPRTPPSAVAGAGGSANGSLQKVPSQQSLTEPEELPLPPGWATQYTLHGRKYYIDHNAHTTHWNHPLEREGLPVGWRRVVSKMHGTYYENQYTGQSQRQHPCLTSYYVYTTSAEPPKAIRPEASLYAPPTHTHNALVPANPYLLEEIPKWLAVYSEADSSKDHLLQFNMFSLPELEGFDSMLVRLFKQELGTIVGFYERYRRALILEKNRRAGQNQNQNQ [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Drosophila melanogaster [Accession]=MF7000389 [Entry] [Entry number]=576 [Entry name]=Zika virus capsid protein [PDB ID]=6c44 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Capsid proteins [Sequence domain]=Flavivirus capsid protein C [Evidence level]=Direct evidence [Evidence text]=The structure of flavivirus C protein shows a fold with a large hydrophobic dimerization surface contributed by two pairs of helices, one of which has characteristics of a coiled-coil. The large relative interaction surface area explains the high stability of the dimer and is consistent with the estimated Kd < 10 nM. The hydrophobic core of the dimer is assembled from both monomers, which strongly suggests that the monomeric form of the protein would be unstable (PMID:14993605). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2140015,MF7000391 [UniProt ID chain A]=A0A1V0E2H9 [UniProt boundaries chain A]=35-104 [UniProt coverage chain A]=2% [Name chain A]=Genome polyprotein [UniProt sequence chain A]=MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFXAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKXPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSVVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQXLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKXGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPVLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFVDENHPYRTWAYHGSYEAPTQGSASSLVNGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAXSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGEEEKYMDYLSTQVRYLGEEGSTPGVL [Source organism chain A]=Zika virus [UniProt ID chain B]=A0A1V0E2H9 [UniProt boundaries chain B]=35-104 [UniProt coverage chain B]=2% [Name chain B]=Genome polyprotein [UniProt sequence chain B]=MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFXAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKXPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSVVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQXLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKXGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPVLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFVDENHPYRTWAYHGSYEAPTQGSASSLVNGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAXSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGEEEKYMDYLSTQVRYLGEEGSTPGVL [Source organism chain B]=Zika virus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Zika virus [Accession]=MF7000391 [Entry] [Entry number]=579 [Entry name]=AtaR antitoxin [PDB ID]=6gto [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Monomeric states are largely disordered but stabilised in the dimer by helix-helix contacts. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=J7QA90 [UniProt boundaries chain A]=9-70 [UniProt coverage chain A]=70% [Name chain A]=DUF1778 domain-containing protein [UniProt sequence chain A]=MSAVKKQRIDLRLTDDDKSMIEEAAAISNQSVSQFMLNSASQRAAEVIEQHRRVILNEESWTRVMDALSNPPSPGEKLKRAAKRLQGM [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=J7QA90 [UniProt boundaries chain A-2]=9-70 [UniProt coverage chain A-2]=70% [Name chain A-2]=DUF1778 domain-containing protein [UniProt sequence chain A-2]=MSAVKKQRIDLRLTDDDKSMIEEAAAISNQSVSQFMLNSASQRAAEVIEQHRRVILNEESWTRVMDALSNPPSPGEKLKRAAKRLQGM [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.97 [Source organism]=Escherichia coli [Accession]=MF7000394 [Entry] [Entry number]=582 [Entry name]=Prohibitin 2 [PDB ID]=6iqe [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:31522117). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q99623 [UniProt boundaries chain A]=188-245 [UniProt coverage chain A]=19% [Name chain A]=Prohibitin-2 [UniProt sequence chain A]=MAQNLKDLAGRLPAGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q99623 [UniProt boundaries chain A-2]=188-245 [UniProt coverage chain A-2]=19% [Name chain A-2]=Prohibitin-2 [UniProt sequence chain A-2]=MAQNLKDLAGRLPAGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Homo sapiens [Accession]=MF7000397 [Entry] [Entry number]=583 [Entry name]=PadR-like transcriptional regulator BC1756 [PDB ID]=6jyi [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q81F45 [UniProt boundaries chain A]=1-170 [UniProt coverage chain A]=94% [Name chain A]=Transcriptional repressor PadR [UniProt sequence chain A]=MKGRDVVLGLLMQKELSGYDIKIVFEDVFTHFFDGSFGMIYPTLRQLENEGKIKKEVVMQEGKPNKKMYFITDEGREEFYQYMQTPVEKDVLRSDFLMRMYFGNYSDDVTIKKWIKDEIERKEAYIADLRLKYEKWRVGITFVEEISLDVGIASYSAQVETLKKKLEELEAKENNKTEE [Source organism chain A]=15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) [UniProt ID chain B]=Q81F45 [UniProt boundaries chain B]=2-173 [UniProt coverage chain B]=96% [Name chain B]=Transcriptional repressor PadR [UniProt sequence chain B]=MKGRDVVLGLLMQKELSGYDIKIVFEDVFTHFFDGSFGMIYPTLRQLENEGKIKKEVVMQEGKPNKKMYFITDEGREEFYQYMQTPVEKDVLRSDFLMRMYFGNYSDDVTIKKWIKDEIERKEAYIADLRLKYEKWRVGITFVEEISLDVGIASYSAQVETLKKKLEELEAKENNKTEE [Source organism chain B]=15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) [ExpTech]=X-ray [Resolution]=1.92 [Source organism]=15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) [Accession]=MF7000398 [Entry] [Entry number]=584 [Entry name]=STAS domain of cyanobacteria bicarbonate transporter BicA [PDB ID]=6ki2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. BicASTAS forms a compact homodimer (PMID:31712753). There is beta sheet augmentation between the monomers. Only dimeric forms were detected by SEC-MALS and SDS-PAGE. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q55415 [UniProt boundaries chain A]=409-547 [UniProt coverage chain A]=24% [Name chain A]=Bicarbonate transporter BicA [UniProt sequence chain A]=MQITNKIHFRNLQGDLFGGVTAAVIALPMALAFGIASGAGATAGLWGAVIVGFFAALFGGTPTLISEPTGPMTVVQTAVIASLVAADPDNGLAMAFTVVMMAGLFQIAFGLLKLGKYVTMMPYTVISGFMSGIGIILVILQLAPFLGQASPKGGVIGTLQALPNLVSNVRPVETLLALMTVGIIWFMPSRWKKFAPPQLVALVLGTIISITLFGDLDIRRIGEIQAGLPALQLPVFQADQLQRMLIDAAVLGMLGCIDALLTSVVADSLTRTEHNSNKELVGQGIGNVMSGLFGGLGGAGATMGTVVNIQSGGRTALSGLIRAMVLLVVILGAAKLAATIPLAVLAGIAFKVGVDIIDWGFLKRAHHVSIKGALIMYAVIVLTVLVDLIAAVGIGVFIANILTIDRMSALQSKAVKSISDADDEILLSANEKRWLDEGNGRVLLFQLSGPMIFGVAKAIAREHNAIQECAAIVFDLSDVPHLGVTASLALENAIEEAAEKGRAVYIVGATGQTKRRLEKLQVFRFVPESNCYDDRSEALKDAVLALGPHESEDSPSSSSVQTTY [Source organism chain A]=Synechocystis sp [UniProt ID chain B]=Q55415 [UniProt boundaries chain B]=409-547 [UniProt coverage chain B]=24% [Name chain B]=Bicarbonate transporter BicA [UniProt sequence chain B]=MQITNKIHFRNLQGDLFGGVTAAVIALPMALAFGIASGAGATAGLWGAVIVGFFAALFGGTPTLISEPTGPMTVVQTAVIASLVAADPDNGLAMAFTVVMMAGLFQIAFGLLKLGKYVTMMPYTVISGFMSGIGIILVILQLAPFLGQASPKGGVIGTLQALPNLVSNVRPVETLLALMTVGIIWFMPSRWKKFAPPQLVALVLGTIISITLFGDLDIRRIGEIQAGLPALQLPVFQADQLQRMLIDAAVLGMLGCIDALLTSVVADSLTRTEHNSNKELVGQGIGNVMSGLFGGLGGAGATMGTVVNIQSGGRTALSGLIRAMVLLVVILGAAKLAATIPLAVLAGIAFKVGVDIIDWGFLKRAHHVSIKGALIMYAVIVLTVLVDLIAAVGIGVFIANILTIDRMSALQSKAVKSISDADDEILLSANEKRWLDEGNGRVLLFQLSGPMIFGVAKAIAREHNAIQECAAIVFDLSDVPHLGVTASLALENAIEEAAEKGRAVYIVGATGQTKRRLEKLQVFRFVPESNCYDDRSEALKDAVLALGPHESEDSPSSSSVQTTY [Source organism chain B]=Synechocystis sp [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Synechocystis sp [Accession]=MF7000399 [Entry] [Entry number]=585 [Entry name]=Rootletin [PDB ID]=6l5h [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:32325071). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q5TZA2 [UniProt boundaries chain A]=1108-1187 [UniProt coverage chain A]=3% [Name chain A]=Rootletin [UniProt sequence chain A]=MSLGLAGAQEVELTLETVIQTLESSVLCQEKGLGARDLAQDAQITSLPALIREIVTRNLSQPESPVLLPATEMASLLSLQEENQLLQQELSRVEDLLAQSRAERDELAIKYNAVSERLEQALRLEPGELETQEPRGLVRQSVELRRQLQEEQASYRRKLQAYQEGQQRQAQLVQRLQGKILQYKKRCSELEQQLLERSGELEQQRLRDTEHSQDLESALIRLEEEQQRSASLAQVNAMLREQLDQAGSANQALSEDIRKVTNDWTRCRKELEHREAAWRREEESFNAYFSNEHSRLLLLWRQVVGFRRLVSEVKMFTERDLLQLGGELARTSRAVQEAGLGLSTGLRLAESRAEAALEKQALLQAQLEEQLRDKVLREKDLAQQQMQSDLDKADLSARVTELGLAVKRLEKQNLEKDQVNKDLTEKLEALESLRLQEQAALETEDGEGLQQTLRDLAQAVLSDSESGVQLSGSERTADASNGSLRGLSGQRTPSPPRRSSPGRGRSPRRGPSPACSDSSTLALIHSALHKRQLQVQDMRGRYEASQDLLGTLRKQLSDSESERRALEEQLQRLRDKTDGAMQAHEDAQREVQRLRSANELLSREKSNLAHSLQVAQQQAEELRQEREKLQAAQEELRRQRDRLEEEQEDAVQDGARVRRELERSHRQLEQLEGKRSVLAKELVEVREALSRATLQRDMLQAEKAEVAEALTKAEAGRVELELSMTKLRAEEASLQDSLSKLSALNESLAQDKLDLNRLVAQLEEEKSALQGRQRQAEQEATVAREEQERLEELRLEQEVARQGLEGSLRVAEQAQEALEQQLPTLRHERSQLQEQLAQLSRQLSGREQELEQARREAQRQVEALERAAREKEALAKEHAGLAVQLVAAEREGRTLSEEATRLRLEKEALEGSLFEVQRQLAQLEARREQLEAEGQALLLAKETLTGELAGLRQQIIATQEKASLDKELMAQKLVQAEREAQASLREQRAAHEEDLQRLQREKEAAWRELEAERAQLQSQLQREQEELLARLEAEKEELSEEIAALQQERDEGLLLAESEKQQALSLKESEKTALSEKLMGTRHSLATISLEMERQKRDAQSRQEQDRSTVNALTSELRDLRAQREEAAAAHAQEVRRLQEQARDLGKQRDSCLREAEELRTQLRLLEDARDGLRRELLEAQRKLRESQEGREVQRQEAGELRRSLGEGAKEREALRRSNEELRSAVKKAESERISLKLANEDKEQKLALLEEARTAVGKEAGELRTGLQEVERSRLEARRELQELRRQMKMLDSENTRLGRELAELQGRLALGERAEKESRRETLGLRQRLLKGEASLEVMRQELQVAQRKLQEQEGEFRTRERRLLGSLEEARGTEKQQLDHARGLELKLEAARAEAAELGLRLSAAEGRAQGLEAELARVEVQRRAAEAQLGGLRSALRRGLGLGRAPSPAPRPVPGSPARDAPAEGSGEGLNSPSTLECSPGSQPPSPGPATSPASPDLDPEAVRGALREFLQELRSAQRERDELRTQTSALNRQLAEMEAERDSATSRARQLQKAVAESEEARRSVDGRLSGVQAELALQEESVRRSERERRATLDQVATLERSLQATESELRASQEKISKMKANETKLEGDKRRLKEVLDASESRTVKLELQRRSLEGELQRSRLGLSDREAQAQALQDRVDSLQRQVADSEVKAGTLQLTVERLNGALAKVEESEGALRDKVRGLTEALAQSSASLNSTRDKNLHLQKALTACEHDRQVLQERLDAARQALSEARKQSSSLGEQVQTLRGEVADLELQRVEAEGQLQQLREVLRQRQEGEAAALNTVQKLQDERRLLQERLGSLQRALAQLEAEKREVERSALRLEKDRVALRRTLDKVEREKLRSHEDTVRLSAEKGRLDRTLTGAELELAEAQRQIQQLEAQVVVLEQSHSPAQLEVDAQQQQLELQQEVERLRSAQAQTERTLEARERAHRQRVRGLEEQVSTLKGQLQQELRRSSAPFSPPSGPPEK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q5TZA2 [UniProt boundaries chain B]=1108-1187 [UniProt coverage chain B]=3% [Name chain B]=Rootletin [UniProt sequence chain B]=MSLGLAGAQEVELTLETVIQTLESSVLCQEKGLGARDLAQDAQITSLPALIREIVTRNLSQPESPVLLPATEMASLLSLQEENQLLQQELSRVEDLLAQSRAERDELAIKYNAVSERLEQALRLEPGELETQEPRGLVRQSVELRRQLQEEQASYRRKLQAYQEGQQRQAQLVQRLQGKILQYKKRCSELEQQLLERSGELEQQRLRDTEHSQDLESALIRLEEEQQRSASLAQVNAMLREQLDQAGSANQALSEDIRKVTNDWTRCRKELEHREAAWRREEESFNAYFSNEHSRLLLLWRQVVGFRRLVSEVKMFTERDLLQLGGELARTSRAVQEAGLGLSTGLRLAESRAEAALEKQALLQAQLEEQLRDKVLREKDLAQQQMQSDLDKADLSARVTELGLAVKRLEKQNLEKDQVNKDLTEKLEALESLRLQEQAALETEDGEGLQQTLRDLAQAVLSDSESGVQLSGSERTADASNGSLRGLSGQRTPSPPRRSSPGRGRSPRRGPSPACSDSSTLALIHSALHKRQLQVQDMRGRYEASQDLLGTLRKQLSDSESERRALEEQLQRLRDKTDGAMQAHEDAQREVQRLRSANELLSREKSNLAHSLQVAQQQAEELRQEREKLQAAQEELRRQRDRLEEEQEDAVQDGARVRRELERSHRQLEQLEGKRSVLAKELVEVREALSRATLQRDMLQAEKAEVAEALTKAEAGRVELELSMTKLRAEEASLQDSLSKLSALNESLAQDKLDLNRLVAQLEEEKSALQGRQRQAEQEATVAREEQERLEELRLEQEVARQGLEGSLRVAEQAQEALEQQLPTLRHERSQLQEQLAQLSRQLSGREQELEQARREAQRQVEALERAAREKEALAKEHAGLAVQLVAAEREGRTLSEEATRLRLEKEALEGSLFEVQRQLAQLEARREQLEAEGQALLLAKETLTGELAGLRQQIIATQEKASLDKELMAQKLVQAEREAQASLREQRAAHEEDLQRLQREKEAAWRELEAERAQLQSQLQREQEELLARLEAEKEELSEEIAALQQERDEGLLLAESEKQQALSLKESEKTALSEKLMGTRHSLATISLEMERQKRDAQSRQEQDRSTVNALTSELRDLRAQREEAAAAHAQEVRRLQEQARDLGKQRDSCLREAEELRTQLRLLEDARDGLRRELLEAQRKLRESQEGREVQRQEAGELRRSLGEGAKEREALRRSNEELRSAVKKAESERISLKLANEDKEQKLALLEEARTAVGKEAGELRTGLQEVERSRLEARRELQELRRQMKMLDSENTRLGRELAELQGRLALGERAEKESRRETLGLRQRLLKGEASLEVMRQELQVAQRKLQEQEGEFRTRERRLLGSLEEARGTEKQQLDHARGLELKLEAARAEAAELGLRLSAAEGRAQGLEAELARVEVQRRAAEAQLGGLRSALRRGLGLGRAPSPAPRPVPGSPARDAPAEGSGEGLNSPSTLECSPGSQPPSPGPATSPASPDLDPEAVRGALREFLQELRSAQRERDELRTQTSALNRQLAEMEAERDSATSRARQLQKAVAESEEARRSVDGRLSGVQAELALQEESVRRSERERRATLDQVATLERSLQATESELRASQEKISKMKANETKLEGDKRRLKEVLDASESRTVKLELQRRSLEGELQRSRLGLSDREAQAQALQDRVDSLQRQVADSEVKAGTLQLTVERLNGALAKVEESEGALRDKVRGLTEALAQSSASLNSTRDKNLHLQKALTACEHDRQVLQERLDAARQALSEARKQSSSLGEQVQTLRGEVADLELQRVEAEGQLQQLREVLRQRQEGEAAALNTVQKLQDERRLLQERLGSLQRALAQLEAEKREVERSALRLEKDRVALRRTLDKVEREKLRSHEDTVRLSAEKGRLDRTLTGAELELAEAQRQIQQLEAQVVVLEQSHSPAQLEVDAQQQQLELQQEVERLRSAQAQTERTLEARERAHRQRVRGLEEQVSTLKGQLQQELRRSSAPFSPPSGPPEK [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.30 [Source organism]=Homo sapiens [Accession]=MF7000400 [Entry] [Entry number]=586 [Entry name]=N-terminal Chaetomium/Mozart1 complex [PDB ID]=6l82 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. The observed state is the heterodimer. Highly intertwined dimer with large buried surface areas where the helices support each other (PMID:32610137). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=G0SGA5 [UniProt boundaries chain A]=1-103 [UniProt coverage chain A]=11% [Name chain A]=Spindle pole body component [UniProt sequence chain A]=MAFLAQLGALADDLVSAIVGIPEDQTTQRDACRDFVLRSLRHHNFGRTNQFEVQDRLNGLEERFSIVGRDALADALRTRLDALEPHQNQFTPELLHLLLELADQPAQKARLSDLGGLDKPKKEEAPPLTWRQIAKEDNWKDDPEIWRFISYREDSSDDDRSRADQPADSQSVISLESLTTATTEDESCRLTPEDLVVEPDGADLLRQIQKAQSWRNMPALDAEGPPKKTPISTIHLLREALFMLSGLETTLFDQDCAPALDYQLHGVAWTTYKALATSFSECGRKLIPLRSFIKTKEQSPLLQVFQDSAQKALASFDRTLSSIQERFVSIQADTIVSAMSVLEEVSKAVVPLHALSGIVRQLGEERNPHAFRYLELLYDSVELAQLQGQMDTYKLLGRAFFDCFQVYLRPIRLWMEEGRVLPGDRTFFVSESPTKLPLSQVWKGQFNLRQTPDGALHAPRFLKFALHRIFTAGKSIVVLKHMKRHEPVTKYGVSAAEPKMDFETVCPPELEFAPFSELFNTAFQNWIESKHHTAAVTLRELLFTSYGLSEELRALQHVYFMSNYSVVNDFTSSIFRHIDTVNDSWQDRFALTELAQDALSSCIIRERLSAEIDLRILADHVSAPRNSVRFFLPAIRLRYRLPWPVQIVVPEDSIRAYQTVFTYQLQLHRALSALHQPIFTFRKPSPAKEQRLYYRLHTHLLWFTNTLLTYLTTFVLAPNTAQLTTALDAAEDIDEMVAAHGAFVSRILAESGLTPAMAPIREAILDVLDLAIRVEGVHHKEAERWEREKSERERLEVMASPYTSPEKKRRLLALPPRRARRSRGISVSEEDWDDQTDEVGRAEEGKSYGAMLRDSQKEFERLLRFVAAALRGTARASKDEAASKWDMLAEMLEAGIKESMHG [Source organism chain A]= [UniProt ID chain B]=G0RZC6 [UniProt boundaries chain B]=9-78 [UniProt coverage chain B]=84% [Name chain B]=Mitotic-spindle organizing protein 1 [UniProt sequence chain B]=MPPSERAEKQAAAQQAVDILHEIATILNCHLDRRTLSICISMIENGVNPEALANVIKELRVLGQDPQQLDALVANYLASSRRR [Source organism chain B]= [ExpTech]=X-ray [Resolution]=2.24 [Source organism]= [Accession]=MF7000401 [Entry] [Entry number]=587 [Entry name]=Id1/hE47 complex [PDB ID]=6mgn [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Basic helix-loop-helix (bHLH) [Sequence domain]=Helix-loop-helix DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294, PMID:9488706). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100009,MF2110021,MF2110023,MF2100010,MF7000192,MF7000402,MF7000403,MF7000444,MF7000371 [UniProt ID chain A]=P15923 [UniProt boundaries chain A]=561-612 [UniProt coverage chain A]=7% [Name chain A]=Transcription factor E2-alpha [UniProt sequence chain A]=MNQPQRMAPVGTDKELSDLLDFSMMFPLPVTNGKGRPASLAGAQFGGSGLEDRPSSGSWGSGDQSSSSFDPSRTFSEGTHFTESHSSLSSSTFLGPGLGGKSGERGAYASFGRDAGVGGLTQAGFLSGELALNSPGPLSPSGMKGTSQYYPSYSGSSRRRAADGSLDTQPKKVRKVPPGLPSSVYPPSSGEDYGRDATAYPSAKTPSSTYPAPFYVADGSLHPSAELWSPPGQAGFGPMLGGGSSPLPLPPGSGPVGSSGSSSTFGGLHQHERMGYQLHGAEVNGGLPSASSFSSAPGATYGGVSSHTPPVSGADSLLGSRGTTAGSSGDALGKALASIYSPDHSSNNFSSSPSTPVGSPQGLAGTSQWPRAGAPGALSPSYDGGLHGLQSKIEDHLDEAIHVLRSHAVGTAGDMHTLLPGHGALASGFTGPMSLGGRHAGLVGGSHPEDGLAGSTSLMHNHAALPSQPGTLPDLSRPPDSYSGLGRAGATAAASEIKREEKEDEENTSAADHSEEEKKELKAPRARTSPDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLNSEKPQTKLLILHQAVSVILNLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQMVLSAPHPGLSEAHNPAGHM [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P20067 [UniProt boundaries chain B]=58-104 [UniProt coverage chain B]=27% [Name chain B]=DNA-binding protein inhibitor ID-1 [UniProt sequence chain B]=MKVASGSAAAAAGPSCSLKAGRTAGEVVLGLSEQSVAISRCAGTRLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTTGGRGLPVRAPLSTLNGEISALAAEVRSESEYYIILQWETEATGGGCPPSLLFRRIAI [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Mus musculus ;Homo sapiens [Accession]=MF7000402 [Entry] [Entry number]=588 [Entry name]=HLH motif of DNA-binding protein inhibitor ID-1 [PDB ID]=6u2u [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Basic helix-loop-helix (bHLH) [Sequence domain]=Helix-loop-helix DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294, PMID:9488706). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100009,MF2110021,MF2110023,MF2100010,MF7000192,MF7000402,MF7000403,MF7000444,MF7000371 [UniProt ID chain A]=P20067 [UniProt boundaries chain A]=59-104 [UniProt coverage chain A]=27% [Name chain A]=DNA-binding protein inhibitor ID-1 [UniProt sequence chain A]=MKVASGSAAAAAGPSCSLKAGRTAGEVVLGLSEQSVAISRCAGTRLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTTGGRGLPVRAPLSTLNGEISALAAEVRSESEYYIILQWETEATGGGCPPSLLFRRIAI [Source organism chain A]=Mus musculus [UniProt ID chain B]=P20067 [UniProt boundaries chain B]=59-102 [UniProt coverage chain B]=26% [Name chain B]=DNA-binding protein inhibitor ID-1 [UniProt sequence chain B]=MKVASGSAAAAAGPSCSLKAGRTAGEVVLGLSEQSVAISRCAGTRLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTTGGRGLPVRAPLSTLNGEISALAAEVRSESEYYIILQWETEATGGGCPPSLLFRRIAI [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Mus musculus [Accession]=MF7000403 [Entry] [Entry number]=591 [Entry name]=HVO_2922 protein (Haloferax volcanii) [PDB ID]=6q2z [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=- [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The dimeric structure is crucial for protein stability and most likely for its functionality. Mutagenesis at the b-sheet dimer interface leads to a loss of the stability and protein aggregation (PMID:31161645). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=D4GXU1 [UniProt boundaries chain A]=1-60 [UniProt coverage chain A]=100% [Name chain A]=UPF0339 family protein [UniProt sequence chain A]=MNKAHFEVFVDAADKYRWRLVHDNGNILADSGEGYASKQKAKQGIESVKRNAPDADVIEA [Source organism chain A]=NCIMB 2012 / VKM B-1768 / DS2) [UniProt ID chain B]=D4GXU1 [UniProt boundaries chain B]=1-60 [UniProt coverage chain B]=100% [Name chain B]=UPF0339 family protein [UniProt sequence chain B]=MNKAHFEVFVDAADKYRWRLVHDNGNILADSGEGYASKQKAKQGIESVKRNAPDADVIEA [Source organism chain B]=NCIMB 2012 / VKM B-1768 / DS2) [ExpTech]=NMR [Resolution]=N/A [Source organism]=NCIMB 2012 / VKM B-1768 / DS2) [Accession]=MF7000407 [Entry] [Entry number]=592 [Entry name]=ssDNA-binding RNA polymerase cofactor Drc [PDB ID]=6qlc [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=- [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. Two Drc monomers strongly interact via 26 hydrogen bonds and six salt bridges to form a stable dimer (PMID:31724707). There is domain swapping and beta sheet augmentation, the monomers most probably would not be stable. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=C8ZKB3 [UniProt boundaries chain A]=18-99 [UniProt coverage chain A]=82% [Name chain A]=Uncharacterized protein [UniProt sequence chain A]=MALVKKNQARNTQATDNKGASAYLNFHFPTRDGKDVRLVSLGLRADDALHMQLQEFLTVDDKGKPLSETAYAERCKKLVSRLIIKLGVTRSEEERALDL [Source organism chain A]=Pseudomonas phage LUZ7 [UniProt ID chain A-2]=C8ZKB3 [UniProt boundaries chain A-2]=18-99 [UniProt coverage chain A-2]=82% [Name chain A-2]=Uncharacterized protein [UniProt sequence chain A-2]=MALVKKNQARNTQATDNKGASAYLNFHFPTRDGKDVRLVSLGLRADDALHMQLQEFLTVDDKGKPLSETAYAERCKKLVSRLIIKLGVTRSEEERALDL [Source organism chain A-2]=Pseudomonas phage LUZ7 [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Pseudomonas phage LUZ7 [Accession]=MF7000408 [Entry] [Entry number]=593 [Entry name]=Domain-swapped N-lobe dimer of Arc 2 [PDB ID]=6sib [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms, however there is no InterPro domain rendered to this region and the three-three helices of the two monomers most probably do not constitute a stable fold on their own. Large relative interaction surface area, extensive interchain helix packing interactions within the domain-swapped dimer. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q7JV70 [UniProt boundaries chain A]=45-109 [UniProt coverage chain A]=33% [Name chain A]=Activity-regulated cytoskeleton associated protein 2 [UniProt sequence chain A]=MTQMSDEQFRIFIETIKSLGPIKEEPPSKGSFSNCTVRFSGQRDHDAVDEFINAVETYKEVEGISDKDALKGLPLLFKSIAVVWWKGVRRDAKTWSDALQLLRDHFSPTKPSYQIYMEIFETKQSYDEVIDSFICKQRALLAKLPEGRHDEETELDFIYGLMQPKYRESIPRHEVKTFRELLDRGRTVERTRH [Source organism chain A]=Drosophila melanogaster [UniProt ID chain A-2]=Q7JV70 [UniProt boundaries chain A-2]=45-109 [UniProt coverage chain A-2]=33% [Name chain A-2]=Activity-regulated cytoskeleton associated protein 2 [UniProt sequence chain A-2]=MTQMSDEQFRIFIETIKSLGPIKEEPPSKGSFSNCTVRFSGQRDHDAVDEFINAVETYKEVEGISDKDALKGLPLLFKSIAVVWWKGVRRDAKTWSDALQLLRDHFSPTKPSYQIYMEIFETKQSYDEVIDSFICKQRALLAKLPEGRHDEETELDFIYGLMQPKYRESIPRHEVKTFRELLDRGRTVERTRH [Source organism chain A-2]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Drosophila melanogaster [Accession]=MF7000409 [Entry] [Entry number]=594 [Entry name]=Coiled coil region of septin 6 [PDB ID]=6wbp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:33639214). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q14141 [UniProt boundaries chain A]=347-397 [UniProt coverage chain A]=11% [Name chain A]=Septin-6 [UniProt sequence chain A]=MAATDIARQVGEGCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLQSNTYDLQESNVRLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHTYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADAISKSELTKFKIKITSELVSNGVQIYQFPTDDESVAEINGTMNAHLPFAVIGSTEELKIGNKMMRARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQDEKKKLEDKKKSLDDEVNAFKQRKTAAELLQSQGSQAGGSQTLKRDKEKKNNPWLCTE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q14141 [UniProt boundaries chain B]=347-399 [UniProt coverage chain B]=12% [Name chain B]=Septin-6 [UniProt sequence chain B]=MAATDIARQVGEGCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLQSNTYDLQESNVRLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHTYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADAISKSELTKFKIKITSELVSNGVQIYQFPTDDESVAEINGTMNAHLPFAVIGSTEELKIGNKMMRARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQDEKKKLEDKKKSLDDEVNAFKQRKTAAELLQSQGSQAGGSQTLKRDKEKKNNPWLCTE [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF7000410 [Entry] [Entry number]=598 [Entry name]=Coiled coil domain of Atg11 [PDB ID]=6vzf [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:32896530). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q12527 [UniProt boundaries chain A]=699-784 [UniProt coverage chain A]=7% [Name chain A]=Autophagy-related protein 11 [UniProt sequence chain A]=MADADEYSTAPTQQEITPLQTTATIINAISGECITTNVDFFVSLDKFKQFIARKWKIPPDQLLILLPYGNKLKPSMFKELLINRSFTLNDFYVYDRRLFSLVSKPTPTNLLTSKDSNPMNSPNSNDLTETLEYLIKNSHISQYQGSDTIMIKPMPSPLEDADVDLSRLNYHSVTSLLTTNLGWLSALEIDVHYFKSLIPDIIAHIKRIFDGLTVCSQYLKLYCFDVESLYNSNVQFLNQLVDNGMTSKWEKCFNDTLSKLTALEGDSLQKFINIESLLENEKSVKILNHSINGKLNKIKREIDENASFRDIITVNIDRLRQMFTPNESKFELEDQMAESFEVLVSEMRTRSRNVLDKEEEEFNSQEFLKSMNVMLEKDKKESVKTLFTISQALYSQIGELIDLKKSLQKHAVAILGNIAFTQMEILGIKRLLLNECNKDLELYKKYEVEFAQVEDLPLIYGLYLIEKYRRLSWFQQILSFISNFNQDLELFKQNELRTRNKWVKNFGSIATVFCEDLLSSSDFKRLNEYHSHTSPPNEDEEDENENSIANYRQDLVKVSQAIDNYMTQIKETDVSEPIIDLLSKTLFETKRFHIIYSNFKNNNNNSSNGNSISPEGSIALKSDDVVKGYKTRIKKLESLLHEFQYSDIGHWPQGVLNTHLKPFRGSATSINKKKFLGASVLLEPANISEVNIDSVSQANNHQIQELESNVDDLLHQLQLLKEENNRKSMQISEMGKKISDLEVEKTAYRETLTNLNQELARLTNEEQSHRTEIFTLNASFKKQLNDIISQDNEKIEKLTGDYDDVSKSRERLQMDLDESNKKHEQEVNLLKADIERLGKQIVTSEKSYAETNSSSMEKGEKFETIPLAEDPGRENQISAYTQTLQDRIFDIISTNIFILENIGLLLTFDNNNNIQIRRVKGLKKGTAQSNILDESTQMLDAHDNSLIKSPVFQKLKDEYELIKSVANGSEKDTQQSIFLGNITQLYDNKLYEVAVIRRFKDIETLAKKLTKENKIKRTLLERFQREKVTLRNFQIGDLALFLPTRENVNSVGSMSSSTSSLSSSFSSVDLSTPPPLDAMSIQSSPSVIHSNVINQASISGRDKNKLMRPWAAFTAFEESTRYFLKDEKGLTKGKEWFVGRIVTLEHFVADSPSNNPFRLPKGSVWFQVTAVVVSYQGV [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=Q12527 [UniProt boundaries chain A-2]=699-784 [UniProt coverage chain A-2]=7% [Name chain A-2]=Autophagy-related protein 11 [UniProt sequence chain A-2]=MADADEYSTAPTQQEITPLQTTATIINAISGECITTNVDFFVSLDKFKQFIARKWKIPPDQLLILLPYGNKLKPSMFKELLINRSFTLNDFYVYDRRLFSLVSKPTPTNLLTSKDSNPMNSPNSNDLTETLEYLIKNSHISQYQGSDTIMIKPMPSPLEDADVDLSRLNYHSVTSLLTTNLGWLSALEIDVHYFKSLIPDIIAHIKRIFDGLTVCSQYLKLYCFDVESLYNSNVQFLNQLVDNGMTSKWEKCFNDTLSKLTALEGDSLQKFINIESLLENEKSVKILNHSINGKLNKIKREIDENASFRDIITVNIDRLRQMFTPNESKFELEDQMAESFEVLVSEMRTRSRNVLDKEEEEFNSQEFLKSMNVMLEKDKKESVKTLFTISQALYSQIGELIDLKKSLQKHAVAILGNIAFTQMEILGIKRLLLNECNKDLELYKKYEVEFAQVEDLPLIYGLYLIEKYRRLSWFQQILSFISNFNQDLELFKQNELRTRNKWVKNFGSIATVFCEDLLSSSDFKRLNEYHSHTSPPNEDEEDENENSIANYRQDLVKVSQAIDNYMTQIKETDVSEPIIDLLSKTLFETKRFHIIYSNFKNNNNNSSNGNSISPEGSIALKSDDVVKGYKTRIKKLESLLHEFQYSDIGHWPQGVLNTHLKPFRGSATSINKKKFLGASVLLEPANISEVNIDSVSQANNHQIQELESNVDDLLHQLQLLKEENNRKSMQISEMGKKISDLEVEKTAYRETLTNLNQELARLTNEEQSHRTEIFTLNASFKKQLNDIISQDNEKIEKLTGDYDDVSKSRERLQMDLDESNKKHEQEVNLLKADIERLGKQIVTSEKSYAETNSSSMEKGEKFETIPLAEDPGRENQISAYTQTLQDRIFDIISTNIFILENIGLLLTFDNNNNIQIRRVKGLKKGTAQSNILDESTQMLDAHDNSLIKSPVFQKLKDEYELIKSVANGSEKDTQQSIFLGNITQLYDNKLYEVAVIRRFKDIETLAKKLTKENKIKRTLLERFQREKVTLRNFQIGDLALFLPTRENVNSVGSMSSSTSSLSSSFSSVDLSTPPPLDAMSIQSSPSVIHSNVINQASISGRDKNKLMRPWAAFTAFEESTRYFLKDEKGLTKGKEWFVGRIVTLEHFVADSPSNNPFRLPKGSVWFQVTAVVVSYQGV [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.03 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000414 [Entry] [Entry number]=599 [Entry name]=Coiled coil region of septin 4 [PDB ID]=6wb3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Septin homodimer [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:33639214). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000415,MF7000416 [UniProt ID chain A]=O43236 [UniProt boundaries chain A]=448-477 [UniProt coverage chain A]=6% [Name chain A]=Septin-4 [UniProt sequence chain A]=MDRSLGWQGNSVPEDRTEAGIKRFLEDTTDDGELSKFVKDFSGNASCHPPEAKTWASRPQVPEPRPQAPDLYDDDLEFRPPSRPQSSDNQQYFCAPAPLSPSARPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPPEVDHKKRKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSMTRLVVKERNRNKLTRESGTDFPIPAVPPGTDPETEKLIREKDEELRRMQEMLHKIQKQMKENY [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O43236 [UniProt boundaries chain B]=448-477 [UniProt coverage chain B]=6% [Name chain B]=Septin-4 [UniProt sequence chain B]=MDRSLGWQGNSVPEDRTEAGIKRFLEDTTDDGELSKFVKDFSGNASCHPPEAKTWASRPQVPEPRPQAPDLYDDDLEFRPPSRPQSSDNQQYFCAPAPLSPSARPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPPEVDHKKRKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSMTRLVVKERNRNKLTRESGTDFPIPAVPPGTDPETEKLIREKDEELRRMQEMLHKIQKQMKENY [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=Homo sapiens [Accession]=MF7000415 [Entry] [Entry number]=600 [Entry name]=Coiled coil region of septin 5 [PDB ID]=6wcu [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Septin homodimer [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:33639214). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000415,MF7000416 [UniProt ID chain A]=Q99719 [UniProt boundaries chain A]=340-369 [UniProt coverage chain A]=8% [Name chain A]=Septin-5 [UniProt sequence chain A]=MSTGLRYKSKLATPEDKQDIDKQYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVHSLFLTDLYKDRKLLSAEERISQTVEILKHTVDIEEKGVKLKLTIVDTPGFGDAVNNTECWKPITDYVDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPVDVGFMKALHEKVNIVPLIAKADCLVPSEIRKLKERIREEIDKFGIHVYQFPECDSDEDEDFKQQDRELKESAPFAVIGSNTVVEAKGQRVRGRLYPWGIVEVENQAHCDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDSRMESPIPILPLPTPDAETEKLIRMKDEELRRMQEMLQRMKQQMQDQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q99719 [UniProt boundaries chain B]=340-369 [UniProt coverage chain B]=8% [Name chain B]=Septin-5 [UniProt sequence chain B]=MSTGLRYKSKLATPEDKQDIDKQYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVHSLFLTDLYKDRKLLSAEERISQTVEILKHTVDIEEKGVKLKLTIVDTPGFGDAVNNTECWKPITDYVDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPVDVGFMKALHEKVNIVPLIAKADCLVPSEIRKLKERIREEIDKFGIHVYQFPECDSDEDEDFKQQDRELKESAPFAVIGSNTVVEAKGQRVRGRLYPWGIVEVENQAHCDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDSRMESPIPILPLPTPDAETEKLIRMKDEELRRMQEMLQRMKQQMQDQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF7000416 [Entry] [Entry number]=603 [Entry name]=Dimerization domain of CheA [PDB ID]=6y1y [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:33188180). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O85747 [UniProt boundaries chain A]=344-468 [UniProt coverage chain A]=15% [Name chain A]=Chemotaxis protein CheA [UniProt sequence chain A]=MSDYLDINNEELLKDFFSEAEQQVEILESNVLVIEQNPEDRNSIDEIFRAAHTLKGGSATVEMLELSKFTHAMEDLLDEIRSGSVKVTGETVDLLLKSIDIIKLMLDARASGSIYSDDVSGIVNQLRSFIPAKAEKKSSKASAPKVSIPASVSPVSAPKVQASASNLDIKDYFSEYEILELAETIQKGEDLYAVIVKFDESNLMNSVGGIQVFAALKDYGSVLKTVPDFDALYEDEFHETVIYFLSSASDSKILEKAAFIGDVTLSASAERLDIKDKTPESPKPAKAAPAQSAPEASVSEVKVSEKTEEKPVQESKEQPSKPEKKQSQTSPQGSGHSSGSILRVDANRIDYLLNLVSETVITKASLNQSTIEFAELYDKFQNSSTIYKDKTRRLLDKMPEYLEKIQQGYDINSIKQDVLNEYSSLLEVFGDFDSLMKAAVTKFKSSSQNLGRISGELQEGVMKIRMVPISQIFSRFPRVVRDLSRDLNKNVQLVIEGEDTELDKSVVEDLLDPIMHCVRNSLDHGVESPEVRKGLGKPEQGILLLKASNEGNMIVIEVADDGHGIDVEAVKQKAVERGILHPNKSLTDVEAFQLVFAPGFSTSKTISSVSGRGVGLDVVKTHIEKLNGTVMVESEPNVGTRFIIKLPLTLAIIQGLLIRVGDEVYSIPITSVIESHRVKPDEINRIDNYEVFNVRDEVYSLLRLNRLFGITSAETDDDGYNYIVVVGTEEKKVGLMVDSLIGEEAVVIKPLKDQFTNSPGIAGASILGDGSVSLIIDVAQLLELGLKQEMQARERREASIW [Source organism chain A]=Treponema denticola [UniProt ID chain B]=O85747 [UniProt boundaries chain B]=341-468 [UniProt coverage chain B]=15% [Name chain B]=Chemotaxis protein CheA [UniProt sequence chain B]=MSDYLDINNEELLKDFFSEAEQQVEILESNVLVIEQNPEDRNSIDEIFRAAHTLKGGSATVEMLELSKFTHAMEDLLDEIRSGSVKVTGETVDLLLKSIDIIKLMLDARASGSIYSDDVSGIVNQLRSFIPAKAEKKSSKASAPKVSIPASVSPVSAPKVQASASNLDIKDYFSEYEILELAETIQKGEDLYAVIVKFDESNLMNSVGGIQVFAALKDYGSVLKTVPDFDALYEDEFHETVIYFLSSASDSKILEKAAFIGDVTLSASAERLDIKDKTPESPKPAKAAPAQSAPEASVSEVKVSEKTEEKPVQESKEQPSKPEKKQSQTSPQGSGHSSGSILRVDANRIDYLLNLVSETVITKASLNQSTIEFAELYDKFQNSSTIYKDKTRRLLDKMPEYLEKIQQGYDINSIKQDVLNEYSSLLEVFGDFDSLMKAAVTKFKSSSQNLGRISGELQEGVMKIRMVPISQIFSRFPRVVRDLSRDLNKNVQLVIEGEDTELDKSVVEDLLDPIMHCVRNSLDHGVESPEVRKGLGKPEQGILLLKASNEGNMIVIEVADDGHGIDVEAVKQKAVERGILHPNKSLTDVEAFQLVFAPGFSTSKTISSVSGRGVGLDVVKTHIEKLNGTVMVESEPNVGTRFIIKLPLTLAIIQGLLIRVGDEVYSIPITSVIESHRVKPDEINRIDNYEVFNVRDEVYSLLRLNRLFGITSAETDDDGYNYIVVVGTEEKKVGLMVDSLIGEEAVVIKPLKDQFTNSPGIAGASILGDGSVSLIIDVAQLLELGLKQEMQARERREASIW [Source organism chain B]=Treponema denticola [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Treponema denticola [Accession]=MF7000419 [Entry] [Entry number]=604 [Entry name]=MKLP2 [PDB ID]=6yip [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:32356865). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O95235 [UniProt boundaries chain A]=596-664 [UniProt coverage chain A]=7% [Name chain A]=Kinesin-like protein KIF20A [UniProt sequence chain A]=MSQGILSPPAGLLSDDDVVVSPMFESTAADLGSVVRKNLLSDCSVVSTSLEDKQQVPSEDSMEKVKVYLRVRPLLPSELERQEDQGCVRIENVETLVLQAPKDSFALKSNERGIGQATHRFTFSQIFGPEVGQASFFNLTVKEMVKDVLKGQNWLIYTYGVTNSGKTHTIQGTIKDGGILPRSLALIFNSLQGQLHPTPDLKPLLSNEVIWLDSKQIRQEEMKKLSLLNGGLQEEELSTSLKRSVYIESRIGTSTSFDSGIAGLSSISQCTSSSQLDETSHRWAQPDTAPLPVPANIRFSIWISFFEIYNELLYDLLEPPSQQRKRQTLRLCEDQNGNPYVKDLNWIHVQDAEEAWKLLKVGRKNQSFASTHLNQNSSRSHSIFSIRILHLQGEGDIVPKISELSLCDLAGSERCKDQKSGERLKEAGNINTSLHTLGRCIAALRQNQQNRSKQNLVPFRDSKLTRVFQGFFTGRGRSCMIVNVNPCASTYDETLHVAKFSAIASQLVHAPPMQLGFPSLHSFIKEHSLQVSPSLEKGAKADTGLDDDIENEADISMYGKEELLQVVEAMKTLLLKERQEKLQLEMHLRDEICNEMVEQMQQREQWCSEHLDTQKELLEEMYEEKLNILKESLTSFYQEEIQERDEKIEELEALLQEARQQSVAHQQSGSELALRRSQRLAASASTQQLQEVKAKLQQCKAELNSTTEELHKYQKMLEPPPSAKPFTIDVDKKLEEGQKNIRLLRTELQKLGESLQSAERACCHSTGAGKLRQALTTCDDILIKQDQTLAELQNNMVLVKLDLRKKAACIAEQYHTVLKLQGQVSAKKRLGTNQENQQPNQQPPGKKPFLRNLLPRTPTCQSSTDCSPYARILRSRRSPLLKSGPFGKKY [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O95235 [UniProt boundaries chain B]=601-662 [UniProt coverage chain B]=6% [Name chain B]=Kinesin-like protein KIF20A [UniProt sequence chain B]=MSQGILSPPAGLLSDDDVVVSPMFESTAADLGSVVRKNLLSDCSVVSTSLEDKQQVPSEDSMEKVKVYLRVRPLLPSELERQEDQGCVRIENVETLVLQAPKDSFALKSNERGIGQATHRFTFSQIFGPEVGQASFFNLTVKEMVKDVLKGQNWLIYTYGVTNSGKTHTIQGTIKDGGILPRSLALIFNSLQGQLHPTPDLKPLLSNEVIWLDSKQIRQEEMKKLSLLNGGLQEEELSTSLKRSVYIESRIGTSTSFDSGIAGLSSISQCTSSSQLDETSHRWAQPDTAPLPVPANIRFSIWISFFEIYNELLYDLLEPPSQQRKRQTLRLCEDQNGNPYVKDLNWIHVQDAEEAWKLLKVGRKNQSFASTHLNQNSSRSHSIFSIRILHLQGEGDIVPKISELSLCDLAGSERCKDQKSGERLKEAGNINTSLHTLGRCIAALRQNQQNRSKQNLVPFRDSKLTRVFQGFFTGRGRSCMIVNVNPCASTYDETLHVAKFSAIASQLVHAPPMQLGFPSLHSFIKEHSLQVSPSLEKGAKADTGLDDDIENEADISMYGKEELLQVVEAMKTLLLKERQEKLQLEMHLRDEICNEMVEQMQQREQWCSEHLDTQKELLEEMYEEKLNILKESLTSFYQEEIQERDEKIEELEALLQEARQQSVAHQQSGSELALRRSQRLAASASTQQLQEVKAKLQQCKAELNSTTEELHKYQKMLEPPPSAKPFTIDVDKKLEEGQKNIRLLRTELQKLGESLQSAERACCHSTGAGKLRQALTTCDDILIKQDQTLAELQNNMVLVKLDLRKKAACIAEQYHTVLKLQGQVSAKKRLGTNQENQQPNQQPPGKKPFLRNLLPRTPTCQSSTDCSPYARILRSRRSPLLKSGPFGKKY [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.43 [Source organism]=Homo sapiens [Accession]=MF7000420 [Entry] [Entry number]=607 [Entry name]=Coiled coil domain of KKT4 (Leishmania mexicana) [PDB ID]=6zpj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=KKT4 coiled coil domain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:33915106). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000423,MF7000424 [UniProt ID chain A]=E9AN40 [UniProt boundaries chain A]=184-284 [UniProt coverage chain A]=13% [Name chain A]=BRCT domain-containing protein [UniProt sequence chain A]=MSTDAQELVRQLTENPEVLESMQHMISLLRANPPRISGSNNGGGLGNAETNGPERGAPQCVRPPRRGYGADVDCDHHQPTTRRKLRSSDGTAHSATSLSASSLTQEAHSFYGDDRVGARTTVSDHNGTTGGASSPTPSFVSTGSRAAPQVVTAASRHAPRRSSLLPSPHEHRPTTAPDEQLMATANKLTEAQRRIAELEKELQRTTQRVDQLSDVVQRQKDELQAAKDRHALEMEETRHAYNAVIHRKDEVQEEALRQLLKSRQLMVSAARYEAVVAAKKLHAQRLEKENNTGADDAMGSPKGLAGVQASANPNERGTHPGLAPSQTSVNARHSSTLGYGSGTTAKYSSALKRDRQNDEGDLVDDAGVETGAHEPGEARYGEAAHHHPPVKRTTLDTSRLQGSADRVVQGRRGVAATKAETSPAYITTPTPAGKASTALVGTRTQSSSARKRRTPRTPSRTNAERIAGSVAENRIRSQQRLPGTTSLKIESPTPVVSTAWTADRSLTGSRTPPPSSAGVCTVSEAVTKHHQLYPQQQVHQVPSTRPPLMQRAAGRLPPAPHRTAAASTAVPNTRSGTSSIASGGPTRSPSPVNPKRGAMLPRRFIFTGLKDHEPQRLVSAIAAVGEDAAALASDLDEPPPSSTTHIVLRGTPRSVKALCGVVSGKWLVSPEYVYNSQQSGFWLDELEEGGLRIFPPPLKCQRFLLTVEHPGIRAKLAQVIEYGGGEVLASGSDKRGPGAGDTVAQDVVVITSGDDLLRYATQDRV [Source organism chain A]=Leishmania mexicana [UniProt ID chain B]=E9AN40 [UniProt boundaries chain B]=184-258 [UniProt coverage chain B]=9% [Name chain B]=BRCT domain-containing protein [UniProt sequence chain B]=MSTDAQELVRQLTENPEVLESMQHMISLLRANPPRISGSNNGGGLGNAETNGPERGAPQCVRPPRRGYGADVDCDHHQPTTRRKLRSSDGTAHSATSLSASSLTQEAHSFYGDDRVGARTTVSDHNGTTGGASSPTPSFVSTGSRAAPQVVTAASRHAPRRSSLLPSPHEHRPTTAPDEQLMATANKLTEAQRRIAELEKELQRTTQRVDQLSDVVQRQKDELQAAKDRHALEMEETRHAYNAVIHRKDEVQEEALRQLLKSRQLMVSAARYEAVVAAKKLHAQRLEKENNTGADDAMGSPKGLAGVQASANPNERGTHPGLAPSQTSVNARHSSTLGYGSGTTAKYSSALKRDRQNDEGDLVDDAGVETGAHEPGEARYGEAAHHHPPVKRTTLDTSRLQGSADRVVQGRRGVAATKAETSPAYITTPTPAGKASTALVGTRTQSSSARKRRTPRTPSRTNAERIAGSVAENRIRSQQRLPGTTSLKIESPTPVVSTAWTADRSLTGSRTPPPSSAGVCTVSEAVTKHHQLYPQQQVHQVPSTRPPLMQRAAGRLPPAPHRTAAASTAVPNTRSGTSSIASGGPTRSPSPVNPKRGAMLPRRFIFTGLKDHEPQRLVSAIAAVGEDAAALASDLDEPPPSSTTHIVLRGTPRSVKALCGVVSGKWLVSPEYVYNSQQSGFWLDELEEGGLRIFPPPLKCQRFLLTVEHPGIRAKLAQVIEYGGGEVLASGSDKRGPGAGDTVAQDVVVITSGDDLLRYATQDRV [Source organism chain B]=Leishmania mexicana [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Leishmania mexicana [Accession]=MF7000423 [Entry] [Entry number]=608 [Entry name]=Coiled coil domain of KKT4 (Trypanosoma cruzi) [PDB ID]=6zpm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=KKT4 coiled coil domain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:33915106). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000423,MF7000424 [UniProt ID chain A]=A0A2V2WCI2 [UniProt boundaries chain A]=117-218 [UniProt coverage chain A]=15% [Name chain A]=Putative kinetoplastid kinetochore protein 4 [UniProt sequence chain A]=MEPNVLSVLQQLTSNPQLVGQLQSLLTVLSNVEQDGTGGGAMAARPAATTLGGIPSPALASAPSSVHPTQKRQGMSAAPRSASTQTASAARHARLVEANNSQLSSGVSEATAYEGVSLQRYEKLVKECRRLEEELEQKTHEASDASQRVRQLERETTRLMRRVEQLVSAVEGQKQKLDETEAKHKLELAEIENRHELEIQSKMSSHEEALRRLMDARRLMAAAVQYEQTLKSPAAERQLSAVVTPVNRRGLQSRPGSSNKQQQQRQWGNEKGAKREAEAEEKSAFVSQHSVPVKRERDGASRSLSAVYRKKRTPRTPSLTAADRVLATTDINSAATAAPHSKTKSHSAKVERELPHGPADTTAAFVENRYLVKARNPSSSTVSPGPAMSTITEAMARHHHQQKQQQQQQQRDATNNVESKFVAQYGAAVLPPAPSLPSPPPLPLPTTTKTSLATASRTPRQRRPPHAPLQQQHSRSGQRSGTSSVVGGPTRSPSPVNPKRGAEQPRCFVVTSLTEEERARVKAAVAAIGQHGVVLESDYEDPPPFTATHIVVRGPPRSMKALCGVVGSKWLVQPEYVYASRDAGFWLDEYEEGGLRCFPPPLKCQRFLLTMPEGIVKEKLEQVIEYGGGEVVRPARDGRSYDQGVVVIASGDDLLHFATRIE [Source organism chain A]=Trypanosoma cruzi [UniProt ID chain B]=A0A2V2WCI2 [UniProt boundaries chain B]=117-215 [UniProt coverage chain B]=14% [Name chain B]=Putative kinetoplastid kinetochore protein 4 [UniProt sequence chain B]=MEPNVLSVLQQLTSNPQLVGQLQSLLTVLSNVEQDGTGGGAMAARPAATTLGGIPSPALASAPSSVHPTQKRQGMSAAPRSASTQTASAARHARLVEANNSQLSSGVSEATAYEGVSLQRYEKLVKECRRLEEELEQKTHEASDASQRVRQLERETTRLMRRVEQLVSAVEGQKQKLDETEAKHKLELAEIENRHELEIQSKMSSHEEALRRLMDARRLMAAAVQYEQTLKSPAAERQLSAVVTPVNRRGLQSRPGSSNKQQQQRQWGNEKGAKREAEAEEKSAFVSQHSVPVKRERDGASRSLSAVYRKKRTPRTPSLTAADRVLATTDINSAATAAPHSKTKSHSAKVERELPHGPADTTAAFVENRYLVKARNPSSSTVSPGPAMSTITEAMARHHHQQKQQQQQQQRDATNNVESKFVAQYGAAVLPPAPSLPSPPPLPLPTTTKTSLATASRTPRQRRPPHAPLQQQHSRSGQRSGTSSVVGGPTRSPSPVNPKRGAEQPRCFVVTSLTEEERARVKAAVAAIGQHGVVLESDYEDPPPFTATHIVVRGPPRSMKALCGVVGSKWLVQPEYVYASRDAGFWLDEYEEGGLRCFPPPLKCQRFLLTMPEGIVKEKLEQVIEYGGGEVVRPARDGRSYDQGVVVIASGDDLLHFATRIE [Source organism chain B]=Trypanosoma cruzi [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Trypanosoma cruzi [Accession]=MF7000424 [Entry] [Entry number]=609 [Entry name]=Apoptosis inhibitor ORFV125 [PDB ID]=7ads [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=Analytical size-exclusion chromatography indicated only dimeric form. Domain-swapped homodimer, where A1 helices swap. Stability of the monomeric form was not addressed, but probably it is not very stable (PMID:33175095). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=A0A0R8HV90 [UniProt boundaries chain A]=4-142 [UniProt coverage chain A]=80% [Name chain A]=Apoptosis inhibitor [UniProt sequence chain A]=MANRDDIDASAVMAAYLAREYAEAVEEQLTPRERDALEALRVSGEEVRSPLLQELSNAGEHRANPENSHIPAALVSALLEAPTSPGRMVTAVELCAQMGRLWTRGRQLVDFMRLVYVLLDRLPPTADEDLGAWLQAVARVHGTRRRLHRALGVGAVVAGVGMLLLGVRVLRRT [Source organism chain A]=Orf virus [UniProt ID chain A-2]=A0A0R8HV90 [UniProt boundaries chain A-2]=4-142 [UniProt coverage chain A-2]=80% [Name chain A-2]=Apoptosis inhibitor [UniProt sequence chain A-2]=MANRDDIDASAVMAAYLAREYAEAVEEQLTPRERDALEALRVSGEEVRSPLLQELSNAGEHRANPENSHIPAALVSALLEAPTSPGRMVTAVELCAQMGRLWTRGRQLVDFMRLVYVLLDRLPPTADEDLGAWLQAVARVHGTRRRLHRALGVGAVVAGVGMLLLGVRVLRRT [Source organism chain A-2]=Orf virus [ExpTech]=X-ray [Resolution]=2.22 [Source organism]=Orf virus [Accession]=MF7000425 [Entry] [Entry number]=610 [Entry name]=Atypical Tm1 (Tm1-I/C) [PDB ID]=7bjg [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:34140355). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q8IGY1 [UniProt boundaries chain A]=487-583 [UniProt coverage chain A]=13% [Name chain A]=RE08101p [UniProt sequence chain A]=MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNESISRTFGIVSKRSQQVKRLENLSLGVDPQEKTQVQPQSGKTVAKPKQRQQKQLFKSDKAKEKSSRQQRKRAGTRSTRNPRTQSESSGLSSRWCSIEEQLNLLDDLLYYCDEEAELYLAQLYERFETLRRSRSSSPVSDFWSDSDMEHDDSSTSGTGSHTASNTSLVPASLKRRGHQHHPRFSGTRRPNVPNVQEILAALYRGDSKSALSNLRGETQPEEEQPQQQTEEVLPPSRSTLSLPLSESVTNSLGSNSPTPTDESSVQDEGASNPAAALIAEDAAPPAGTTTSKSKKKKREKGERSEKSDKSEKSDRKKKSSGKKERSKRSNPMEQSSDSLATDLSAGAIDEGIALADDDDNQAAEWSKLRCTSEAAEIVAEREARRNKGRCADYPGLAFGRSIFSSDTMMKFNIIRNELHNIMNTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKERYKDIGDDLDTAFVELILKE [Source organism chain A]=Drosophila melanogaster [UniProt ID chain A-2]=Q8IGY1 [UniProt boundaries chain A-2]=487-583 [UniProt coverage chain A-2]=13% [Name chain A-2]=RE08101p [UniProt sequence chain A-2]=MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNESISRTFGIVSKRSQQVKRLENLSLGVDPQEKTQVQPQSGKTVAKPKQRQQKQLFKSDKAKEKSSRQQRKRAGTRSTRNPRTQSESSGLSSRWCSIEEQLNLLDDLLYYCDEEAELYLAQLYERFETLRRSRSSSPVSDFWSDSDMEHDDSSTSGTGSHTASNTSLVPASLKRRGHQHHPRFSGTRRPNVPNVQEILAALYRGDSKSALSNLRGETQPEEEQPQQQTEEVLPPSRSTLSLPLSESVTNSLGSNSPTPTDESSVQDEGASNPAAALIAEDAAPPAGTTTSKSKKKKREKGERSEKSDKSEKSDRKKKSSGKKERSKRSNPMEQSSDSLATDLSAGAIDEGIALADDDDNQAAEWSKLRCTSEAAEIVAEREARRNKGRCADYPGLAFGRSIFSSDTMMKFNIIRNELHNIMNTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKERYKDIGDDLDTAFVELILKE [Source organism chain A-2]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=2.45 [Source organism]=Drosophila melanogaster [Accession]=MF7000426 [Entry] [Entry number]=616 [Entry name]=ZAD-domain of M1BP protein [PDB ID]=7po9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, AD-type [Sequence domain]=Zinc-finger associated domain (zf-AD) [Evidence level]=Direct evidence [Evidence text]=A common mechanism of dimerization of ZADs is dominated by hydrophobic interactions, which are part of one large hydrophobic core originating from the union of hydrophobic cores of adjacent monomers. The monomeric structure has two nearly perpendicular α-helices (α1 and α2) as well as looped regions knotted by a zinc ion. The helices of the monomers are definitely involved in helix packing interactions (PMID:35580610). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000971,MF7000432 [UniProt ID chain A]=Q9VHM3 [UniProt boundaries chain A]=8-95 [UniProt coverage chain A]=21% [Name chain A]=LD30467p [UniProt sequence chain A]=MSKSALKHLKSTCRVCAKYASNKRSPKLFERSNTKMIDNIEALTGLRLENYGCLPDQICECCSMELASAVKLRERCIAAQRELLLGLTEEQRQGISAFYRAAVMGEDIVQTVKTPDDDEVYATYQEIVLEEPKEEIDDTKVEYDNTYYEVAEGHAGEDDAASLIEEADYDSIMAEDEEQQQTLELDEDTELIVGDVNDAYVYDSDDEVAVLDNVLDDEYEHENIVVKKCSLPPKPKVRSDDARRRGTGGVYICEQCGNHIKGRMAFELHCRRHRGDKQFGCELCQSRFCTTSELKRHMRKHTGERPFACKYCGRCFTDYTTRVKHERTHTNERPYVCGTCGKAFTTGYILKNHMLIHSGERAYRCELCDKSFMLPTHLSTHFRSGVHKRHLEKAEMKQVLEQEQKRELKEEEEDSLHI [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=Q9VHM3 [UniProt boundaries chain B]=11-94 [UniProt coverage chain B]=20% [Name chain B]=LD30467p [UniProt sequence chain B]=MSKSALKHLKSTCRVCAKYASNKRSPKLFERSNTKMIDNIEALTGLRLENYGCLPDQICECCSMELASAVKLRERCIAAQRELLLGLTEEQRQGISAFYRAAVMGEDIVQTVKTPDDDEVYATYQEIVLEEPKEEIDDTKVEYDNTYYEVAEGHAGEDDAASLIEEADYDSIMAEDEEQQQTLELDEDTELIVGDVNDAYVYDSDDEVAVLDNVLDDEYEHENIVVKKCSLPPKPKVRSDDARRRGTGGVYICEQCGNHIKGRMAFELHCRRHRGDKQFGCELCQSRFCTTSELKRHMRKHTGERPFACKYCGRCFTDYTTRVKHERTHTNERPYVCGTCGKAFTTGYILKNHMLIHSGERAYRCELCDKSFMLPTHLSTHFRSGVHKRHLEKAEMKQVLEQEQKRELKEEEEDSLHI [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Drosophila melanogaster [Accession]=MF7000432 [Entry] [Entry number]=617 [Entry name]=ZNHIT3/NUFIP1 complex (Plasmodium falciparum) [PDB ID]=7qdw [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Pac-Hit fold domain + enclosed helix [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=This entry shows structural similarity to entry 2mjf (Pac-Hit fold domain + enclosed helix). There the amino acids involved in the interaction turned to be required for both stability and solubility of the two partners (PMID:25170085). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q8I2Y4 [UniProt boundaries chain A]=265-332 [UniProt coverage chain A]=20% [Name chain A]=Zinc finger protein, putative [UniProt sequence chain A]=MDEYDYNYATYDIDNFTNNFEDNLINYNQIDFINDNAEINNYSNEYYAYDEDLVEENVSEKRIHNKVLLSNDNEFDNNLINISNEIKTENSNNDTSLLKKRKIINDILLNIKKKMKKNDTLCIICLQNEKKYTFTCCYEYYCSLECFKKHDQQKCRNQNKNEPKISGSHNINMDDIKNSNHQKYEDTYYYQNEEDINKKQNDKVIENTIKLDNENKKNEINNINDMDTTCSNFPNNNLSTSLLNNDNNIPNNNENSESSDDYTDDYDMLTEEQKKKLKEDHTLKILLKNNYVREVFKQFTLSNDKIGYLSHYINDPTIVQVIDHIMKTIDDT [Source organism chain A]=Plasmodium falciparum [UniProt ID chain B]=Q8IK99 [UniProt boundaries chain B]=817-841 [UniProt coverage chain B]=2% [Name chain B]=FMR1-interacting protein 1 conserved domain-containing protein [UniProt sequence chain B]=MNNYEKKSNALDKKNSRNEFCEAYKTVEKMQINHYTVENNISTNEGMNIPYNDMYKEENVINQKDYTTTCNNLIYNESDELNGCNKIVEHNNNELKCLNRNKNNEALIISQSSTKYLENYFSSYNNNNNIHNHNNIHNIHNHNNIHNIHNHNNHNIHNIHNNPFCCKHNHMGCMNNHIKCINNQIGCFNHHIGCPNNHGDCNNKHICYYNIHDCNNNILKSEDKEEKQNLCQTFKQNYANNQTMLLSTPHSEGIVDNIHKQNDSEIKNEKNLDHNINLQGNNYTKNNMTHEQDYIYKEDISKNYNIVQNITNSFPSMINKKETDKGNVNNNKNKDKNEQNNEKENNNENEHSNVNGHNNVNEHSNVNEHSNVNEHSNVNKHNNTNVHNNENMWGYFNEGALYNFSSIYNAKQRRPYTNYGNHMKHHQNKMNNDTNNSYYNNNNYNNNNNNIGFIEKNNINKNNRNNKVNFDRGSKHNINFNNKRFNNYNNENKTEYNLNYEHKNKKSVHKYNYSHNNYNNNYYNNNNYKKNNYDKHRLNYNNNNHNNNNLNYSHEQNEESYTLPHSYDNNICNHPRNNIISSNPSTKGLNKQNNNYDKKKMDKANVKVNHNINNNRVINKEKSSNTFFCKYCNVNIEEGKLSDHNKNEHIICPIDDCNKIYNIDDMEVHLLNHMKNEKNEIILNDAKEIEKWISERKKNYPTRNKILNNMNKNESKKKNKPKCLIEELLFERYCSAIGKNLYHKNESEKSIFVPLLSKLSDKNYPNIYENSYYNISSSNNHSDIQKKRNKNPKGKEIIDTLNIHKRTPLIYQLMKNDIYTYEKKLIKSIEYITKNKFFDDSFNKKKKHIEEL [Source organism chain B]=Plasmodium falciparum [ExpTech]=NMR [Resolution]=N/A [Source organism]=Plasmodium falciparum [Accession]=MF7000433 [Entry] [Entry number]=618 [Entry name]=Red1-Iss10 complex [PDB ID]=7quu [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The authors produced Red1192–236, but 1D NMR analysis revealed that in absence of Iss10, the WT and mutated variants are unfolded. Red1 that contains the helix-turn-helix (HTH) is unfolded in isolation, furthermore there is a coiled coil interaction between helices a1 of the two proteins, which makes up a large fraction of the Iss10 region in the complex, so Iss10 is also most likely unfolded in isolation (no experiments done with monomeric Iss10) (PMID:36002457). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O14269 [UniProt boundaries chain A]=2-44 [UniProt coverage chain A]=7% [Name chain A]=Uncharacterized protein C7D4.14c [UniProt sequence chain A]=MDAVEPSVEKEYKKIISFRDTVFEGKHQQFLVPNNVRLKFLRDRLHKSLKNFDSVKRKVEIANDEGNNKLLKSSPKAQTRDENTPSEFKNGGFSNRESMSENCFSKSSTNLPRLDINRDFNSLLNSQTKPEATGLMKEDITPVVNTSKQSSTGTQEESSKPEKSNKLLAKSTLSLYGNQAFNPSSVLPSNSSSTPKENKKNVNKETYQPNTFRRSPLKNDTGSVELSNLYMPSPPSSALPVSLVSAPSPPRATNVAVPCLKHLESSEQGNNLLINKAFTSPRLPSPPQSTRPSSTRFPSVPLSDEKNSIVSVKNEEPSVILGNQSPISDLHPYSPSWIPYPKELQSLQVNRIPELSLENNVMSTRDYKDIMPHPRPSAVLLDKPVSLDQTSHPFPHQNTYILPPGIRNSVDYDGTFLSRKSLPPYNGIHRLHESPSQFSNQSRYNWEPILENRSLLHLNRPPPIETHYSYESNNSSFSPYYHKRHRQISPYYPTSSVYGVYESPPHMSDSRISRQHMPLTHTTYEPSAPYYNDYELAEEIERRRHHSFYDY [Source organism chain A]=Schizosaccharomyces pombe [UniProt ID chain B]=Q9UTR8 [UniProt boundaries chain B]=192-235 [UniProt coverage chain B]=6% [Name chain B]=NURS complex subunit red1 [UniProt sequence chain B]=MSRSINLDELRKKALESKKKNEEDESNDSDKEDGEISEDDPVIDQSNSVPPMKVPTFPEQIPQLPPFDRFPGTNANFFPFGAPFMLPPALMFGPNTVPFFPQTASSNKTFSKRKRSSENSFNNRNKAKSSETSDSSNTSQSFKENRALKDTATSRPLALSSDTSYQKSEKAKSEKSPFLSTSKNSDANYSKTTNQKEAEKAVSQLFEVGVRFNDFIAEGIEPSVVHTLFLKLGLDSSSASSQGSLTLSADKAARSAKLRKIDSNLSDTHILPGDNGTPTVLPERKNLISLPLLKQDDWLSSSKPFGSSTPNVVIEFDSDDDGDDFSNSKIEQSNLEKPPSNSENGLTMSRSDYLALLRNKEEEIRRMTKLILRLESNKKPYRSPTSAADMKLPSVPVAAVDNKSKTHLDTFEKVVDLSSKADFVEAGPSISSSGASSSAATTNSDTTEQILEAPWLRKTEQIAVVHEEHPAQIKKSEIDILNNLIEKEEGELTKYQTLVKSKTEILTQLYTRKKQLLEQQGKGNVACLPKESDLSMDSITEVSAQADENSSQILSSKTSNAPNGTTETDFEDKVPLVDYISPFYRFKSYRFNQQFVERVPLKYRSLTYSNKIEPMKVFCKYETTGGVCNDDHCEASHFRDIKMTDDEIIQDLSRYIEGNDEIEKESYKSGLDIVMKNTDENTDFVDVATRIVEYHNLWKSERMTIPVAKVSI [Source organism chain B]=Schizosaccharomyces pombe [ExpTech]=NMR [Resolution]=N/A [Source organism]=Schizosaccharomyces pombe [Accession]=MF7000434 [Entry] [Entry number]=619 [Entry name]=C-terminal domain of CapH (I99M mutant) [PDB ID]=7t5v [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disoder of the monomeric forms, however the dimer structure is highly intertwined, the helices are tightly packed between the monomers. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=A0A1X1LKI5 [UniProt boundaries chain A]=74-107 [UniProt coverage chain A]=31% [Name chain A]=Helix-turn-helix domain-containing protein [UniProt sequence chain A]=MATRLGEKLRDLRKQRGLTLEKLADMAGLSKSYLWELENRESQRPSAEKLTALADALGVGTSFFLEDDLREPEERHLDDAFFRGYKNLEPEAKAQLRKILDTFKKDF [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=A0A1X1LKI5 [UniProt boundaries chain A-2]=74-107 [UniProt coverage chain A-2]=31% [Name chain A-2]=Helix-turn-helix domain-containing protein [UniProt sequence chain A-2]=MATRLGEKLRDLRKQRGLTLEKLADMAGLSKSYLWELENRESQRPSAEKLTALADALGVGTSFFLEDDLREPEERHLDDAFFRGYKNLEPEAKAQLRKILDTFKKDF [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.26 [Source organism]=Escherichia coli [Accession]=MF7000435 [Entry] [Entry number]=622 [Entry name]=Tad1/ 1''-3' gcADPR complex [PDB ID]=7uaw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Thoeris anti-defense 1 [Evidence level]=Direct evidence [Evidence text]=Tightly interlocked homodimer with head to tail arrangement. Both, beta sheet augmentation and formation of a four-helix bundle by the C-terminal two helices of the monomers takes place for dimerization. Ligand binding is coordinated by both monomers (PMID:36174646). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000438,MF7000439 [UniProt ID chain A]=P0DW58 [UniProt boundaries chain A]=1-124 [UniProt coverage chain A]=100% [Name chain A]=Thoeris anti-defense 1 [UniProt sequence chain A]=MKELSTIQKREKLNTVERIGSEGPGGAYHEYVIKSNSMDSQGNYDVYETIKFQKGARKEEKSQHGVIDSDLLEIVRDRLKSFQAGPFSSRENACALTHVEEALMWMNRRVEDRIERNVLGTNTK [Source organism chain A]=Clostridium botulinum [UniProt ID chain B]=P0DW58 [UniProt boundaries chain B]=1-124 [UniProt coverage chain B]=100% [Name chain B]=Thoeris anti-defense 1 [UniProt sequence chain B]=MKELSTIQKREKLNTVERIGSEGPGGAYHEYVIKSNSMDSQGNYDVYETIKFQKGARKEEKSQHGVIDSDLLEIVRDRLKSFQAGPFSSRENACALTHVEEALMWMNRRVEDRIERNVLGTNTK [Source organism chain B]=Clostridium botulinum [ExpTech]=X-ray [Resolution]=1.72 [Source organism]=Clostridium botulinum [Accession]=MF7000438 [Entry] [Entry number]=623 [Entry name]=Tad1/ 1''-2' gcADPR complex [PDB ID]=8smd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Thoeris anti-defense 1 [Evidence level]=Direct evidence [Evidence text]=Tightly interlocked homodimer with head to tail arrangement. Both, beta sheet augmentation and formation of a four-helix bundle by the C-terminal two helices of the monomers takes place for dimerization. Ligand binding is coordinated by both monomers (PMID:36174646). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000438,MF7000439 [UniProt ID chain A]=P0DW58 [UniProt boundaries chain A]=1-124 [UniProt coverage chain A]=100% [Name chain A]=Thoeris anti-defense 1 [UniProt sequence chain A]=MKELSTIQKREKLNTVERIGSEGPGGAYHEYVIKSNSMDSQGNYDVYETIKFQKGARKEEKSQHGVIDSDLLEIVRDRLKSFQAGPFSSRENACALTHVEEALMWMNRRVEDRIERNVLGTNTK [Source organism chain A]=Clostridium botulinum [UniProt ID chain B]=P0DW58 [UniProt boundaries chain B]=2-124 [UniProt coverage chain B]=99% [Name chain B]=Thoeris anti-defense 1 [UniProt sequence chain B]=MKELSTIQKREKLNTVERIGSEGPGGAYHEYVIKSNSMDSQGNYDVYETIKFQKGARKEEKSQHGVIDSDLLEIVRDRLKSFQAGPFSSRENACALTHVEEALMWMNRRVEDRIERNVLGTNTK [Source organism chain B]=Clostridium botulinum [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Clostridium botulinum [Accession]=MF7000439 [Entry] [Entry number]=624 [Entry name]=C-terminal domain of flagelliform fibroin [PDB ID]=7vu7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Spidroin, C-terminal domain [Sequence domain]=- [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disoder of the monomeric forms, however the dimer structure is highly intertwined, the helices are tightly packed in the spidroin helical domain. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=A0A4Y2M0V6 [UniProt boundaries chain A]=2587-2675 [UniProt coverage chain A]=3% [Name chain A]=Flagelliform spidroin [UniProt sequence chain A]=GGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTESVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYRPGGAGGLYGPGGAGAPGGPGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYRPGGAGGLYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTESVTVGGAGGPGAGGVSRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGAGAPGGPGGAGGPGGPGGAGVSGGVVPAAGGAAPGAGGSGPTTVTEVVSITISGGQPSGGVLPGGSYTPAAGGSSRLPSLINGIMSSMQGGGFNYQNFGNVLSQFATGTGTCNSNDLNLLMDALLSALHTLSYQGMGTVPSYPSPSAMSAYSQSVRRCFGY [Source organism chain A]=Araneus ventricosus [UniProt ID chain B]=A0A4Y2M0V6 [UniProt boundaries chain B]=2587-2675 [UniProt coverage chain B]=3% [Name chain B]=Flagelliform spidroin [UniProt sequence chain B]=GGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTESVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYRPGGAGGLYGPGGAGAPGGPGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYRPGGAGGLYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTESVTVGGAGGPGAGGVSRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGPGAPGGPGGPGGPGGPGGPGGAGMGGGVGPGAGGVGGGAGGSGPVSVSSSVTVGGAGGPGAGGPGAGGPGAGGVGPGGLGGPGGFGGPGGPGGPGGPGAPGGGAGGLYGPGGAGGLYGPGGAGGMYGPGGAGGLYGPGGAGAPGGPGGPGGFGGPGGFGGAAGAGAGGVGPGGVSGGAGGSGPVTVTETVTVGGAGGPGAGGVGRPSGPGAGGAPGGFGGPGGPGGPGGPGGPGGPGGAAGGAGAGGVGPGGGASGGAGGAGPVSVSSSVVVGGAGGPGGPGAGGAGPGGAGPGGMYGPGGAGGLYGSGSGGSFGPGGGGAGAPGGPGGAGGPGGPGGAGVSGGVVPAAGGAAPGAGGSGPTTVTEVVSITISGGQPSGGVLPGGSYTPAAGGSSRLPSLINGIMSSMQGGGFNYQNFGNVLSQFATGTGTCNSNDLNLLMDALLSALHTLSYQGMGTVPSYPSPSAMSAYSQSVRRCFGY [Source organism chain B]=Araneus ventricosus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Araneus ventricosus [Accession]=MF7000440 [Entry] [Entry number]=625 [Entry name]=Periplasmic protein dimer [PDB ID]=7vw0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Six-helix bundle [Sequence domain]=Domain of unknown function (DUF305) [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disoder of the monomeric forms. An Orf91 protomer consists of three helices of which the C-terminal two helices belong to domain of unknown function 305 (DUF305), and two Orf91s dimerize into a six-helical bundle (PMID:35066349). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000441,MF7000442,MF7000443 [UniProt ID chain A]=V5J1S8 [UniProt boundaries chain A]=30-116 [UniProt coverage chain A]=75% [Name chain A]=DUF305 domain-containing protein [UniProt sequence chain A]=MKIKNTLFVILMLSLPAISAEHSEMKMSDMHSSASSQEYMAGMKNMHEKMMAAVNESNPDKAFAKGMIAHHEGAIAMAETELKYGKDPEMRKLAQDIIKAQKGEIEQMNKWLDSHK [Source organism chain A]=Escherichia coli [UniProt ID chain B]=V5J1S8 [UniProt boundaries chain B]=27-116 [UniProt coverage chain B]=77% [Name chain B]=DUF305 domain-containing protein [UniProt sequence chain B]=MKIKNTLFVILMLSLPAISAEHSEMKMSDMHSSASSQEYMAGMKNMHEKMMAAVNESNPDKAFAKGMIAHHEGAIAMAETELKYGKDPEMRKLAQDIIKAQKGEIEQMNKWLDSHK [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.45 [Source organism]=Escherichia coli [Accession]=MF7000441 [Entry] [Entry number]=626 [Entry name]=Periplasmic protein dimer [PDB ID]=7vw1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Six-helix bundle [Sequence domain]=Domain of unknown function (DUF305) [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disoder of the monomeric forms. An Orf91 protomer consists of three helices of which the C-terminal two helices belong to domain of unknown function 305 (DUF305), and two Orf91s dimerize into a six-helical bundle (PMID:35066349). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000441,MF7000442,MF7000443 [UniProt ID chain A]=V5J1S8 [UniProt boundaries chain A]=32-116 [UniProt coverage chain A]=73% [Name chain A]=DUF305 domain-containing protein [UniProt sequence chain A]=MKIKNTLFVILMLSLPAISAEHSEMKMSDMHSSASSQEYMAGMKNMHEKMMAAVNESNPDKAFAKGMIAHHEGAIAMAETELKYGKDPEMRKLAQDIIKAQKGEIEQMNKWLDSHK [Source organism chain A]=Escherichia coli [UniProt ID chain B]=V5J1S8 [UniProt boundaries chain B]=25-116 [UniProt coverage chain B]=79% [Name chain B]=DUF305 domain-containing protein [UniProt sequence chain B]=MKIKNTLFVILMLSLPAISAEHSEMKMSDMHSSASSQEYMAGMKNMHEKMMAAVNESNPDKAFAKGMIAHHEGAIAMAETELKYGKDPEMRKLAQDIIKAQKGEIEQMNKWLDSHK [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.49 [Source organism]=Escherichia coli [Accession]=MF7000442 [Entry] [Entry number]=627 [Entry name]=Periplasmic protein dimer [PDB ID]=7vw2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Six-helix bundle [Sequence domain]=Domain of unknown function (DUF305) [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disoder of the monomeric forms. An Orf91 protomer consists of three helices of which the C-terminal two helices belong to domain of unknown function 305 (DUF305), and two Orf91s dimerize into a six-helical bundle (PMID:35066349). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000441,MF7000442,MF7000443 [UniProt ID chain A]=V5J1S8 [UniProt boundaries chain A]=32-116 [UniProt coverage chain A]=73% [Name chain A]=DUF305 domain-containing protein [UniProt sequence chain A]=MKIKNTLFVILMLSLPAISAEHSEMKMSDMHSSASSQEYMAGMKNMHEKMMAAVNESNPDKAFAKGMIAHHEGAIAMAETELKYGKDPEMRKLAQDIIKAQKGEIEQMNKWLDSHK [Source organism chain A]=Escherichia coli [UniProt ID chain B]=V5J1S8 [UniProt boundaries chain B]=32-116 [UniProt coverage chain B]=73% [Name chain B]=DUF305 domain-containing protein [UniProt sequence chain B]=MKIKNTLFVILMLSLPAISAEHSEMKMSDMHSSASSQEYMAGMKNMHEKMMAAVNESNPDKAFAKGMIAHHEGAIAMAETELKYGKDPEMRKLAQDIIKAQKGEIEQMNKWLDSHK [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.19 [Source organism]=Escherichia coli [Accession]=MF7000443 [Entry] [Entry number]=628 [Entry name]=Formate dehydrogenase 1 [PDB ID]=7wz6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Basic helix-loop-helix (bHLH) [Sequence domain]=Helix-loop-helix DNA-binding domain [Evidence level]=Direct evidence [Evidence text]=Monomeric elements of basic helix-loop-helix domains were shown to be natively unfolded with a pH-dependent premolten globule conformation, as shown by several spectroscopic techniques (NMR, fluorescence, FTIR, and circular dichroism) (PMID:20102160,PMID:8303294, PMID:9488706). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2100009,MF2110021,MF2110023,MF2100010,MF7000192,MF7000402,MF7000403,MF7000444,MF7000371 [UniProt ID chain A]=P15806 [UniProt boundaries chain A]=547-606 [UniProt coverage chain A]=9% [Name chain A]=Transcription factor E2-alpha [UniProt sequence chain A]=MMNQSQRMAPVGSDKELSDLLDFSMMFPLPVANGKSRPASLGGTQFAGSGLEDRPSSGSWGSSDQNSSSFDPSRTYSEGAHFSDSHSSLPPSTFLGAGLGGKGSERNAYATFGRDTSVGTLSQAGFLPGELSLSSPGPLSPSGIKSSSQYYPSFPSNPRRRAADGGLDTQPKKVRKVPPGLPSSVYPPSSGDSYSRDAAAYPSAKTPSSAYPSPFYVADGSLHPSAELWSTPSQVGFGPMLGDGSSPLPLAPGSSSVGSGTFGGLQQQDRMGYQLHGSEVNGSLPAVSSFSAAPGTYSGTSGHTPPVSGAAAESLLGTRGTTASSSGDALGKALASIYSPDHSSNNFSPSPSTPVGSPQGLPGTSQWPRAGAPSALSPNYDAGLHGLSKMEDRLDEAIHVLRSHAVGTASDLHGLLPGHGALTTSFTGPMSLGGRHAGLVGGSHPEEGLTSGASLLHNHASLPSQPSSLPDLSQRPPDSYSGLGRAGTTAGASEIKREEKEDEEIASVADAEEDKKDLKVPRTRTSPDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLSSEKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQLALSAAHPGLGEAHNPAGHL [Source organism chain A]=Mus musculus [UniProt ID chain B]=P10085 [UniProt boundaries chain B]=116-165 [UniProt coverage chain B]=15% [Name chain B]=Myoblast determination protein 1 [UniProt sequence chain B]=MELLSPPLRDIDLTGPDGSLCSFETADDFYDDPCFDSPDLRFFEDLDPRLVHMGALLKPEEHAHFPTAVHPGPGAREDEHVRAPSGHHQAGRCLLWACKACKRKTTNADRRKAATMRERRRLSKVNEAFETLKRCTSSNPNQRLPKVEILRNAIRYIEGLQALLRDQDAAPPGAAAFYAPGPLPPGRGSEHYSGDSDASSPRSNCSDGMMDYSGPPSGPRRQNGYDTAYYSEAARESRPGKSAAVSSLDCLSSIVERISTDSPAAPALLLADAPPESPPGPPEGASLSDTEQGTQTPSPDAAPQCPAGSNPNAIYQVL [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Mus musculus [Accession]=MF7000444 [Entry] [Entry number]=629 [Entry name]=NAD-binding-2 domain-containing protein (mutant) [PDB ID]=8a5z [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=No contradicting information [Evidence text]=There is no information about the monomeric forms of the constituting partners. The C-terminal part is an intertwined, all-helical dimerization domain, while the N-terminal NADP-binding domain is well-folded. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=A0A0L8BGL4 [UniProt boundaries chain A]=2-293 [UniProt coverage chain A]=98% [Name chain A]=Uncharacterized protein [UniProt sequence chain A]=MKPSISVLGTGRMGSALARALLQAGYRTVVWNRTSEKAEPLAALGATVAPTVRQAIDASGIVIVNVSDYAATSTLLRASDVTPGLRGKLIVELTSGTPEGARETSQWTAAHGARYLDGAILATPDFIGTDAGTILLSGALEPFAANEDVFRALGGNVQHIGTEPGLANALDSAVLALMWGALFGGLHAIAVCRAEEIDLGELGRQWAATAPVVEGLVADLIKRTSAGRFVSDAETLSSISPHYGAFQHLKELMEARRIDRTVVDGYDAIFRRAIASGHLHDDFAALSQFMGKAEQP [Source organism chain A]=Ensifer adhaerens [UniProt ID chain B]=A0A0L8BGL4 [UniProt boundaries chain B]=1-295 [UniProt coverage chain B]=99% [Name chain B]=Uncharacterized protein [UniProt sequence chain B]=MKPSISVLGTGRMGSALARALLQAGYRTVVWNRTSEKAEPLAALGATVAPTVRQAIDASGIVIVNVSDYAATSTLLRASDVTPGLRGKLIVELTSGTPEGARETSQWTAAHGARYLDGAILATPDFIGTDAGTILLSGALEPFAANEDVFRALGGNVQHIGTEPGLANALDSAVLALMWGALFGGLHAIAVCRAEEIDLGELGRQWAATAPVVEGLVADLIKRTSAGRFVSDAETLSSISPHYGAFQHLKELMEARRIDRTVVDGYDAIFRRAIASGHLHDDFAALSQFMGKAEQP [Source organism chain B]=Ensifer adhaerens [ExpTech]=X-ray [Resolution]=2.31 [Source organism]=Ensifer adhaerens [Accession]=MF7000445 [Entry] [Entry number]=632 [Entry name]=Plasmalemma vesicle-associated protein, CC1 [PDB ID]=8arf [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:36107127). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=None [UniProt ID chain B]=Q96EA4 [UniProt boundaries chain B]=2-98 [UniProt coverage chain B]=16% [Name chain B]=Protein Spindly [UniProt sequence chain B]=MEADIITNLRCRLKEAEEERLKAAQYGLQLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEFEQQERLLAMLEQKNGEIKHLLGEIRNLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIESTKGELSIQRMKALFESQRALDIERKLFANERCLQLSESENMKLRAKLDELKLKYEPEETVEVPVLKKRREVLPVDITTAKDACVNNSALGGEVYRLPPQKEETQSCPNSLEDNNLQLEKSVSIYTPVVSLSPHKNLPVDMQLKKEKKCVKLIGVPADAEALSERSGNTPNSPRLAAESKLQTEVKEGKETSSKLEKETCKKLHPILYVSSKSTPETQCPQQ [Source organism chain B]=Homo sapiens [UniProt ID chain A]=Q96EA4 [UniProt boundaries chain A]=2-97 [UniProt coverage chain A]=15% [Name chain A]=Protein Spindly [UniProt sequence chain A]=MEADIITNLRCRLKEAEEERLKAAQYGLQLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEFEQQERLLAMLEQKNGEIKHLLGEIRNLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIESTKGELSIQRMKALFESQRALDIERKLFANERCLQLSESENMKLRAKLDELKLKYEPEETVEVPVLKKRREVLPVDITTAKDACVNNSALGGEVYRLPPQKEETQSCPNSLEDNNLQLEKSVSIYTPVVSLSPHKNLPVDMQLKKEKKCVKLIGVPADAEALSERSGNTPNSPRLAAESKLQTEVKEGKETSSKLEKETCKKLHPILYVSSKSTPETQCPQQ [Source organism chain A]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Homo sapiens [Accession]=MF7000448 [Entry] [Entry number]=634 [Entry name]=Ndc80:Nuf2 loop region [PDB ID]=8g0p [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:36883282). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O14777 [UniProt boundaries chain A]=370-509 [UniProt coverage chain A]=21% [Name chain A]=Kinetochore protein NDC80 homolog [UniProt sequence chain A]=MKRSSVSSGGAGRLSMQELRSQDVNKQGLYTPQTKEKPTFGKLSINKPTSERKVSLFGKRTSGHGSRNSQLGIFSSSEKIKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFLCPSYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHTAMKESSPLFDDGQPWGEETEDGIMHNKLFLDYTIKCYESFMSGADSFDEMNAELQSKLKDLFNVDAFKLESLEAKNRALNEQIARLEQEREKEPNRLESLRKLKASLQGDVQKYQAYMSNLESHSAILDQKLNGLNEEIARVELECETIKQENTRLQNIIDNQKYSVADIERINHERNELQQTINKLTKDLEAEQQKLWNEELKYARGKEAIETQLAEYHKLARKLKLIPKGAENSKGYDFEIKFNPEAGANCLVKYRAQVYVPLKELLNETEEEINKALNKKMGLEDTLEQLNAMITESKRSVRTLKEEVQKLDDLYQQKIKEAEEEDEKCASELESLEKHKHLLESTVNQGLSEAMNELDAVQREYQLVVQTTTEERRKVGNNLQRLLEMVATHVGSVEKHLEEQIAKVDREYEECMSEDLSENIKEIRDKYEKKATLIKSSEE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9BZD4 [UniProt boundaries chain B]=252-347 [UniProt coverage chain B]=20% [Name chain B]=Kinetochore protein Nuf2 [UniProt sequence chain B]=METLSFPRYNVAEIVIHIRNKILTGADGKNLTKNDLYPNPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSEVMYPHLMEGFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEGNSQKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEIFLNLKTALEKYHDGIEKAAEDSYAKIDEKTAELKRKMFKMST [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000450 [Entry] [Entry number]=635 [Entry name]=Escherichia Coli Glyoxalase I (Zn-bound) [PDB ID]=1fa5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P0AC81 [UniProt boundaries chain A]=1-135 [UniProt coverage chain A]=100% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AC81 [UniProt boundaries chain B]=1-135 [UniProt coverage chain B]=100% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Escherichia coli [Accession]=MF7000451 [Entry] [Entry number]=636 [Entry name]=Escherichia Coli Glyoxalase I (Ni-bound) [PDB ID]=1f9z [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P0AC81 [UniProt boundaries chain A]=1-135 [UniProt coverage chain A]=100% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AC81 [UniProt boundaries chain B]=1-135 [UniProt coverage chain B]=100% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Escherichia coli [Accession]=MF7000452 [Entry] [Entry number]=637 [Entry name]=Escherichia Coli Glyoxalase I (CO-bound) [PDB ID]=1fa6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P0AC81 [UniProt boundaries chain A]=1-135 [UniProt coverage chain A]=100% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AC81 [UniProt boundaries chain B]=1-135 [UniProt coverage chain B]=100% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Escherichia coli [Accession]=MF7000453 [Entry] [Entry number]=638 [Entry name]=Escherichia Coli Glyoxalase I (CD-bound) [PDB ID]=1fa7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P0AC81 [UniProt boundaries chain A]=1-135 [UniProt coverage chain A]=100% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AC81 [UniProt boundaries chain B]=1-135 [UniProt coverage chain B]=100% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Escherichia coli [Accession]=MF7000454 [Entry] [Entry number]=639 [Entry name]=Escherichia Coli Glyoxalase I (apo form) [PDB ID]=1fa8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P0AC81 [UniProt boundaries chain A]=1-135 [UniProt coverage chain A]=100% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AC81 [UniProt boundaries chain B]=1-135 [UniProt coverage chain B]=100% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Escherichia coli [Accession]=MF7000455 [Entry] [Entry number]=640 [Entry name]=Fosfomycin Resistance Protein A (FosA) with substrate [PDB ID]=1lqp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9I4K6 [UniProt boundaries chain A]=1-134 [UniProt coverage chain A]=99% [Name chain A]=Glutathione transferase FosA [UniProt sequence chain A]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9I4K6 [UniProt boundaries chain B]=1-134 [UniProt coverage chain B]=99% [Name chain B]=Glutathione transferase FosA [UniProt sequence chain B]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=1.19 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000456 [Entry] [Entry number]=641 [Entry name]=Fosfomycin Resistance Protein A (FosA) [PDB ID]=1lqk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9I4K6 [UniProt boundaries chain A]=1-134 [UniProt coverage chain A]=99% [Name chain A]=Glutathione transferase FosA [UniProt sequence chain A]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9I4K6 [UniProt boundaries chain B]=1-134 [UniProt coverage chain B]=99% [Name chain B]=Glutathione transferase FosA [UniProt sequence chain B]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000457 [Entry] [Entry number]=642 [Entry name]=Fosfomycin Resistance Protein A (FosA) with Tl [PDB ID]=1lqo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9I4K6 [UniProt boundaries chain A]=1-134 [UniProt coverage chain A]=99% [Name chain A]=Glutathione transferase FosA [UniProt sequence chain A]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9I4K6 [UniProt boundaries chain B]=1-134 [UniProt coverage chain B]=99% [Name chain B]=Glutathione transferase FosA [UniProt sequence chain B]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000458 [Entry] [Entry number]=643 [Entry name]=Fosfomycin Resistance Protein A (FosA) with phosphonoformate [PDB ID]=1nki [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9I4K6 [UniProt boundaries chain A]=1-134 [UniProt coverage chain A]=99% [Name chain A]=Glutathione transferase FosA [UniProt sequence chain A]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9I4K6 [UniProt boundaries chain B]=1-134 [UniProt coverage chain B]=99% [Name chain B]=Glutathione transferase FosA [UniProt sequence chain B]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=0.95 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000459 [Entry] [Entry number]=644 [Entry name]=Probable Fosfomycin Resistance Protein (PA1129) from Pseudomonas aeruginosa [PDB ID]=1nnr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9I4K6 [UniProt boundaries chain A]=1-134 [UniProt coverage chain A]=99% [Name chain A]=Glutathione transferase FosA [UniProt sequence chain A]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9I4K6 [UniProt boundaries chain B]=1-134 [UniProt coverage chain B]=99% [Name chain B]=Glutathione transferase FosA [UniProt sequence chain B]=MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGGPAADYTHYAFGIAAADFARFAAQLRAHGVREWKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLAACRQAPYAGMRFAD [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000460 [Entry] [Entry number]=645 [Entry name]=Mouse Glyoxalase I complex [PDB ID]=2za0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9CPU0 [UniProt boundaries chain A]=4-183 [UniProt coverage chain A]=97% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9CPU0 [UniProt boundaries chain B]=9-184 [UniProt coverage chain B]=95% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Mus musculus [Accession]=MF7000461 [Entry] [Entry number]=646 [Entry name]=EhpR from Enterobacter agglomerans [PDB ID]=3sk2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q8GPH6 [UniProt boundaries chain A]=1-129 [UniProt coverage chain A]=100% [Name chain A]=Phenazine antibiotic resistance protein EhpR [UniProt sequence chain A]=MTDLAGPTITPNLQLVYVSNVERSTDFYRFIFKKEPVFVTPRYVAFPSSGDALFAIWSGGEEPVAEIPRFSEIGIMLPTGEDVDKLFNEWTKQKSHQIIVIKEPYTDVFGRTFLISDPDGHIIRVCPLD [Source organism chain A]=Enterobacter agglomerans [UniProt ID chain B]=Q8GPH6 [UniProt boundaries chain B]=1-129 [UniProt coverage chain B]=100% [Name chain B]=Phenazine antibiotic resistance protein EhpR [UniProt sequence chain B]=MTDLAGPTITPNLQLVYVSNVERSTDFYRFIFKKEPVFVTPRYVAFPSSGDALFAIWSGGEEPVAEIPRFSEIGIMLPTGEDVDKLFNEWTKQKSHQIIVIKEPYTDVFGRTFLISDPDGHIIRVCPLD [Source organism chain B]=Enterobacter agglomerans [ExpTech]=X-ray [Resolution]=1.01 [Source organism]=Enterobacter agglomerans [Accession]=MF7000462 [Entry] [Entry number]=647 [Entry name]=Human Glyoxalase I with N-hydroxypyridone inhibitor [PDB ID]=3vw9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q04760 [UniProt boundaries chain A]=9-184 [UniProt coverage chain A]=95% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q04760 [UniProt boundaries chain B]=9-184 [UniProt coverage chain B]=95% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.47 [Source organism]=Homo sapiens [Accession]=MF7000463 [Entry] [Entry number]=648 [Entry name]=Mouse Glyoxalase I complexed with zopolrestat [PDB ID]=4kyh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9CPU0 [UniProt boundaries chain A]=6-182 [UniProt coverage chain A]=96% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9CPU0 [UniProt boundaries chain B]=9-184 [UniProt coverage chain B]=95% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Mus musculus [Accession]=MF7000464 [Entry] [Entry number]=649 [Entry name]=Mouse Glyoxalase I complexed with indomethacin [PDB ID]=4kyk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9CPU0 [UniProt boundaries chain A]=6-184 [UniProt coverage chain A]=97% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9CPU0 [UniProt boundaries chain B]=8-184 [UniProt coverage chain B]=96% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Mus musculus [Accession]=MF7000465 [Entry] [Entry number]=650 [Entry name]=FosB with Yn and sulfate (Bacillus cereus) [PDB ID]=4jh2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.27 [Source organism]=Bacillus cereus [Accession]=MF7000466 [Entry] [Entry number]=651 [Entry name]=FosB with Zn and Fosfomycin (Bacillus cereus) [PDB ID]=4jh3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Bacillus cereus [Accession]=MF7000467 [Entry] [Entry number]=652 [Entry name]=FosB with Ni and Fosfomycin (Bacillus cereus) [PDB ID]=4jh4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Bacillus cereus [Accession]=MF7000468 [Entry] [Entry number]=653 [Entry name]=FosB with Co and Fosfomycin (Bacillus cereus) [PDB ID]=4jh5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.77 [Source organism]=Bacillus cereus [Accession]=MF7000469 [Entry] [Entry number]=654 [Entry name]=FosB with Mn and Fosfomycin (Bacillus cereus) [PDB ID]=4jh6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.32 [Source organism]=Bacillus cereus [Accession]=MF7000470 [Entry] [Entry number]=655 [Entry name]=FosB with Mn and L-Cysteine-Fosfomycin (Bacillus cereus) [PDB ID]=4jh7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.55 [Source organism]=Bacillus cereus [Accession]=MF7000471 [Entry] [Entry number]=656 [Entry name]=FosB with Zn and L-Cysteine-Fosfomycin (Bacillus cereus) [PDB ID]=4jh8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.41 [Source organism]=Bacillus cereus [Accession]=MF7000472 [Entry] [Entry number]=657 [Entry name]=FosB with Mn and BSH-Fosfomycin (Bacillus cereus) [PDB ID]=4jh9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.77 [Source organism]=Bacillus cereus [Accession]=MF7000473 [Entry] [Entry number]=658 [Entry name]=FosB, apo form (Staphylococcus aureus) [PDB ID]=4nb2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P60864 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=99% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=P60864 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=99% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=1.89 [Source organism]=Staphylococcus aureus [Accession]=MF7000474 [Entry] [Entry number]=659 [Entry name]=FosB with BS-Cys9 disulfide (Staphylococcus aureus) [PDB ID]=4nb0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P60864 [UniProt boundaries chain A]=2-138 [UniProt coverage chain A]=98% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=P60864 [UniProt boundaries chain B]=2-138 [UniProt coverage chain B]=98% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=1.62 [Source organism]=Staphylococcus aureus [Accession]=MF7000475 [Entry] [Entry number]=660 [Entry name]=FosB with Zn and Sulfate (Staphylococcus aureus) [PDB ID]=4naz [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P60864 [UniProt boundaries chain A]=2-139 [UniProt coverage chain A]=99% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain A-2]=P60864 [UniProt boundaries chain A-2]=2-139 [UniProt coverage chain A-2]=99% [Name chain A-2]=Metallothiol transferase FosB [UniProt sequence chain A-2]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain A-2]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=1.15 [Source organism]=Staphylococcus aureus [Accession]=MF7000476 [Entry] [Entry number]=661 [Entry name]=FosB with Zn and Sulfate (Staphylococcus aureus) [PDB ID]=4nay [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P60864 [UniProt boundaries chain A]=2-138 [UniProt coverage chain A]=98% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain A-2]=P60864 [UniProt boundaries chain A-2]=2-138 [UniProt coverage chain A-2]=98% [Name chain A-2]=Metallothiol transferase FosB [UniProt sequence chain A-2]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain A-2]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=1.42 [Source organism]=Staphylococcus aureus [Accession]=MF7000477 [Entry] [Entry number]=662 [Entry name]=FosB with L-Cysteine-Cys9 disulfide (Staphylococcus aureus) [PDB ID]=4nb1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=P60864 [UniProt boundaries chain A]=1-139 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=P60864 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=99% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLKSINHICFSVRNLNDSIHFYRDILLGKLLLTGKKTAYFELAGLWIALNEEKDIPRNEIHFSYTHIAFTIDDSEFKYWHQRLKDNNVNILEGRVRDIRDRQSIYFTDPDGHKLELHTGTLENRLNYYKEAKPHMTFYK [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Staphylococcus aureus [Accession]=MF7000478 [Entry] [Entry number]=663 [Entry name]=Ni- and Zn-bound GloA2 [PDB ID]=4mtt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9I5L8 [UniProt boundaries chain A]=1-128 [UniProt coverage chain A]=97% [Name chain A]=Aldoketomutase [UniProt sequence chain A]=MRILHSMLRVADLEAALEFYTRALDMRLLRRRDYPEGRFTLAFVGYQDERAAAALELTHNWDRDGYTQGDGYGHLAIEVEDAAVTCARARALGYRVTREAGLMQHGRSVIAFLEDPDGYKVELIQKGTQFD [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9I5L8 [UniProt boundaries chain B]=1-127 [UniProt coverage chain B]=96% [Name chain B]=Aldoketomutase [UniProt sequence chain B]=MRILHSMLRVADLEAALEFYTRALDMRLLRRRDYPEGRFTLAFVGYQDERAAAALELTHNWDRDGYTQGDGYGHLAIEVEDAAVTCARARALGYRVTREAGLMQHGRSVIAFLEDPDGYKVELIQKGTQFD [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.17 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000479 [Entry] [Entry number]=664 [Entry name]=Ni-bound GloA2 [PDB ID]=4mtq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9I5L8 [UniProt boundaries chain A]=1-128 [UniProt coverage chain A]=97% [Name chain A]=Aldoketomutase [UniProt sequence chain A]=MRILHSMLRVADLEAALEFYTRALDMRLLRRRDYPEGRFTLAFVGYQDERAAAALELTHNWDRDGYTQGDGYGHLAIEVEDAAVTCARARALGYRVTREAGLMQHGRSVIAFLEDPDGYKVELIQKGTQFD [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9I5L8 [UniProt boundaries chain B]=1-128 [UniProt coverage chain B]=97% [Name chain B]=Aldoketomutase [UniProt sequence chain B]=MRILHSMLRVADLEAALEFYTRALDMRLLRRRDYPEGRFTLAFVGYQDERAAAALELTHNWDRDGYTQGDGYGHLAIEVEDAAVTCARARALGYRVTREAGLMQHGRSVIAFLEDPDGYKVELIQKGTQFD [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.17 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000480 [Entry] [Entry number]=665 [Entry name]=Ni- and Zn-bound GloA2 at high resolution [PDB ID]=4mts [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9I5L8 [UniProt boundaries chain A]=1-129 [UniProt coverage chain A]=98% [Name chain A]=Aldoketomutase [UniProt sequence chain A]=MRILHSMLRVADLEAALEFYTRALDMRLLRRRDYPEGRFTLAFVGYQDERAAAALELTHNWDRDGYTQGDGYGHLAIEVEDAAVTCARARALGYRVTREAGLMQHGRSVIAFLEDPDGYKVELIQKGTQFD [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9I5L8 [UniProt boundaries chain B]=1-127 [UniProt coverage chain B]=96% [Name chain B]=Aldoketomutase [UniProt sequence chain B]=MRILHSMLRVADLEAALEFYTRALDMRLLRRRDYPEGRFTLAFVGYQDERAAAALELTHNWDRDGYTQGDGYGHLAIEVEDAAVTCARARALGYRVTREAGLMQHGRSVIAFLEDPDGYKVELIQKGTQFD [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000481 [Entry] [Entry number]=666 [Entry name]=Zn-bound GloA2 [PDB ID]=4mtr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9I5L8 [UniProt boundaries chain A]=1-128 [UniProt coverage chain A]=97% [Name chain A]=Aldoketomutase [UniProt sequence chain A]=MRILHSMLRVADLEAALEFYTRALDMRLLRRRDYPEGRFTLAFVGYQDERAAAALELTHNWDRDGYTQGDGYGHLAIEVEDAAVTCARARALGYRVTREAGLMQHGRSVIAFLEDPDGYKVELIQKGTQFD [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9I5L8 [UniProt boundaries chain B]=1-127 [UniProt coverage chain B]=96% [Name chain B]=Aldoketomutase [UniProt sequence chain B]=MRILHSMLRVADLEAALEFYTRALDMRLLRRRDYPEGRFTLAFVGYQDERAAAALELTHNWDRDGYTQGDGYGHLAIEVEDAAVTCARARALGYRVTREAGLMQHGRSVIAFLEDPDGYKVELIQKGTQFD [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=1.83 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000482 [Entry] [Entry number]=667 [Entry name]=Mouse Glyoxalase I with baicalein [PDB ID]=4x2a [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9CPU0 [UniProt boundaries chain A]=15-181 [UniProt coverage chain A]=90% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9CPU0 [UniProt boundaries chain B]=8-183 [UniProt coverage chain B]=95% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Mus musculus [Accession]=MF7000483 [Entry] [Entry number]=668 [Entry name]=Mouse Glyoxalase I with 18-beta-glycyrrhetinic acid [PDB ID]=4pv5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q9CPU0 [UniProt boundaries chain A]=13-182 [UniProt coverage chain A]=92% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9CPU0 [UniProt boundaries chain B]=3-184 [UniProt coverage chain B]=98% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Mus musculus [Accession]=MF7000484 [Entry] [Entry number]=669 [Entry name]=Fosfomycin resistance protein (Klebsiella pneumoniae) [PDB ID]=5v91 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=A0A0E1CQ35 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=99% [Name chain A]=Fosfomycin resistance protein [UniProt sequence chain A]=MLSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLSCGDLWLCLSLDPQRRVTPPEESDYTHYAFSISEADFASFAARLEAAGVAVWKLNRSEGASHYFLDPDGHKLELHVGSLAQRLAACREQPYKGMVFFEQ [Source organism chain A]=Klebsiella pneumoniae 30660/NJST258_1 [UniProt ID chain B]=A0A0E1CQ35 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=99% [Name chain B]=Fosfomycin resistance protein [UniProt sequence chain B]=MLSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLSCGDLWLCLSLDPQRRVTPPEESDYTHYAFSISEADFASFAARLEAAGVAVWKLNRSEGASHYFLDPDGHKLELHVGSLAQRLAACREQPYKGMVFFEQ [Source organism chain B]=Klebsiella pneumoniae 30660/NJST258_1 [ExpTech]=X-ray [Resolution]=1.30 [Source organism]=Klebsiella pneumoniae 30660/NJST258_1 [Accession]=MF7000485 [Entry] [Entry number]=670 [Entry name]=Fosfomycin resistance protein with bound fosfomycin (Klebsiella pneumoniae) [PDB ID]=5v3d [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=A0A0E1CQ35 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=99% [Name chain A]=Fosfomycin resistance protein [UniProt sequence chain A]=MLSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLSCGDLWLCLSLDPQRRVTPPEESDYTHYAFSISEADFASFAARLEAAGVAVWKLNRSEGASHYFLDPDGHKLELHVGSLAQRLAACREQPYKGMVFFEQ [Source organism chain A]=Klebsiella pneumoniae 30660/NJST258_1 [UniProt ID chain B]=A0A0E1CQ35 [UniProt boundaries chain B]=1-137 [UniProt coverage chain B]=98% [Name chain B]=Fosfomycin resistance protein [UniProt sequence chain B]=MLSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLSCGDLWLCLSLDPQRRVTPPEESDYTHYAFSISEADFASFAARLEAAGVAVWKLNRSEGASHYFLDPDGHKLELHVGSLAQRLAACREQPYKGMVFFEQ [Source organism chain B]=Klebsiella pneumoniae 30660/NJST258_1 [ExpTech]=X-ray [Resolution]=1.54 [Source organism]=Klebsiella pneumoniae 30660/NJST258_1 [Accession]=MF7000486 [Entry] [Entry number]=671 [Entry name]=TnmS1 protein (Streptomyces sp. CB03234) [PDB ID]=5umq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=A0A125SA24 [UniProt boundaries chain A]=1-124 [UniProt coverage chain A]=98% [Name chain A]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain A]=MISHIGTIDVFVNDQDKAIDFYVNTLGFELREDQAFGPMRWVEVAPAGSQTRIVLCTKHFPVYEEGKIGRFTDIQLVTEDIKATHEELVRRGVNFTRAPEQMPFGGANASFQDPDGNEFLLLQPSR [Source organism chain A]=Streptomyces sp [UniProt ID chain B]=A0A125SA24 [UniProt boundaries chain B]=1-125 [UniProt coverage chain B]=99% [Name chain B]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain B]=MISHIGTIDVFVNDQDKAIDFYVNTLGFELREDQAFGPMRWVEVAPAGSQTRIVLCTKHFPVYEEGKIGRFTDIQLVTEDIKATHEELVRRGVNFTRAPEQMPFGGANASFQDPDGNEFLLLQPSR [Source organism chain B]=Streptomyces sp [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Streptomyces sp [Accession]=MF7000487 [Entry] [Entry number]=672 [Entry name]=TnmS3 protein (Streptomyces sp. CB03234) [PDB ID]=5ump [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=A0A125SA29 [UniProt boundaries chain A]=1-120 [UniProt coverage chain A]=96% [Name chain A]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain A]=MAISHVQLFSVPVSDQEKAKDFYVETVGFDLLADQPGVHGRWLQVAPKGADTSLVLVDWFPTMPPGSLRGLLLRTDDVDADCARLQERGVAVDGPKNTPWGRQAMFSDPDGNVIGLNQPSASAG [Source organism chain A]=Streptomyces sp [UniProt ID chain B]=A0A125SA29 [UniProt boundaries chain B]=1-120 [UniProt coverage chain B]=96% [Name chain B]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain B]=MAISHVQLFSVPVSDQEKAKDFYVETVGFDLLADQPGVHGRWLQVAPKGADTSLVLVDWFPTMPPGSLRGLLLRTDDVDADCARLQERGVAVDGPKNTPWGRQAMFSDPDGNVIGLNQPSASAG [Source organism chain B]=Streptomyces sp [ExpTech]=X-ray [Resolution]=1.08 [Source organism]=Streptomyces sp [Accession]=MF7000488 [Entry] [Entry number]=673 [Entry name]=TnmS3 protein with riboflavin [PDB ID]=5umx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=A0A125SA29 [UniProt boundaries chain A]=1-119 [UniProt coverage chain A]=95% [Name chain A]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain A]=MAISHVQLFSVPVSDQEKAKDFYVETVGFDLLADQPGVHGRWLQVAPKGADTSLVLVDWFPTMPPGSLRGLLLRTDDVDADCARLQERGVAVDGPKNTPWGRQAMFSDPDGNVIGLNQPSASAG [Source organism chain A]=Streptomyces sp [UniProt ID chain B]=A0A125SA29 [UniProt boundaries chain B]=1-119 [UniProt coverage chain B]=95% [Name chain B]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain B]=MAISHVQLFSVPVSDQEKAKDFYVETVGFDLLADQPGVHGRWLQVAPKGADTSLVLVDWFPTMPPGSLRGLLLRTDDVDADCARLQERGVAVDGPKNTPWGRQAMFSDPDGNVIGLNQPSASAG [Source organism chain B]=Streptomyces sp [ExpTech]=X-ray [Resolution]=1.59 [Source organism]=Streptomyces sp [Accession]=MF7000489 [Entry] [Entry number]=674 [Entry name]=TnmS3 protein with tiancimycin [PDB ID]=5umy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=A0A125SA29 [UniProt boundaries chain A]=1-120 [UniProt coverage chain A]=96% [Name chain A]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain A]=MAISHVQLFSVPVSDQEKAKDFYVETVGFDLLADQPGVHGRWLQVAPKGADTSLVLVDWFPTMPPGSLRGLLLRTDDVDADCARLQERGVAVDGPKNTPWGRQAMFSDPDGNVIGLNQPSASAG [Source organism chain A]=Streptomyces sp [UniProt ID chain B]=A0A125SA29 [UniProt boundaries chain B]=1-120 [UniProt coverage chain B]=96% [Name chain B]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain B]=MAISHVQLFSVPVSDQEKAKDFYVETVGFDLLADQPGVHGRWLQVAPKGADTSLVLVDWFPTMPPGSLRGLLLRTDDVDADCARLQERGVAVDGPKNTPWGRQAMFSDPDGNVIGLNQPSASAG [Source organism chain B]=Streptomyces sp [ExpTech]=X-ray [Resolution]=1.78 [Source organism]=Streptomyces sp [Accession]=MF7000490 [Entry] [Entry number]=675 [Entry name]=TnmS3 protein with TNM C [PDB ID]=6bbx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=A0A125SA29 [UniProt boundaries chain A]=1-120 [UniProt coverage chain A]=96% [Name chain A]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain A]=MAISHVQLFSVPVSDQEKAKDFYVETVGFDLLADQPGVHGRWLQVAPKGADTSLVLVDWFPTMPPGSLRGLLLRTDDVDADCARLQERGVAVDGPKNTPWGRQAMFSDPDGNVIGLNQPSASAG [Source organism chain A]=Streptomyces sp [UniProt ID chain B]=A0A125SA29 [UniProt boundaries chain B]=1-120 [UniProt coverage chain B]=96% [Name chain B]=Glyoxalase/bleomycin resisance protein/dioxygenase [UniProt sequence chain B]=MAISHVQLFSVPVSDQEKAKDFYVETVGFDLLADQPGVHGRWLQVAPKGADTSLVLVDWFPTMPPGSLRGLLLRTDDVDADCARLQERGVAVDGPKNTPWGRQAMFSDPDGNVIGLNQPSASAG [Source organism chain B]=Streptomyces sp [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Streptomyces sp [Accession]=MF7000491 [Entry] [Entry number]=676 [Entry name]=FosA3 with inhibitor (ANY1) [PDB ID]=5wep [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=D7UQM0 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=FosA3 [UniProt sequence chain A]=MLQGLNHLTLAVSDLASSLAFYQQLPGMRLHASWDSGAYLSCGALWLCLSLDEQRRKTPPQESDYTHYAFSVAEEEFAGVVALLAQAGAEVWKDNRSEGASYYFLDPDGHKLELHVGNLAQRLAACRERPYKGMVFFD [Source organism chain A]=Escherichia coli [UniProt ID chain B]=D7UQM0 [UniProt boundaries chain B]=1-137 [UniProt coverage chain B]=99% [Name chain B]=FosA3 [UniProt sequence chain B]=MLQGLNHLTLAVSDLASSLAFYQQLPGMRLHASWDSGAYLSCGALWLCLSLDEQRRKTPPQESDYTHYAFSVAEEEFAGVVALLAQAGAEVWKDNRSEGASYYFLDPDGHKLELHVGNLAQRLAACRERPYKGMVFFD [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=3.50 [Source organism]=Escherichia coli [Accession]=MF7000492 [Entry] [Entry number]=677 [Entry name]=N-demethylindolmycin synthase (PluN2) with N-demethylindolmycin [PDB ID]=6p29 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=A0A167HII1 [UniProt boundaries chain A]=1-132 [UniProt coverage chain A]=100% [Name chain A]=VOC domain-containing protein [UniProt sequence chain A]=MEFNNTIPELVCRDIDSSLSFYTHKLGFKVLFEREEQGFFFLYKNDIQLMLQQLGETAWMSHGNDTPFGNGMNIAFKVESLDDLDCSSPSEDIFLETETIEYRVLDGVASVNQVIFRDPDGYLIRFVEQVNQ [Source organism chain A]=Pseudoalteromonas luteoviolacea CPMOR-1 [UniProt ID chain B]=A0A167HII1 [UniProt boundaries chain B]=1-130 [UniProt coverage chain B]=98% [Name chain B]=VOC domain-containing protein [UniProt sequence chain B]=MEFNNTIPELVCRDIDSSLSFYTHKLGFKVLFEREEQGFFFLYKNDIQLMLQQLGETAWMSHGNDTPFGNGMNIAFKVESLDDLDCSSPSEDIFLETETIEYRVLDGVASVNQVIFRDPDGYLIRFVEQVNQ [Source organism chain B]=Pseudoalteromonas luteoviolacea CPMOR-1 [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Pseudoalteromonas luteoviolacea CPMOR-1 [Accession]=MF7000493 [Entry] [Entry number]=678 [Entry name]=FosB with Fosfomycin (Enterococcus faecium) [PDB ID]=7n7g [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=F1C939 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=99% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MIKGINHITYSVSNIAKSIEFYRDILGADILVESETLAYFNLGGIWLALNEEKNIPRSEIKYSYTHIAFTISDNDFEDWYNWLKENEVNILEGRDRDIRDKKSIYFTDLDGHKLELHTGSLEDRLSYYKEAKPHMNFYI [Source organism chain A]=Enterococcus faecium [UniProt ID chain B]=F1C939 [UniProt boundaries chain B]=1-139 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MIKGINHITYSVSNIAKSIEFYRDILGADILVESETLAYFNLGGIWLALNEEKNIPRSEIKYSYTHIAFTISDNDFEDWYNWLKENEVNILEGRDRDIRDKKSIYFTDLDGHKLELHTGSLEDRLSYYKEAKPHMNFYI [Source organism chain B]=Enterococcus faecium [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Enterococcus faecium [Accession]=MF7000494 [Entry] [Entry number]=679 [Entry name]=Glyoxalase (Gossypium hirsutum) [PDB ID]=7vq6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=A0A1U8Q028 [UniProt boundaries chain A]=6-180 [UniProt coverage chain A]=96% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MGSMDSKESPANNPGLHTPPDEATKGYIMQQTMFRIKDPKRTLEFYSRVLGMSLLNKVDVPYMKMTLYMMGYEDVSSAPSDPVEKTIWTFGRPATMELTHFWGTENDPEFKGYHNGNSEPIGFGHIGITVDDMYKACERFESLGVEFVKKPSDGYTFIKDPDGYWIEIFDLNGIRAIVNTL [Source organism chain A]=Gossypium hirsutum [UniProt ID chain B]=A0A1U8Q028 [UniProt boundaries chain B]=6-180 [UniProt coverage chain B]=96% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MGSMDSKESPANNPGLHTPPDEATKGYIMQQTMFRIKDPKRTLEFYSRVLGMSLLNKVDVPYMKMTLYMMGYEDVSSAPSDPVEKTIWTFGRPATMELTHFWGTENDPEFKGYHNGNSEPIGFGHIGITVDDMYKACERFESLGVEFVKKPSDGYTFIKDPDGYWIEIFDLNGIRAIVNTL [Source organism chain B]=Gossypium hirsutum [ExpTech]=X-ray [Resolution]=1.39 [Source organism]=Gossypium hirsutum [Accession]=MF7000495 [Entry] [Entry number]=680 [Entry name]=Human Glyoxalase I (with C-ter His tag) [PDB ID]=7wsz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q04760 [UniProt boundaries chain A]=9-184 [UniProt coverage chain A]=95% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q04760 [UniProt boundaries chain B]=9-182 [UniProt coverage chain B]=94% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.52 [Source organism]=Homo sapiens [Accession]=MF7000496 [Entry] [Entry number]=681 [Entry name]=Human Glyoxalase I (with C-ter His tag) with TLSC702 [PDB ID]=7wt0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q04760 [UniProt boundaries chain A]=2-184 [UniProt coverage chain A]=99% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q04760 [UniProt boundaries chain B]=2-184 [UniProt coverage chain B]=99% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000497 [Entry] [Entry number]=682 [Entry name]=Human Glyoxalase I (with C-ter His tag) in inhibitor-free form [PDB ID]=7wt1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q04760 [UniProt boundaries chain A]=9-184 [UniProt coverage chain A]=95% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q04760 [UniProt boundaries chain B]=9-184 [UniProt coverage chain B]=95% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.85 [Source organism]=Homo sapiens [Accession]=MF7000498 [Entry] [Entry number]=683 [Entry name]=Human Glyoxalase I with TLSC702 [PDB ID]=7wt2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q04760 [UniProt boundaries chain A]=2-184 [UniProt coverage chain A]=99% [Name chain A]=Lactoylglutathione lyase [UniProt sequence chain A]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q04760 [UniProt boundaries chain B]=2-184 [UniProt coverage chain B]=99% [Name chain B]=Lactoylglutathione lyase [UniProt sequence chain B]=MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000499 [Entry] [Entry number]=684 [Entry name]=FosB with Zinc and 2-phosphonopropionic acid (Bacillus cereus) [PDB ID]=8e7q [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Bacillus cereus [Accession]=MF7000500 [Entry] [Entry number]=685 [Entry name]=FosB Zinc and Phosphonoacetate (Bacillus cereus) [PDB ID]=8e7r [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.98 [Source organism]=Bacillus cereus [Accession]=MF7000501 [Entry] [Entry number]=686 [Entry name]=FosB with Zinc and (1-hydroxy-2-methylpropyl)phosphonic acid (Bacillus cereus) [PDB ID]=8g7g [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=2.23 [Source organism]=Bacillus cereus [Accession]=MF7000502 [Entry] [Entry number]=687 [Entry name]=FosB with Zinc and (1-hydroxypropan-2-yl)phosphonic acid (Bacillus cereus) [PDB ID]=8g7h [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.81 [Source organism]=Bacillus cereus [Accession]=MF7000503 [Entry] [Entry number]=688 [Entry name]=FosB with Zinc and Sulfate (Bacillus cereus) [PDB ID]=8g7i [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain A]=Q739M9 [UniProt boundaries chain A]=1-138 [UniProt coverage chain A]=100% [Name chain A]=Metallothiol transferase FosB [UniProt sequence chain A]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain A]=Bacillus cereus [UniProt ID chain B]=Q739M9 [UniProt boundaries chain B]=1-138 [UniProt coverage chain B]=100% [Name chain B]=Metallothiol transferase FosB [UniProt sequence chain B]=MLNGINHLCFSVSNLEDSIEFYEKVLEGELLVRGRKLAYFNICGVWVALNEEIHIPRNEIYQSYTHIAFSVEQKDFESLLQRLEENDVHILKGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREDKPHMTFY [Source organism chain B]=Bacillus cereus [ExpTech]=X-ray [Resolution]=1.83 [Source organism]=Bacillus cereus [Accession]=MF7000504 [Entry] [Entry number]=689 [Entry name]=Klebsiella pneumoniae fosfomycin-resistance protein (FosAKP) [PDB ID]=8r37 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [Evidence level]=Indirect evidence [Evidence text]=The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000098,MF7000451,MF7000452,MF7000453,MF7000454,MF7000455,MF7000082,MF7000456,MF7000457,MF7000458,MF7000102,MF7000459,MF7000460,MF7000083,MF7000084,MF7000103,MF7000104,MF7000461,MF7000462,MF7000463,MF7000464,MF7000465,MF7000466,MF7000467,MF7000468,MF7000469,MF7000470,MF7000471,MF7000472,MF7000473,MF7000322,MF7000474,MF7000475,MF7000476,MF7000477,MF7000478,MF7000479,MF7000480,MF7000481,MF7000482,MF7000483,MF7000484,MF7000485,MF7000486,MF7000487,MF7000488,MF7000489,MF7000490,MF7000491,MF7000492,MF7000493,MF7000494,MF7000495,MF7000496,MF7000497,MF7000498,MF7000499,MF7000500,MF7000501,MF7000502,MF7000503,MF7000504,MF7000323,MF7000505 [UniProt ID chain B]=A0A086IRG1 [UniProt boundaries chain B]=1-139 [UniProt coverage chain B]=100% [Name chain B]=FosA family fosfomycin resistance glutathione transferase [UniProt sequence chain B]=MLSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLSCGDLWLCLSLDPQRRVTPPEESDYTHYAFSISEADFASFAARLEAAGVAVWKLNRSEGASHYFLDPDGHKLELHVGSLAQRLAACREQPYKGMVFFEQ [Source organism chain B]=Klebsiella pneumoniae [UniProt ID chain A]=A0A086IRG1 [UniProt boundaries chain A]=1-139 [UniProt coverage chain A]=100% [Name chain A]=FosA family fosfomycin resistance glutathione transferase [UniProt sequence chain A]=MLSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLSCGDLWLCLSLDPQRRVTPPEESDYTHYAFSISEADFASFAARLEAAGVAVWKLNRSEGASHYFLDPDGHKLELHVGSLAQRLAACREQPYKGMVFFEQ [Source organism chain A]=Klebsiella pneumoniae [ExpTech]=X-ray [Resolution]=1.48 [Source organism]=Klebsiella pneumoniae [Accession]=MF7000505 [Entry] [Entry number]=690 [Entry name]=NADH oxidase (Thermus thermophilus) [PDB ID]=1nox [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q60049 [UniProt boundaries chain A]=6-205 [UniProt coverage chain A]=97% [Name chain A]=NADH dehydrogenase [UniProt sequence chain A]=MEATLPVLDAKTAALKRRSIRRYRKDPVPEGLLREILEAALRAPSAWNLQPWRIVVVRDPATKRALREAAFGQAHVEEAPVVLVLYADLEDALAHLDEVIHPGVQGERREAQKQAIQRAFAAMGQEARKAWASGQSYILLGYLLLLLEAYGLGSVPMLGFDPERVRAILGLPSHAAIPALVALGYPAEEGYPSHRLPLERVVLWR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q60049 [UniProt boundaries chain A-2]=6-205 [UniProt coverage chain A-2]=97% [Name chain A-2]=NADH dehydrogenase [UniProt sequence chain A-2]=MEATLPVLDAKTAALKRRSIRRYRKDPVPEGLLREILEAALRAPSAWNLQPWRIVVVRDPATKRALREAAFGQAHVEEAPVVLVLYADLEDALAHLDEVIHPGVQGERREAQKQAIQRAFAAMGQEARKAWASGQSYILLGYLLLLLEAYGLGSVPMLGFDPERVRAILGLPSHAAIPALVALGYPAEEGYPSHRLPLERVVLWR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.59 [Source organism]=Thermus thermophilus [Accession]=MF7000506 [Entry] [Entry number]=691 [Entry name]=NADPH:FMN oxidoreductase (Vibrio harveyi) [PDB ID]=1bkj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q56691 [UniProt boundaries chain A]=2-240 [UniProt coverage chain A]=99% [Name chain A]=NADPH-flavin oxidoreductase [UniProt sequence chain A]=MNNTIETILAHRSIRKFTAVPITDEQRQTIIQAGLAASSSSMLQVVSIVRVTDSEKRNELAQFAGNQAYVESAAEFLVFCIDYQRHATINPDVQADFTELTLIGAVDSGIMAQNCLLAAESMGLGGVYIGGLRNSAAQVDELLGLPENSAVLFGMCLGHPDQNPEVKPRLPAHVVVHENQYQELNLDDIQSYDQTMQAYYASRTSNQKLSTWSQEVTGKLAGESRPHILPYLNSKGLAKR [Source organism chain A]=Vibrio harveyi [UniProt ID chain B]=Q56691 [UniProt boundaries chain B]=2-240 [UniProt coverage chain B]=99% [Name chain B]=NADPH-flavin oxidoreductase [UniProt sequence chain B]=MNNTIETILAHRSIRKFTAVPITDEQRQTIIQAGLAASSSSMLQVVSIVRVTDSEKRNELAQFAGNQAYVESAAEFLVFCIDYQRHATINPDVQADFTELTLIGAVDSGIMAQNCLLAAESMGLGGVYIGGLRNSAAQVDELLGLPENSAVLFGMCLGHPDQNPEVKPRLPAHVVVHENQYQELNLDDIQSYDQTMQAYYASRTSNQKLSTWSQEVTGKLAGESRPHILPYLNSKGLAKR [Source organism chain B]=Vibrio harveyi [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Vibrio harveyi [Accession]=MF7000507 [Entry] [Entry number]=692 [Entry name]=NADPH:FMN oxidoreductase with NAD+ (Vibrio harveyi) [PDB ID]=2bkj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q56691 [UniProt boundaries chain A]=2-240 [UniProt coverage chain A]=99% [Name chain A]=NADPH-flavin oxidoreductase [UniProt sequence chain A]=MNNTIETILAHRSIRKFTAVPITDEQRQTIIQAGLAASSSSMLQVVSIVRVTDSEKRNELAQFAGNQAYVESAAEFLVFCIDYQRHATINPDVQADFTELTLIGAVDSGIMAQNCLLAAESMGLGGVYIGGLRNSAAQVDELLGLPENSAVLFGMCLGHPDQNPEVKPRLPAHVVVHENQYQELNLDDIQSYDQTMQAYYASRTSNQKLSTWSQEVTGKLAGESRPHILPYLNSKGLAKR [Source organism chain A]=Vibrio harveyi [UniProt ID chain B]=Q56691 [UniProt boundaries chain B]=2-240 [UniProt coverage chain B]=99% [Name chain B]=NADPH-flavin oxidoreductase [UniProt sequence chain B]=MNNTIETILAHRSIRKFTAVPITDEQRQTIIQAGLAASSSSMLQVVSIVRVTDSEKRNELAQFAGNQAYVESAAEFLVFCIDYQRHATINPDVQADFTELTLIGAVDSGIMAQNCLLAAESMGLGGVYIGGLRNSAAQVDELLGLPENSAVLFGMCLGHPDQNPEVKPRLPAHVVVHENQYQELNLDDIQSYDQTMQAYYASRTSNQKLSTWSQEVTGKLAGESRPHILPYLNSKGLAKR [Source organism chain B]=Vibrio harveyi [ExpTech]=X-ray [Resolution]=2.08 [Source organism]=Vibrio harveyi [Accession]=MF7000508 [Entry] [Entry number]=693 [Entry name]=FMN-dependent nitroreductase (Escherichia coli) [PDB ID]=1ds7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=1-217 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=1-217 [UniProt coverage chain B]=100% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.06 [Source organism]=Escherichia coli [Accession]=MF7000509 [Entry] [Entry number]=694 [Entry name]=Mutant flavoprotein (Escherichia coli) [PDB ID]=1f5v [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P17117 [UniProt boundaries chain A]=1-240 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P17117 [UniProt boundaries chain B]=1-240 [UniProt coverage chain B]=100% [Name chain B]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain B]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Escherichia coli [Accession]=MF7000510 [Entry] [Entry number]=695 [Entry name]=Nitroreductase with nicotinic acid (Escherichia coli) [PDB ID]=1icr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=2-217 [UniProt coverage chain A]=99% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=2-217 [UniProt coverage chain B]=99% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Escherichia coli [Accession]=MF7000511 [Entry] [Entry number]=696 [Entry name]=Prodrug-Activating-System CB1954 with FMN-dependent nitroreductase [PDB ID]=1idt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=1-217 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=2-217 [UniProt coverage chain B]=99% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Escherichia coli [Accession]=MF7000512 [Entry] [Entry number]=697 [Entry name]=Nitroreductase Prodrug-Activating System [PDB ID]=1oo5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=1-217 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=1-217 [UniProt coverage chain B]=100% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Escherichia coli [Accession]=MF7000513 [Entry] [Entry number]=698 [Entry name]=Nitroreductase with the dinitrobenzamide prodrug SN23862 (Escherichia coli) [PDB ID]=1oo6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=1-217 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=1-217 [UniProt coverage chain B]=100% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Escherichia coli [Accession]=MF7000514 [Entry] [Entry number]=699 [Entry name]=Nitroreductase with the dinitrobenzamide prodrug SN27217 (Escherichia coli) [PDB ID]=1oon [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=2-217 [UniProt coverage chain A]=99% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=2-217 [UniProt coverage chain B]=99% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.49 [Source organism]=Escherichia coli [Accession]=MF7000515 [Entry] [Entry number]=700 [Entry name]=Nitroreductase with the inhibitor dicoumarol (Escherichia coli) [PDB ID]=1ooq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=1-217 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=2-217 [UniProt coverage chain B]=99% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Escherichia coli [Accession]=MF7000516 [Entry] [Entry number]=701 [Entry name]=Nitroreductase with bound acetate (Escherichia coli) [PDB ID]=1ylr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=2-217 [UniProt coverage chain A]=99% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=1-217 [UniProt coverage chain B]=100% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Escherichia coli [Accession]=MF7000517 [Entry] [Entry number]=702 [Entry name]=Nitroreductase with bound acetate (Escherichia coli) [PDB ID]=1ylu [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=2-217 [UniProt coverage chain A]=99% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=2-217 [UniProt coverage chain B]=99% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Escherichia coli [Accession]=MF7000518 [Entry] [Entry number]=703 [Entry name]=Hypothetical oxidoreductase YcnD (Bacillus subtilis) [PDB ID]=1zch [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P94424 [UniProt boundaries chain A]=1-249 [UniProt coverage chain A]=100% [Name chain A]=FMN reductase [NAD(P)H] [UniProt sequence chain A]=MNEVIKSLTDHRSIRSYTDEPVAQEQLDQIIEAVQSAPSSINGQQVTVITVQDKERKKKISELAGGQPWIDQAPVFLLFCADFNRAKIALEDLHDFKMEITNGLESVLVGAVDAGIALGTATAAAESLGLGTVPIGAVRGNPQELIELLELPKYVFPLSGLVIGHPADRSAKKPRLPQEAVNHQETYLNQDELTSHIQAYDEQMSEYMNKRTNGKETRNWSQSIASYYERLYYPHIREMLEKQGFKVEK [Source organism chain A]=Bacillus subtilis [UniProt ID chain A-2]=P94424 [UniProt boundaries chain A-2]=1-249 [UniProt coverage chain A-2]=100% [Name chain A-2]=FMN reductase [NAD(P)H] [UniProt sequence chain A-2]=MNEVIKSLTDHRSIRSYTDEPVAQEQLDQIIEAVQSAPSSINGQQVTVITVQDKERKKKISELAGGQPWIDQAPVFLLFCADFNRAKIALEDLHDFKMEITNGLESVLVGAVDAGIALGTATAAAESLGLGTVPIGAVRGNPQELIELLELPKYVFPLSGLVIGHPADRSAKKPRLPQEAVNHQETYLNQDELTSHIQAYDEQMSEYMNKRTNGKETRNWSQSIASYYERLYYPHIREMLEKQGFKVEK [Source organism chain A-2]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.85 [Source organism]=Bacillus subtilis [Accession]=MF7000519 [Entry] [Entry number]=704 [Entry name]=Mouse iodotyrosine deiodinase (IYD) with to FMN and mono-iodotyrosine (MIT) [PDB ID]=3gfd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q9DCX8 [UniProt boundaries chain A]=66-285 [UniProt coverage chain A]=77% [Name chain A]=Iodotyrosine deiodinase 1 [UniProt sequence chain A]=MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9DCX8 [UniProt boundaries chain B]=66-285 [UniProt coverage chain B]=77% [Name chain B]=Iodotyrosine deiodinase 1 [UniProt sequence chain B]=MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.45 [Source organism]=Mus musculus [Accession]=MF7000520 [Entry] [Entry number]=705 [Entry name]=Mouse iodotyrosine deiodinase (IYD) with FMN [PDB ID]=3gb5 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q9DCX8 [UniProt boundaries chain A]=68-285 [UniProt coverage chain A]=76% [Name chain A]=Iodotyrosine deiodinase 1 [UniProt sequence chain A]=MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=Q9DCX8 [UniProt boundaries chain A-2]=68-285 [UniProt coverage chain A-2]=76% [Name chain A-2]=Iodotyrosine deiodinase 1 [UniProt sequence chain A-2]=MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Mus musculus [Accession]=MF7000521 [Entry] [Entry number]=706 [Entry name]=Nitroreductase CinD with FMN (Lactococcus lactis) [PDB ID]=2wqf [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q9CED0 [UniProt boundaries chain A]=2-202 [UniProt coverage chain A]=99% [Name chain A]=Nitroreductase domain-containing protein [UniProt sequence chain A]=MSFIKSLENRRTIYALGRNVQDEEKVIETIKEAVRFSPTAFNSQTGRLLILTGDAQDKLWDEIVAPELKAAMEAQGVPESAWDNTRAKLDGFKAAFGTILFFEDQAVVKNLQEQFALYADNFPVWSEQGSGIISVNVWTALAELGLGANLQHYNPLIDEAVAKEWNLPESWKLRGQLVFGSIEAPAGEKTFMDDADRFIVAK [Source organism chain A]=Lactococcus lactis subsp lactis [UniProt ID chain A-2]=Q9CED0 [UniProt boundaries chain A-2]=2-202 [UniProt coverage chain A-2]=99% [Name chain A-2]=Nitroreductase domain-containing protein [UniProt sequence chain A-2]=MSFIKSLENRRTIYALGRNVQDEEKVIETIKEAVRFSPTAFNSQTGRLLILTGDAQDKLWDEIVAPELKAAMEAQGVPESAWDNTRAKLDGFKAAFGTILFFEDQAVVKNLQEQFALYADNFPVWSEQGSGIISVNVWTALAELGLGANLQHYNPLIDEAVAKEWNLPESWKLRGQLVFGSIEAPAGEKTFMDDADRFIVAK [Source organism chain A-2]=Lactococcus lactis subsp lactis [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=Lactococcus lactis subsp lactis [Accession]=MF7000522 [Entry] [Entry number]=707 [Entry name]=Mouse iodotyrosine deiodinase (IYD) C217A, C239A with FMN and mono-iodotyrosine (MIT) [PDB ID]=3tnz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q9DCX8 [UniProt boundaries chain A]=66-285 [UniProt coverage chain A]=77% [Name chain A]=Iodotyrosine deiodinase 1 [UniProt sequence chain A]=MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9DCX8 [UniProt boundaries chain B]=66-285 [UniProt coverage chain B]=77% [Name chain B]=Iodotyrosine deiodinase 1 [UniProt sequence chain B]=MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Mus musculus [Accession]=MF7000523 [Entry] [Entry number]=708 [Entry name]=Mouse iodotyrosine deiodinase (IYD) C217A, C239A with FMN [PDB ID]=3to0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q9DCX8 [UniProt boundaries chain A]=68-285 [UniProt coverage chain A]=76% [Name chain A]=Iodotyrosine deiodinase 1 [UniProt sequence chain A]=MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9DCX8 [UniProt boundaries chain B]=68-285 [UniProt coverage chain B]=76% [Name chain B]=Iodotyrosine deiodinase 1 [UniProt sequence chain B]=MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.66 [Source organism]=Mus musculus [Accession]=MF7000524 [Entry] [Entry number]=709 [Entry name]=Human iodotyrosine deiodinase (IYD) with FMN [PDB ID]=4ttb [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q6PHW0 [UniProt boundaries chain A]=71-289 [UniProt coverage chain A]=75% [Name chain A]=Iodotyrosine deiodinase 1 [UniProt sequence chain A]=MYFLTPILVAILCILVVWIFKNADRSMEKKKGEPRTRAEARPWVDEDLKDSSDLHQAEEDADEWQESEENVEHIPFSHNHYPEKEMVKRSQEFYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNCGPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRKPLDQIMVTV [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q6PHW0 [UniProt boundaries chain B]=71-289 [UniProt coverage chain B]=75% [Name chain B]=Iodotyrosine deiodinase 1 [UniProt sequence chain B]=MYFLTPILVAILCILVVWIFKNADRSMEKKKGEPRTRAEARPWVDEDLKDSSDLHQAEEDADEWQESEENVEHIPFSHNHYPEKEMVKRSQEFYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNCGPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRKPLDQIMVTV [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.45 [Source organism]=Homo sapiens [Accession]=MF7000525 [Entry] [Entry number]=710 [Entry name]=NfrA1 (Bacillus megaterium) [PDB ID]=5hdj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=A0A0K0VJM9 [UniProt boundaries chain A]=2-248 [UniProt coverage chain A]=99% [Name chain A]=NfrA1 [UniProt sequence chain A]=MNSVIETILNHRSIRKYEDKPLSEEQIQTIVESAQAASTSSYIQAYSIIGVKDKETKRKLAQLAGNQPYVETNGHFFVFCADFHRHDVIAEMEKKDLSTALESTEQFMVAIIDVALAAQNATLAAESMGLGACYIGGLRNELEEVSKLLKLPHHVIPLFGLTVGHPAGITDKKPRLPFKHVYHEETYEPNDEQTKKELTAYNEEISAYYNERTNGKRQDTWTGQMAEMLSNPKRMYMKEFVEKQGFNKK [Source organism chain A]=Priestia megaterium [UniProt ID chain B]=A0A0K0VJM9 [UniProt boundaries chain B]=1-248 [UniProt coverage chain B]=99% [Name chain B]=NfrA1 [UniProt sequence chain B]=MNSVIETILNHRSIRKYEDKPLSEEQIQTIVESAQAASTSSYIQAYSIIGVKDKETKRKLAQLAGNQPYVETNGHFFVFCADFHRHDVIAEMEKKDLSTALESTEQFMVAIIDVALAAQNATLAAESMGLGACYIGGLRNELEEVSKLLKLPHHVIPLFGLTVGHPAGITDKKPRLPFKHVYHEETYEPNDEQTKKELTAYNEEISAYYNERTNGKRQDTWTGQMAEMLSNPKRMYMKEFVEKQGFNKK [Source organism chain B]=Priestia megaterium [ExpTech]=X-ray [Resolution]=1.89 [Source organism]=Priestia megaterium [Accession]=MF7000526 [Entry] [Entry number]=711 [Entry name]=Iodotyrosine deiodinase (IYD) with FMN (Haliscomenobacter hydrossis) [PDB ID]=5ko7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=F4KU78 [UniProt boundaries chain A]=5-222 [UniProt coverage chain A]=98% [Name chain A]=Iodotyrosine deiodinase [UniProt sequence chain A]=MKQKPAFIPYAGAQFEPEEMLSKSAEYYQFMDHRRTVREFSNRAIPLEVIENIVMTASTAPSGAHKQPWTFVVVSDPQIKAKIRQAAEKEEFESYNGRMSNEWLEDLQPFGTDWHKPFLEIAPYLIVVFRKAYDVLPDGTQRKNYYVQESVGIACGFLLAAIHQAGLVALTHTPSPMNFLQKILQRPENERPFLLVPVGYPAEGAMVPDLQRKDKAAVMVVY [Source organism chain A]=Haliscomenobacter hydrossis [UniProt ID chain B]=F4KU78 [UniProt boundaries chain B]=5-222 [UniProt coverage chain B]=98% [Name chain B]=Iodotyrosine deiodinase [UniProt sequence chain B]=MKQKPAFIPYAGAQFEPEEMLSKSAEYYQFMDHRRTVREFSNRAIPLEVIENIVMTASTAPSGAHKQPWTFVVVSDPQIKAKIRQAAEKEEFESYNGRMSNEWLEDLQPFGTDWHKPFLEIAPYLIVVFRKAYDVLPDGTQRKNYYVQESVGIACGFLLAAIHQAGLVALTHTPSPMNFLQKILQRPENERPFLLVPVGYPAEGAMVPDLQRKDKAAVMVVY [Source organism chain B]=Haliscomenobacter hydrossis [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Haliscomenobacter hydrossis [Accession]=MF7000527 [Entry] [Entry number]=712 [Entry name]=NfsA with nitrofurantoin (Escherichia coli) [PDB ID]=7nb9 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P17117 [UniProt boundaries chain A]=1-240 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P17117 [UniProt boundaries chain A-2]=1-240 [UniProt coverage chain A-2]=100% [Name chain A-2]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A-2]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.09 [Source organism]=Escherichia coli [Accession]=MF7000528 [Entry] [Entry number]=713 [Entry name]=NfsA with FMN (Escherichia coli) [PDB ID]=7niy [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P17117 [UniProt boundaries chain A]=1-240 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P17117 [UniProt boundaries chain A-2]=1-240 [UniProt coverage chain A-2]=100% [Name chain A-2]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A-2]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.03 [Source organism]=Escherichia coli [Accession]=MF7000529 [Entry] [Entry number]=714 [Entry name]=NfsA with hydroquinone (Escherichia coli) [PDB ID]=7nmp [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P17117 [UniProt boundaries chain A]=1-240 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P17117 [UniProt boundaries chain A-2]=1-240 [UniProt coverage chain A-2]=100% [Name chain A-2]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A-2]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.25 [Source organism]=Escherichia coli [Accession]=MF7000530 [Entry] [Entry number]=715 [Entry name]=NfsA with 1,4-benzoquinone (Escherichia coli) [PDB ID]=7nnx [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P17117 [UniProt boundaries chain A]=1-240 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P17117 [UniProt boundaries chain A-2]=1-240 [UniProt coverage chain A-2]=100% [Name chain A-2]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A-2]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Escherichia coli [Accession]=MF7000531 [Entry] [Entry number]=716 [Entry name]=FMN and NADPH-dependent nitroreductase NfnB (Sphingopyxis sp. strain HMH) [PDB ID]=7dp0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=A0A2L0VUJ4 [UniProt boundaries chain A]=9-231 [UniProt coverage chain A]=95% [Name chain A]=Nitroreductase family protein [UniProt sequence chain A]=MPATDTLSLSASEALARRRSVRAFTDRPVDRALLARIFEIAQRAPSGGNLQPWQATVVTGERWQAVQDAVAARIVMGREGFQPEYDIYPRGLTDPWDSRRFGVGEALYASLGIARDDKAGRIAQFQQNYRGFGAPVMLFLHCSRIMGPPQWADMGMWLQSVMLLLVEHGLASCPQECWAMYGATVRAELGLGDDQILFSGLAIGHADEEAPVNRWPVPRVGLDEVIDWQGFDA [Source organism chain A]=Sphingopyxis sp MG [UniProt ID chain B]=A0A2L0VUJ4 [UniProt boundaries chain B]=9-231 [UniProt coverage chain B]=95% [Name chain B]=Nitroreductase family protein [UniProt sequence chain B]=MPATDTLSLSASEALARRRSVRAFTDRPVDRALLARIFEIAQRAPSGGNLQPWQATVVTGERWQAVQDAVAARIVMGREGFQPEYDIYPRGLTDPWDSRRFGVGEALYASLGIARDDKAGRIAQFQQNYRGFGAPVMLFLHCSRIMGPPQWADMGMWLQSVMLLLVEHGLASCPQECWAMYGATVRAELGLGDDQILFSGLAIGHADEEAPVNRWPVPRVGLDEVIDWQGFDA [Source organism chain B]=Sphingopyxis sp MG [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Sphingopyxis sp MG [Accession]=MF7000532 [Entry] [Entry number]=717 [Entry name]=FMN and NADPH-dependent nitroreductase NfnB, mutant Y88F (Sphingopyxis sp. strain HMH) [PDB ID]=7dp2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=A0A2L0VUJ4 [UniProt boundaries chain A]=9-231 [UniProt coverage chain A]=95% [Name chain A]=Nitroreductase family protein [UniProt sequence chain A]=MPATDTLSLSASEALARRRSVRAFTDRPVDRALLARIFEIAQRAPSGGNLQPWQATVVTGERWQAVQDAVAARIVMGREGFQPEYDIYPRGLTDPWDSRRFGVGEALYASLGIARDDKAGRIAQFQQNYRGFGAPVMLFLHCSRIMGPPQWADMGMWLQSVMLLLVEHGLASCPQECWAMYGATVRAELGLGDDQILFSGLAIGHADEEAPVNRWPVPRVGLDEVIDWQGFDA [Source organism chain A]=Sphingopyxis sp MG [UniProt ID chain B]=A0A2L0VUJ4 [UniProt boundaries chain B]=9-231 [UniProt coverage chain B]=95% [Name chain B]=Nitroreductase family protein [UniProt sequence chain B]=MPATDTLSLSASEALARRRSVRAFTDRPVDRALLARIFEIAQRAPSGGNLQPWQATVVTGERWQAVQDAVAARIVMGREGFQPEYDIYPRGLTDPWDSRRFGVGEALYASLGIARDDKAGRIAQFQQNYRGFGAPVMLFLHCSRIMGPPQWADMGMWLQSVMLLLVEHGLASCPQECWAMYGATVRAELGLGDDQILFSGLAIGHADEEAPVNRWPVPRVGLDEVIDWQGFDA [Source organism chain B]=Sphingopyxis sp MG [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Sphingopyxis sp MG [Accession]=MF7000533 [Entry] [Entry number]=718 [Entry name]=FMN and NADPH-dependent nitroreductase NfnB, mutant Y88A (Sphingopyxis sp. strain HMH) [PDB ID]=7dp1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=A0A2L0VUJ4 [UniProt boundaries chain A]=9-231 [UniProt coverage chain A]=95% [Name chain A]=Nitroreductase family protein [UniProt sequence chain A]=MPATDTLSLSASEALARRRSVRAFTDRPVDRALLARIFEIAQRAPSGGNLQPWQATVVTGERWQAVQDAVAARIVMGREGFQPEYDIYPRGLTDPWDSRRFGVGEALYASLGIARDDKAGRIAQFQQNYRGFGAPVMLFLHCSRIMGPPQWADMGMWLQSVMLLLVEHGLASCPQECWAMYGATVRAELGLGDDQILFSGLAIGHADEEAPVNRWPVPRVGLDEVIDWQGFDA [Source organism chain A]=Sphingopyxis sp MG [UniProt ID chain B]=A0A2L0VUJ4 [UniProt boundaries chain B]=9-231 [UniProt coverage chain B]=95% [Name chain B]=Nitroreductase family protein [UniProt sequence chain B]=MPATDTLSLSASEALARRRSVRAFTDRPVDRALLARIFEIAQRAPSGGNLQPWQATVVTGERWQAVQDAVAARIVMGREGFQPEYDIYPRGLTDPWDSRRFGVGEALYASLGIARDDKAGRIAQFQQNYRGFGAPVMLFLHCSRIMGPPQWADMGMWLQSVMLLLVEHGLASCPQECWAMYGATVRAELGLGDDQILFSGLAIGHADEEAPVNRWPVPRVGLDEVIDWQGFDA [Source organism chain B]=Sphingopyxis sp MG [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Sphingopyxis sp MG [Accession]=MF7000534 [Entry] [Entry number]=719 [Entry name]=Oxidized iodotyrosine deiodinase (IYD) with to FMN and L-Tyrosine [PDB ID]=6pz0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=B9K712 [UniProt boundaries chain A]=2-186 [UniProt coverage chain A]=99% [Name chain A]=Iodotyrosine deiodinase [UniProt sequence chain A]=MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF [Source organism chain A]=Thermotoga neapolitana [UniProt ID chain B]=B9K712 [UniProt boundaries chain B]=3-186 [UniProt coverage chain B]=98% [Name chain B]=Iodotyrosine deiodinase [UniProt sequence chain B]=MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF [Source organism chain B]=Thermotoga neapolitana [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Thermotoga neapolitana [Accession]=MF7000535 [Entry] [Entry number]=720 [Entry name]=Oxidized iodotyrosine deiodinase (IYD) with FMN and 3-iodo-L-tyrosine [PDB ID]=6q1l [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=B9K712 [UniProt boundaries chain A]=3-186 [UniProt coverage chain A]=98% [Name chain A]=Iodotyrosine deiodinase [UniProt sequence chain A]=MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF [Source organism chain A]=Thermotoga neapolitana [UniProt ID chain B]=B9K712 [UniProt boundaries chain B]=3-186 [UniProt coverage chain B]=98% [Name chain B]=Iodotyrosine deiodinase [UniProt sequence chain B]=MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF [Source organism chain B]=Thermotoga neapolitana [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Thermotoga neapolitana [Accession]=MF7000536 [Entry] [Entry number]=721 [Entry name]=FMN-dependent oxidoreductase RubE7 [PDB ID]=7vqk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=A0A3N6GWZ7 [UniProt boundaries chain A]=5-199 [UniProt coverage chain A]=97% [Name chain A]=Putative malonic semialdehyde reductase RutE [UniProt sequence chain A]=MAGHPLALDEAAQDLLFREARTANTFAPTHIGDEHIEAIYDLVKWGPTSMNQQPMRVVLVRSDESRRALLQHVLEGNRDKVASAPLVAVLAADLSFPDTLPRLFPHAPNARHAYADENARRESAVFNTALQLGYFIIGIRAGGLAAGPIAGFDPEGVHKEFFPGEPVLVTSIVNIGYPGPDAFSARLPRLGYREVVRSV [Source organism chain A]=Streptomyces sp ADI95-17 [UniProt ID chain B]=A0A3N6GWZ7 [UniProt boundaries chain B]=5-199 [UniProt coverage chain B]=97% [Name chain B]=Putative malonic semialdehyde reductase RutE [UniProt sequence chain B]=MAGHPLALDEAAQDLLFREARTANTFAPTHIGDEHIEAIYDLVKWGPTSMNQQPMRVVLVRSDESRRALLQHVLEGNRDKVASAPLVAVLAADLSFPDTLPRLFPHAPNARHAYADENARRESAVFNTALQLGYFIIGIRAGGLAAGPIAGFDPEGVHKEFFPGEPVLVTSIVNIGYPGPDAFSARLPRLGYREVVRSV [Source organism chain B]=Streptomyces sp ADI95-17 [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Streptomyces sp ADI95-17 [Accession]=MF7000537 [Entry] [Entry number]=722 [Entry name]=Nitroreductase with 1-methyl-5-nitroimidazole (Haemophilus influenzae Rd KW20) [PDB ID]=7t2z [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q57431 [UniProt boundaries chain A]=2-220 [UniProt coverage chain A]=99% [Name chain A]=Putative NAD(P)H nitroreductase [UniProt sequence chain A]=MTQLTREQVLELFHQRSSTRYYDPTKKISDEDFECILECGRLSPSSVGSEPWKFLVIQNKTLREKMKPFSWGMINQLDNCSHLVVILAKKNARYDSPFFVDVMARKGLNAEQQQAALTKYKALQEEDMKLLENDRTLFDWCSKQTYIALANMLTGASALGIDSCPIEGFHYDKMNECLAEEGLFDPQEYAVSVAATFGYRSRDIAKKSRKGLDEVVKWVG [Source organism chain A]=Haemophilus influenzae [UniProt ID chain B]=Q57431 [UniProt boundaries chain B]=2-220 [UniProt coverage chain B]=99% [Name chain B]=Putative NAD(P)H nitroreductase [UniProt sequence chain B]=MTQLTREQVLELFHQRSSTRYYDPTKKISDEDFECILECGRLSPSSVGSEPWKFLVIQNKTLREKMKPFSWGMINQLDNCSHLVVILAKKNARYDSPFFVDVMARKGLNAEQQQAALTKYKALQEEDMKLLENDRTLFDWCSKQTYIALANMLTGASALGIDSCPIEGFHYDKMNECLAEEGLFDPQEYAVSVAATFGYRSRDIAKKSRKGLDEVVKWVG [Source organism chain B]=Haemophilus influenzae [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Haemophilus influenzae [Accession]=MF7000538 [Entry] [Entry number]=723 [Entry name]=Nitroreductase with nicotinic acid (Haemophilus influenzae Rd KW20) [PDB ID]=7t33 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q57431 [UniProt boundaries chain A]=2-220 [UniProt coverage chain A]=99% [Name chain A]=Putative NAD(P)H nitroreductase [UniProt sequence chain A]=MTQLTREQVLELFHQRSSTRYYDPTKKISDEDFECILECGRLSPSSVGSEPWKFLVIQNKTLREKMKPFSWGMINQLDNCSHLVVILAKKNARYDSPFFVDVMARKGLNAEQQQAALTKYKALQEEDMKLLENDRTLFDWCSKQTYIALANMLTGASALGIDSCPIEGFHYDKMNECLAEEGLFDPQEYAVSVAATFGYRSRDIAKKSRKGLDEVVKWVG [Source organism chain A]=Haemophilus influenzae [UniProt ID chain B]=Q57431 [UniProt boundaries chain B]=2-220 [UniProt coverage chain B]=99% [Name chain B]=Putative NAD(P)H nitroreductase [UniProt sequence chain B]=MTQLTREQVLELFHQRSSTRYYDPTKKISDEDFECILECGRLSPSSVGSEPWKFLVIQNKTLREKMKPFSWGMINQLDNCSHLVVILAKKNARYDSPFFVDVMARKGLNAEQQQAALTKYKALQEEDMKLLENDRTLFDWCSKQTYIALANMLTGASALGIDSCPIEGFHYDKMNECLAEEGLFDPQEYAVSVAATFGYRSRDIAKKSRKGLDEVVKWVG [Source organism chain B]=Haemophilus influenzae [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Haemophilus influenzae [Accession]=MF7000539 [Entry] [Entry number]=724 [Entry name]=NfsA (Escherichia coli) [PDB ID]=7q0o [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P17117 [UniProt boundaries chain A]=1-240 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P17117 [UniProt boundaries chain A-2]=1-240 [UniProt coverage chain A-2]=100% [Name chain A-2]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A-2]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=0.96 [Source organism]=Escherichia coli [Accession]=MF7000540 [Entry] [Entry number]=725 [Entry name]=NfsA with Fumarate (Escherichia coli) [PDB ID]=8ajx [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P17117 [UniProt boundaries chain A]=1-240 [UniProt coverage chain A]=100% [Name chain A]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P17117 [UniProt boundaries chain A-2]=1-240 [UniProt coverage chain A-2]=100% [Name chain A-2]=Oxygen-insensitive NADPH nitroreductase [UniProt sequence chain A-2]=MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.25 [Source organism]=Escherichia coli [Accession]=MF7000541 [Entry] [Entry number]=726 [Entry name]=NfsB-T41Q/N71S/F124T mutant (Escherichia coli) [PDB ID]=8c5e [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=2-217 [UniProt coverage chain A]=99% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=2-217 [UniProt coverage chain B]=99% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Escherichia coli [Accession]=MF7000542 [Entry] [Entry number]=727 [Entry name]=NfsB mutant N71S T41L (Escherichia coli) [PDB ID]=8c5p [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=2-217 [UniProt coverage chain A]=99% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=2-217 [UniProt coverage chain B]=99% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.69 [Source organism]=Escherichia coli [Accession]=MF7000543 [Entry] [Entry number]=728 [Entry name]=NfsB mutant T41LN71S (Escherichia coli) [PDB ID]=8ccv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=P38489 [UniProt boundaries chain A]=2-217 [UniProt coverage chain A]=99% [Name chain A]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain A]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P38489 [UniProt boundaries chain B]=2-217 [UniProt coverage chain B]=99% [Name chain B]=Oxygen-insensitive NAD(P)H nitroreductase [UniProt sequence chain B]=MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Escherichia coli [Accession]=MF7000544 [Entry] [Entry number]=729 [Entry name]=NfsB_Vv F70A/F108Ywith FMN (Vibrio vulnificus) [PDB ID]=7uwt [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Nitroreductase family [Evidence level]=Indirect evidence [Evidence text]=Authors claim that the homodimeric NAD(P)H nitroreductase is a highly intertwined dimer with the FMN binding site lying at the dimer interface (PMID:18241886). Other structures belonging to the nitroreductase family also have an extensive interaction surface wherein a large hydrophobic solvent-accessible surface becomes buried upon dimer formation, suggesting that the monomers would be unstable on their own (PMID:16229462, PMID:19436071). Domain-swapping is also typical, where the extended C-terminal region extensively interacts with the core domain of the neighbouring monomer, forming an interlocked dimer (PMID:34473996, PMID:19436071, PMID:8885832). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000506,MF7000507,MF7000508,MF7000509,MF7000510,MF7000511,MF7000512,MF7000513,MF7000514,MF7000515,MF7000516,MF7000517,MF7000518,MF7000519,MF7000239,MF7000240,MF7000520,MF7000521,MF7000522,MF7000523,MF7000524,MF7000525,MF7000526,MF7000527,MF7000528,MF7000529,MF7000530,MF7000531,MF7000532,MF7000533,MF7000534,MF7000535,MF7000536,MF7000537,MF7000538,MF7000539,MF7000540,MF7000541,MF7000542,MF7000543,MF7000544,MF7000545 [UniProt ID chain A]=Q7MCD2 [UniProt boundaries chain A]=1-217 [UniProt coverage chain A]=100% [Name chain A]=Nitroreductase [UniProt sequence chain A]=MTIVQAAQSRYSTKAFDASRKLPEEKVAAVKELIRMSASSVNSQPWHFIVASSEEGKARIAKATQGGFAFNERKILDASHVVVFCAKTAIDEAYLLDLLESEDKDGRFADVEAKNGMHAGRSFFVNMHRFDLKDAHHWMEKQVYLNVGTLLLGASAMEIDAVPIEGFDAKVLDEEFGLREKGFTSVVIVPLGYHSEDDFNAKLPKSRWSAETVFTEI [Source organism chain A]=Vibrio vulnificus [UniProt ID chain A-2]=Q7MCD2 [UniProt boundaries chain A-2]=1-217 [UniProt coverage chain A-2]=100% [Name chain A-2]=Nitroreductase [UniProt sequence chain A-2]=MTIVQAAQSRYSTKAFDASRKLPEEKVAAVKELIRMSASSVNSQPWHFIVASSEEGKARIAKATQGGFAFNERKILDASHVVVFCAKTAIDEAYLLDLLESEDKDGRFADVEAKNGMHAGRSFFVNMHRFDLKDAHHWMEKQVYLNVGTLLLGASAMEIDAVPIEGFDAKVLDEEFGLREKGFTSVVIVPLGYHSEDDFNAKLPKSRWSAETVFTEI [Source organism chain A-2]=Vibrio vulnificus [ExpTech]=X-ray [Resolution]=1.85 [Source organism]=Vibrio vulnificus [Accession]=MF7000545 [Entry] [Entry number]=730 [Entry name]=MT-ADPRase with ADPR [PDB ID]=1mk1 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=O33199 [UniProt boundaries chain A]=6-207 [UniProt coverage chain A]=97% [Name chain A]=MutT/nudix family protein [UniProt sequence chain A]=MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=O33199 [UniProt boundaries chain A-2]=6-207 [UniProt coverage chain A-2]=97% [Name chain A-2]=MutT/nudix family protein [UniProt sequence chain A-2]=MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000546 [Entry] [Entry number]=731 [Entry name]=MT-ADPRase, apo form (Mycobacterium tuberculosis) [PDB ID]=1mp2 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=O33199 [UniProt boundaries chain A]=6-207 [UniProt coverage chain A]=97% [Name chain A]=MutT/nudix family protein [UniProt sequence chain A]=MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=O33199 [UniProt boundaries chain A-2]=6-207 [UniProt coverage chain A-2]=97% [Name chain A-2]=MutT/nudix family protein [UniProt sequence chain A-2]=MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000547 [Entry] [Entry number]=732 [Entry name]=MT-ADPRase with Gd and ADP-ribose [PDB ID]=1mqe [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=O33199 [UniProt boundaries chain A]=6-207 [UniProt coverage chain A]=97% [Name chain A]=MutT/nudix family protein [UniProt sequence chain A]=MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=O33199 [UniProt boundaries chain A-2]=6-207 [UniProt coverage chain A-2]=97% [Name chain A-2]=MutT/nudix family protein [UniProt sequence chain A-2]=MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000548 [Entry] [Entry number]=733 [Entry name]=ADP-ribose pyrophosphatase with ADP-ribose and Zn [PDB ID]=1v8r [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-169 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-169 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Thermus thermophilus [Accession]=MF7000549 [Entry] [Entry number]=734 [Entry name]=ADP-ribose pyrophosphatase with ribose-5'-phosphate and Zn [PDB ID]=1v8t [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-168 [UniProt coverage chain A]=92% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-168 [UniProt coverage chain A-2]=92% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Thermus thermophilus [Accession]=MF7000550 [Entry] [Entry number]=735 [Entry name]=ADP-ribose pyrophosphatase [PDB ID]=1v8i [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-168 [UniProt coverage chain A]=92% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-168 [UniProt coverage chain A-2]=92% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.76 [Source organism]=Thermus thermophilus [Accession]=MF7000551 [Entry] [Entry number]=736 [Entry name]=ADP-ribose pyrophosphatase with Zn [PDB ID]=1v8n [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-168 [UniProt coverage chain A]=92% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-168 [UniProt coverage chain A-2]=92% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.74 [Source organism]=Thermus thermophilus [Accession]=MF7000552 [Entry] [Entry number]=737 [Entry name]=ADP-ribose pyrophosphatase (E86Q mutant) with ADP-ribose and Zn [PDB ID]=1v8y [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-168 [UniProt coverage chain A]=92% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-168 [UniProt coverage chain A-2]=92% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Thermus thermophilus [Accession]=MF7000553 [Entry] [Entry number]=738 [Entry name]=ADP-ribose pyrophosphatase with ADP-ribose and Gd [PDB ID]=1v8m [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-169 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-169 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Thermus thermophilus [Accession]=MF7000554 [Entry] [Entry number]=739 [Entry name]=ADP-ribose pyrophosphatase with ADP-ribose [PDB ID]=1v8l [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-169 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-169 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Thermus thermophilus [Accession]=MF7000555 [Entry] [Entry number]=740 [Entry name]=ADP-ribose pyrophosphatase (E82Q mutant) with SO4 and Mg [PDB ID]=1v8u [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-169 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-169 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Thermus thermophilus [Accession]=MF7000556 [Entry] [Entry number]=741 [Entry name]=ADP-ribose pyrophosphatase with AMP and Mg [PDB ID]=1v8s [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-169 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-169 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Thermus thermophilus [Accession]=MF7000557 [Entry] [Entry number]=742 [Entry name]=ADP-ribose pyrophosphatase (E86Q mutant) with ADP-ribose and Mg [PDB ID]=1v8v [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-169 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-169 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.97 [Source organism]=Thermus thermophilus [Accession]=MF7000558 [Entry] [Entry number]=743 [Entry name]=ADP-ribose pyrophosphatase of (E82Q mutant) with SO4 and Zn [PDB ID]=1v8w [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q84CU3 [UniProt boundaries chain A]=11-168 [UniProt coverage chain A]=92% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q84CU3 [UniProt boundaries chain A-2]=11-168 [UniProt coverage chain A-2]=92% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.66 [Source organism]=Thermus thermophilus [Accession]=MF7000559 [Entry] [Entry number]=744 [Entry name]=ADP compounds hydrolase [PDB ID]=1vhz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=P45799 [UniProt boundaries chain A]=2-185 [UniProt coverage chain A]=98% [Name chain A]=ADP compounds hydrolase NudE [UniProt sequence chain A]=MSKSLQKPTILNVETVARSRLFTVESVDLEFSNGVRRVYERMRPTNREAVMIVPIVDDHLILIREYAVGTESYELGFSKGLIDPGESVYEAANRELKEEVGFGANDLTFLKKLSMAPSYFSSKMNIVVAQDLYPESLEGDEPEPLPQVRWPLAHMMDLLEDPDFNEARNVSALFLVREWLKGQGRV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P45799 [UniProt boundaries chain B]=2-186 [UniProt coverage chain B]=99% [Name chain B]=ADP compounds hydrolase NudE [UniProt sequence chain B]=MSKSLQKPTILNVETVARSRLFTVESVDLEFSNGVRRVYERMRPTNREAVMIVPIVDDHLILIREYAVGTESYELGFSKGLIDPGESVYEAANRELKEEVGFGANDLTFLKKLSMAPSYFSSKMNIVVAQDLYPESLEGDEPEPLPQVRWPLAHMMDLLEDPDFNEARNVSALFLVREWLKGQGRV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.32 [Source organism]=Escherichia coli [Accession]=MF7000560 [Entry] [Entry number]=745 [Entry name]=ADP compounds hydrolase [PDB ID]=1vhg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=P45799 [UniProt boundaries chain A]=2-186 [UniProt coverage chain A]=99% [Name chain A]=ADP compounds hydrolase NudE [UniProt sequence chain A]=MSKSLQKPTILNVETVARSRLFTVESVDLEFSNGVRRVYERMRPTNREAVMIVPIVDDHLILIREYAVGTESYELGFSKGLIDPGESVYEAANRELKEEVGFGANDLTFLKKLSMAPSYFSSKMNIVVAQDLYPESLEGDEPEPLPQVRWPLAHMMDLLEDPDFNEARNVSALFLVREWLKGQGRV [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P45799 [UniProt boundaries chain B]=2-186 [UniProt coverage chain B]=99% [Name chain B]=ADP compounds hydrolase NudE [UniProt sequence chain B]=MSKSLQKPTILNVETVARSRLFTVESVDLEFSNGVRRVYERMRPTNREAVMIVPIVDDHLILIREYAVGTESYELGFSKGLIDPGESVYEAANRELKEEVGFGANDLTFLKKLSMAPSYFSSKMNIVVAQDLYPESLEGDEPEPLPQVRWPLAHMMDLLEDPDFNEARNVSALFLVREWLKGQGRV [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Escherichia coli [Accession]=MF7000561 [Entry] [Entry number]=746 [Entry name]=NDX2 with MG2+ and AMP (Thermus thermophilus HB8) [PDB ID]=2yvo [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SJY9 [UniProt boundaries chain A]=1-182 [UniProt coverage chain A]=100% [Name chain A]=MutT/nudix family protein [UniProt sequence chain A]=MSPWERILLEEILSEPVRLVKERVRTHTGRELTYVYRPGPVAASFVLPVTERGTALLVRQYRHPTGKFLLEVPAGKVDEGETPEAAARRELREEVGAEAETLIPLPSFHPQPSFTAVVFHPFLALKARVVTPPTLEEGELLESLELPLTEVYALLAKGEIQDASTALTLFYAEPHLKRLGLL [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SJY9 [UniProt boundaries chain A-2]=1-182 [UniProt coverage chain A-2]=100% [Name chain A-2]=MutT/nudix family protein [UniProt sequence chain A-2]=MSPWERILLEEILSEPVRLVKERVRTHTGRELTYVYRPGPVAASFVLPVTERGTALLVRQYRHPTGKFLLEVPAGKVDEGETPEAAARRELREEVGAEAETLIPLPSFHPQPSFTAVVFHPFLALKARVVTPPTLEEGELLESLELPLTEVYALLAKGEIQDASTALTLFYAEPHLKRLGLL [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.67 [Source organism]=Thermus thermophilus [Accession]=MF7000562 [Entry] [Entry number]=747 [Entry name]=NDX2 with MG2+ and ampcpr (Thermus thermophilus HB8) [PDB ID]=2yvp [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SJY9 [UniProt boundaries chain A]=1-182 [UniProt coverage chain A]=100% [Name chain A]=MutT/nudix family protein [UniProt sequence chain A]=MSPWERILLEEILSEPVRLVKERVRTHTGRELTYVYRPGPVAASFVLPVTERGTALLVRQYRHPTGKFLLEVPAGKVDEGETPEAAARRELREEVGAEAETLIPLPSFHPQPSFTAVVFHPFLALKARVVTPPTLEEGELLESLELPLTEVYALLAKGEIQDASTALTLFYAEPHLKRLGLL [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SJY9 [UniProt boundaries chain A-2]=1-182 [UniProt coverage chain A-2]=100% [Name chain A-2]=MutT/nudix family protein [UniProt sequence chain A-2]=MSPWERILLEEILSEPVRLVKERVRTHTGRELTYVYRPGPVAASFVLPVTERGTALLVRQYRHPTGKFLLEVPAGKVDEGETPEAAARRELREEVGAEAETLIPLPSFHPQPSFTAVVFHPFLALKARVVTPPTLEEGELLESLELPLTEVYALLAKGEIQDASTALTLFYAEPHLKRLGLL [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.66 [Source organism]=Thermus thermophilus [Accession]=MF7000563 [Entry] [Entry number]=748 [Entry name]=E100A GDP-mannose hydrolase (yffh) with Mg (Escherichia coli) [PDB ID]=3o69 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=P37128 [UniProt boundaries chain A]=2-191 [UniProt coverage chain A]=99% [Name chain A]=GDP-mannose pyrophosphatase [UniProt sequence chain A]=MTQQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATILLYNTKKKTVVLIRQFRVATWVNGNESGQLIESCAGLLDNDEPEVCIRKEAIEETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDNQRANAGGGVEDEDIEVLELPFSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P37128 [UniProt boundaries chain B]=3-191 [UniProt coverage chain B]=98% [Name chain B]=GDP-mannose pyrophosphatase [UniProt sequence chain B]=MTQQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATILLYNTKKKTVVLIRQFRVATWVNGNESGQLIESCAGLLDNDEPEVCIRKEAIEETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDNQRANAGGGVEDEDIEVLELPFSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Escherichia coli [Accession]=MF7000564 [Entry] [Entry number]=749 [Entry name]=D152A GDP-mannose hydrolase (yffh) with Mg (Escherichia coli) [PDB ID]=3o6z [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=P37128 [UniProt boundaries chain A]=2-191 [UniProt coverage chain A]=99% [Name chain A]=GDP-mannose pyrophosphatase [UniProt sequence chain A]=MTQQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATILLYNTKKKTVVLIRQFRVATWVNGNESGQLIESCAGLLDNDEPEVCIRKEAIEETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDNQRANAGGGVEDEDIEVLELPFSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P37128 [UniProt boundaries chain B]=3-191 [UniProt coverage chain B]=98% [Name chain B]=GDP-mannose pyrophosphatase [UniProt sequence chain B]=MTQQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATILLYNTKKKTVVLIRQFRVATWVNGNESGQLIESCAGLLDNDEPEVCIRKEAIEETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDNQRANAGGGVEDEDIEVLELPFSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Escherichia coli [Accession]=MF7000565 [Entry] [Entry number]=750 [Entry name]=Nucleoside diphosphate sugar hydrolase (Bdellovibrio bacteriovorus) [PDB ID]=5c8l [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q6MIH8 [UniProt boundaries chain A]=1-182 [UniProt coverage chain A]=100% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MKHLEEKTLSTRQIFKGRYLKIEQDQVQAPDGRTYTREYILHPGAAMMIPLLPNGNVVMIHQYRHAVKKVFLEFPAGKRDHNEETLLTAKRELLEETGYEAKDWKFLTTIHPVIGYSNEHIDLYLARDLTHLEQRLDQGEFIEVVEVKPADLMQLVLEGKVSDVKTQIGAFWLDKFLRGEWN [Source organism chain A]=HD100) [UniProt ID chain B]=Q6MIH8 [UniProt boundaries chain B]=3-181 [UniProt coverage chain B]=98% [Name chain B]=ADP-ribose pyrophosphatase [UniProt sequence chain B]=MKHLEEKTLSTRQIFKGRYLKIEQDQVQAPDGRTYTREYILHPGAAMMIPLLPNGNVVMIHQYRHAVKKVFLEFPAGKRDHNEETLLTAKRELLEETGYEAKDWKFLTTIHPVIGYSNEHIDLYLARDLTHLEQRLDQGEFIEVVEVKPADLMQLVLEGKVSDVKTQIGAFWLDKFLRGEWN [Source organism chain B]=HD100) [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=HD100) [Accession]=MF7000566 [Entry] [Entry number]=751 [Entry name]=Nucleoside diphosphate sugar hydrolase (Bdellovibrio bacteriovorus) [PDB ID]=5c7q [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q6MIH8 [UniProt boundaries chain A]=1-182 [UniProt coverage chain A]=100% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MKHLEEKTLSTRQIFKGRYLKIEQDQVQAPDGRTYTREYILHPGAAMMIPLLPNGNVVMIHQYRHAVKKVFLEFPAGKRDHNEETLLTAKRELLEETGYEAKDWKFLTTIHPVIGYSNEHIDLYLARDLTHLEQRLDQGEFIEVVEVKPADLMQLVLEGKVSDVKTQIGAFWLDKFLRGEWN [Source organism chain A]=HD100) [UniProt ID chain B]=Q6MIH8 [UniProt boundaries chain B]=3-182 [UniProt coverage chain B]=98% [Name chain B]=ADP-ribose pyrophosphatase [UniProt sequence chain B]=MKHLEEKTLSTRQIFKGRYLKIEQDQVQAPDGRTYTREYILHPGAAMMIPLLPNGNVVMIHQYRHAVKKVFLEFPAGKRDHNEETLLTAKRELLEETGYEAKDWKFLTTIHPVIGYSNEHIDLYLARDLTHLEQRLDQGEFIEVVEVKPADLMQLVLEGKVSDVKTQIGAFWLDKFLRGEWN [Source organism chain B]=HD100) [ExpTech]=X-ray [Resolution]=1.52 [Source organism]=HD100) [Accession]=MF7000567 [Entry] [Entry number]=752 [Entry name]=Nucleoside Diphosphate Sugar Hydrolase with ADP-ribose (Bdellovibrio bacteriovorus) [PDB ID]=5c7t [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q6MIH8 [UniProt boundaries chain A]=1-182 [UniProt coverage chain A]=100% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MKHLEEKTLSTRQIFKGRYLKIEQDQVQAPDGRTYTREYILHPGAAMMIPLLPNGNVVMIHQYRHAVKKVFLEFPAGKRDHNEETLLTAKRELLEETGYEAKDWKFLTTIHPVIGYSNEHIDLYLARDLTHLEQRLDQGEFIEVVEVKPADLMQLVLEGKVSDVKTQIGAFWLDKFLRGEWN [Source organism chain A]=HD100) [UniProt ID chain B]=Q6MIH8 [UniProt boundaries chain B]=3-181 [UniProt coverage chain B]=98% [Name chain B]=ADP-ribose pyrophosphatase [UniProt sequence chain B]=MKHLEEKTLSTRQIFKGRYLKIEQDQVQAPDGRTYTREYILHPGAAMMIPLLPNGNVVMIHQYRHAVKKVFLEFPAGKRDHNEETLLTAKRELLEETGYEAKDWKFLTTIHPVIGYSNEHIDLYLARDLTHLEQRLDQGEFIEVVEVKPADLMQLVLEGKVSDVKTQIGAFWLDKFLRGEWN [Source organism chain B]=HD100) [ExpTech]=X-ray [Resolution]=2.06 [Source organism]=HD100) [Accession]=MF7000568 [Entry] [Entry number]=753 [Entry name]=ADP ribose pyrophosphatase (Thermus thermophilus HB8) [PDB ID]=3x0m [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-168 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-168 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.15 [Source organism]=Thermus thermophilus [Accession]=MF7000569 [Entry] [Entry number]=754 [Entry name]=ADP ribose pyrophosphatase (Thermus thermophilus HB8) [PDB ID]=3x0r [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-168 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-168 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.15 [Source organism]=Thermus thermophilus [Accession]=MF7000570 [Entry] [Entry number]=755 [Entry name]=ADP ribose pyrophosphatase (Thermus thermophilus HB8) [PDB ID]=3x0s [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-169 [UniProt coverage chain A]=94% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-169 [UniProt coverage chain A-2]=94% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.10 [Source organism]=Thermus thermophilus [Accession]=MF7000571 [Entry] [Entry number]=756 [Entry name]=ADP ribose pyrophosphatase (Thermus thermophilus HB8) [PDB ID]=3x0k [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-168 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-168 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=0.97 [Source organism]=Thermus thermophilus [Accession]=MF7000572 [Entry] [Entry number]=757 [Entry name]=ADP ribose pyrophosphatase (Thermus thermophilus HB8) [PDB ID]=3x0p [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-168 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-168 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.22 [Source organism]=Thermus thermophilus [Accession]=MF7000573 [Entry] [Entry number]=758 [Entry name]=ADP ribose pyrophosphatase in apo state (Thermus thermophilus HB8) [PDB ID]=3x0i [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-168 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-168 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=0.91 [Source organism]=Thermus thermophilus [Accession]=MF7000574 [Entry] [Entry number]=759 [Entry name]=ADP ribose pyrophosphatase in apo state (Thermus thermophilus HB8) [PDB ID]=3x0j [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-168 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-168 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=0.92 [Source organism]=Thermus thermophilus [Accession]=MF7000575 [Entry] [Entry number]=760 [Entry name]=ADP ribose pyrophosphatase (Thermus thermophilus HB8) [PDB ID]=3x0l [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=9-168 [UniProt coverage chain A]=94% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=9-168 [UniProt coverage chain A-2]=94% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.00 [Source organism]=Thermus thermophilus [Accession]=MF7000576 [Entry] [Entry number]=761 [Entry name]=ADP ribose pyrophosphatase (Thermus thermophilus HB8) [PDB ID]=3x0o [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-168 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-168 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.09 [Source organism]=Thermus thermophilus [Accession]=MF7000577 [Entry] [Entry number]=762 [Entry name]=ADP ribose pyrophosphatase (Thermus thermophilus HB8) [PDB ID]=3x0n [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-168 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-168 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.12 [Source organism]=Thermus thermophilus [Accession]=MF7000578 [Entry] [Entry number]=763 [Entry name]=ADP ribose pyrophosphatase (Thermus thermophilus HB8) [PDB ID]=3x0q [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=NUDIX domain [Evidence level]=Indirect evidence [Evidence text]=The authors claim that ADP-ribose pyrophosphatase forms a symmetric homodimer, wherein the two catalytic sites are formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity (PMID:11323725). E. coli ADPRase elutes as a dimer in gel exclusion chromatography (PMID:11323725). The N-terminal subdomain (residues 1-54) mediates dimerization and is a strong candidate for MSF, while the C-terminal one is a folded Nudix domain. Other structures belonging to the same domain type also show features implying MSF: large relative interface, domain swapping and a lack of the monomeric form in gel filtration experiments (PMID:12906832, PMID:15210687). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000056,MF7000057,MF7000058,MF7000059,MF7000546,MF7000547,MF7000548,MF7000549,MF7000550,MF7000551,MF7000552,MF7000553,MF7000554,MF7000555,MF7000556,MF7000557,MF7000558,MF7000559,MF7000560,MF7000561,MF7000562,MF7000563,MF7000564,MF7000565,MF7000566,MF7000567,MF7000568,MF7000569,MF7000570,MF7000571,MF7000572,MF7000573,MF7000574,MF7000575,MF7000576,MF7000577,MF7000578,MF7000579 [UniProt ID chain A]=Q5SKW5 [UniProt boundaries chain A]=10-168 [UniProt coverage chain A]=93% [Name chain A]=ADP-ribose pyrophosphatase [UniProt sequence chain A]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SKW5 [UniProt boundaries chain A-2]=10-168 [UniProt coverage chain A-2]=93% [Name chain A-2]=ADP-ribose pyrophosphatase [UniProt sequence chain A-2]=MGRVYYGGVERTYLYRGRILNLALEGRYEIVEHKPAVAVIALREGRMLFVRQMRPAVGLAPLEIPAGLIEPGEDPLEAARRELAEETGLSGDLTYLFSYFVSPGFTDEKTHVFLAENLKEVEAHPDEDEAIEVVWMRPEEALERHQRGEVEFSATGLVGVLYYHAFLRGR [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.14 [Source organism]=Thermus thermophilus [Accession]=MF7000579 [Entry] [Entry number]=764 [Entry name]=Calcyclin [PDB ID]=1cnp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P30801 [UniProt boundaries chain A]=1-90 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A6 [UniProt sequence chain A]=MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG [Source organism chain A]=Oryctolagus cuniculus [UniProt ID chain B]=P30801 [UniProt boundaries chain B]=1-90 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A6 [UniProt sequence chain B]=MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG [Source organism chain B]=Oryctolagus cuniculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Oryctolagus cuniculus [Accession]=MF7000580 [Entry] [Entry number]=765 [Entry name]=Ca2+-bound Calcyclin [PDB ID]=1a03 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P30801 [UniProt boundaries chain A]=1-90 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A6 [UniProt sequence chain A]=MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG [Source organism chain A]=Oryctolagus cuniculus [UniProt ID chain B]=P30801 [UniProt boundaries chain B]=1-90 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A6 [UniProt sequence chain B]=MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG [Source organism chain B]=Oryctolagus cuniculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Oryctolagus cuniculus [Accession]=MF7000581 [Entry] [Entry number]=766 [Entry name]=Rabbit calcyclin (apo form) [PDB ID]=2cnp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P30801 [UniProt boundaries chain A]=1-90 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A6 [UniProt sequence chain A]=MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG [Source organism chain A]=Oryctolagus cuniculus [UniProt ID chain B]=P30801 [UniProt boundaries chain B]=1-90 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A6 [UniProt sequence chain B]=MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG [Source organism chain B]=Oryctolagus cuniculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Oryctolagus cuniculus [Accession]=MF7000582 [Entry] [Entry number]=767 [Entry name]=Human migration inhibitory factor-related protein 8 [PDB ID]=1mr8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P05109 [UniProt boundaries chain A]=1-90 [UniProt coverage chain A]=96% [Name chain A]=Protein S100-A8 [UniProt sequence chain A]=MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P05109 [UniProt boundaries chain B]=1-90 [UniProt coverage chain B]=96% [Name chain B]=Protein S100-A8 [UniProt sequence chain B]=MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Homo sapiens [Accession]=MF7000583 [Entry] [Entry number]=768 [Entry name]=S100A1 (apo form) [PDB ID]=1k2h [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P35467 [UniProt boundaries chain A]=2-94 [UniProt coverage chain A]=98% [Name chain A]=Protein S100-A1 [UniProt sequence chain A]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKDLLQTELSSFLDVQKDADAVDKIMKELDENGDGEVDFQEFVVLVAALTVACNNFFWENS [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P35467 [UniProt boundaries chain B]=2-94 [UniProt coverage chain B]=98% [Name chain B]=Protein S100-A1 [UniProt sequence chain B]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKDLLQTELSSFLDVQKDADAVDKIMKELDENGDGEVDFQEFVVLVAALTVACNNFFWENS [Source organism chain B]=Rattus norvegicus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Rattus norvegicus [Accession]=MF7000584 [Entry] [Entry number]=769 [Entry name]=Ca2+-bound Calcyclin [PDB ID]=1jwd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P30801 [UniProt boundaries chain A]=1-90 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A6 [UniProt sequence chain A]=MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG [Source organism chain A]=Oryctolagus cuniculus [UniProt ID chain B]=P30801 [UniProt boundaries chain B]=1-90 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A6 [UniProt sequence chain B]=MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG [Source organism chain B]=Oryctolagus cuniculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Oryctolagus cuniculus [Accession]=MF7000585 [Entry] [Entry number]=770 [Entry name]=S100A3 (apo form) [PDB ID]=1kso [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P33764 [UniProt boundaries chain A]=2-94 [UniProt coverage chain A]=92% [Name chain A]=Protein S100-A3 [UniProt sequence chain A]=MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P33764 [UniProt boundaries chain B]=2-94 [UniProt coverage chain B]=92% [Name chain B]=Protein S100-A3 [UniProt sequence chain B]=MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Homo sapiens [Accession]=MF7000586 [Entry] [Entry number]=771 [Entry name]=Rabbit S100A11 (apo form) [PDB ID]=1nsh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P24480 [UniProt boundaries chain A]=2-102 [UniProt coverage chain A]=99% [Name chain A]=Protein S100-A11 [UniProt sequence chain A]=MSRPTETERCIESLIAVFQKYAGKDGHSVTLSKTEFLSFMNTELAAFTKNQKDPGVLDRMMKKLDLNSDGQLDFQEFLNLIGGLAVACHESFVKAAPPQKRF [Source organism chain A]=Oryctolagus cuniculus [UniProt ID chain B]=P24480 [UniProt boundaries chain B]=2-102 [UniProt coverage chain B]=99% [Name chain B]=Protein S100-A11 [UniProt sequence chain B]=MSRPTETERCIESLIAVFQKYAGKDGHSVTLSKTEFLSFMNTELAAFTKNQKDPGVLDRMMKKLDLNSDGQLDFQEFLNLIGGLAVACHESFVKAAPPQKRF [Source organism chain B]=Oryctolagus cuniculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Oryctolagus cuniculus [Accession]=MF7000587 [Entry] [Entry number]=772 [Entry name]=S100A13 with Ca [PDB ID]=1yut [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q99584 [UniProt boundaries chain A]=1-98 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A13 [UniProt sequence chain A]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q99584 [UniProt boundaries chain B]=1-98 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A13 [UniProt sequence chain B]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000588 [Entry] [Entry number]=773 [Entry name]=S100A13 (apo form) [PDB ID]=1yus [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q99584 [UniProt boundaries chain A]=1-98 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A13 [UniProt sequence chain A]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q99584 [UniProt boundaries chain B]=1-98 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A13 [UniProt sequence chain B]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000589 [Entry] [Entry number]=774 [Entry name]=S100A13 (apo form) [PDB ID]=1yur [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q99584 [UniProt boundaries chain A]=1-98 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A13 [UniProt sequence chain A]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q99584 [UniProt boundaries chain B]=1-98 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A13 [UniProt sequence chain B]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000590 [Entry] [Entry number]=775 [Entry name]=S100A1 with Ca [PDB ID]=1zfs [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P35467 [UniProt boundaries chain A]=2-94 [UniProt coverage chain A]=98% [Name chain A]=Protein S100-A1 [UniProt sequence chain A]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKDLLQTELSSFLDVQKDADAVDKIMKELDENGDGEVDFQEFVVLVAALTVACNNFFWENS [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P35467 [UniProt boundaries chain B]=2-94 [UniProt coverage chain B]=98% [Name chain B]=Protein S100-A1 [UniProt sequence chain B]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKDLLQTELSSFLDVQKDADAVDKIMKELDENGDGEVDFQEFVVLVAALTVACNNFFWENS [Source organism chain B]=Rattus norvegicus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Rattus norvegicus [Accession]=MF7000591 [Entry] [Entry number]=776 [Entry name]=Human S100A13 [PDB ID]=2h2k [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q99584 [UniProt boundaries chain A]=1-91 [UniProt coverage chain A]=92% [Name chain A]=Protein S100-A13 [UniProt sequence chain A]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q99584 [UniProt boundaries chain B]=3-95 [UniProt coverage chain B]=94% [Name chain B]=Protein S100-A13 [UniProt sequence chain B]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000592 [Entry] [Entry number]=777 [Entry name]=S100A1 (apo form) with disulfide between CYS85 residue and b-mercaptoethanol [PDB ID]=2jpt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P02639 [UniProt boundaries chain A]=2-94 [UniProt coverage chain A]=98% [Name chain A]=Protein S100-A1 [UniProt sequence chain A]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDADAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain A]=Bos taurus [UniProt ID chain B]=P02639 [UniProt boundaries chain B]=2-94 [UniProt coverage chain B]=98% [Name chain B]=Protein S100-A1 [UniProt sequence chain B]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDADAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain B]=Bos taurus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bos taurus [Accession]=MF7000593 [Entry] [Entry number]=778 [Entry name]=Human S100A13 with Ca [PDB ID]=2egd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q99584 [UniProt boundaries chain A]=5-90 [UniProt coverage chain A]=87% [Name chain A]=Protein S100-A13 [UniProt sequence chain A]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q99584 [UniProt boundaries chain B]=6-96 [UniProt coverage chain B]=92% [Name chain B]=Protein S100-A13 [UniProt sequence chain B]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF7000594 [Entry] [Entry number]=779 [Entry name]=S100A4 with Ca [PDB ID]=2q91 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P26447 [UniProt boundaries chain A]=2-97 [UniProt coverage chain A]=95% [Name chain A]=Protein S100-A4 [UniProt sequence chain A]=MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P26447 [UniProt boundaries chain B]=2-97 [UniProt coverage chain B]=95% [Name chain B]=Protein S100-A4 [UniProt sequence chain B]=MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.63 [Source organism]=Homo sapiens [Accession]=MF7000595 [Entry] [Entry number]=780 [Entry name]=S100A4 with Ca [PDB ID]=3cga [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P26447 [UniProt boundaries chain A]=4-90 [UniProt coverage chain A]=86% [Name chain A]=Protein S100-A4 [UniProt sequence chain A]=MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P26447 [UniProt boundaries chain B]=4-90 [UniProt coverage chain B]=86% [Name chain B]=Protein S100-A4 [UniProt sequence chain B]=MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.03 [Source organism]=Homo sapiens [Accession]=MF7000596 [Entry] [Entry number]=781 [Entry name]=S100A5 with Ca2+ [PDB ID]=2kax [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P33763 [UniProt boundaries chain A]=1-92 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A5 [UniProt sequence chain A]=METPLEKALTTMVTTFHKYSGREGSKLTLSRKELKELIKKELCLGEMKESSIDDLMKSLDKNSDQEIDFKEYSVFLTMLCMAYNDFFLEDNK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P33763 [UniProt boundaries chain B]=1-92 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A5 [UniProt sequence chain B]=METPLEKALTTMVTTFHKYSGREGSKLTLSRKELKELIKKELCLGEMKESSIDDLMKSLDKNSDQEIDFKEYSVFLTMLCMAYNDFFLEDNK [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000597 [Entry] [Entry number]=782 [Entry name]=S100A5 withCa2+ [PDB ID]=2kay [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P33763 [UniProt boundaries chain A]=1-92 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A5 [UniProt sequence chain A]=METPLEKALTTMVTTFHKYSGREGSKLTLSRKELKELIKKELCLGEMKESSIDDLMKSLDKNSDQEIDFKEYSVFLTMLCMAYNDFFLEDNK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P33763 [UniProt boundaries chain B]=1-92 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A5 [UniProt sequence chain B]=METPLEKALTTMVTTFHKYSGREGSKLTLSRKELKELIKKELCLGEMKESSIDDLMKSLDKNSDQEIDFKEYSVFLTMLCMAYNDFFLEDNK [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000598 [Entry] [Entry number]=783 [Entry name]=S100A13 with a drug amlexanox [PDB ID]=2kot [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q99584 [UniProt boundaries chain A]=1-98 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A13 [UniProt sequence chain A]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q99584 [UniProt boundaries chain B]=1-98 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A13 [UniProt sequence chain B]=MAAEPLTELEESIETVVTTFFTFARQEGRKDSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLIGELAKEIRKKKDLKIRKK [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000599 [Entry] [Entry number]=784 [Entry name]=S100B with Ca and Zn [PDB ID]=3d0y [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P04271 [UniProt boundaries chain A]=1-90 [UniProt coverage chain A]=97% [Name chain A]=Protein S100-B [UniProt sequence chain A]=MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P04271 [UniProt boundaries chain B]=1-90 [UniProt coverage chain B]=97% [Name chain B]=Protein S100-B [UniProt sequence chain B]=MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Homo sapiens [Accession]=MF7000600 [Entry] [Entry number]=785 [Entry name]=Human S100A1 (apo form) [PDB ID]=2l0p [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P23297 [UniProt boundaries chain A]=2-94 [UniProt coverage chain A]=98% [Name chain A]=Protein S100-A1 [UniProt sequence chain A]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P23297 [UniProt boundaries chain B]=2-94 [UniProt coverage chain B]=98% [Name chain B]=Protein S100-A1 [UniProt sequence chain B]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000601 [Entry] [Entry number]=786 [Entry name]=Post-refolded S100A3 [PDB ID]=3nsi [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P33764 [UniProt boundaries chain A]=4-99 [UniProt coverage chain A]=95% [Name chain A]=Protein S100-A3 [UniProt sequence chain A]=MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P33764 [UniProt boundaries chain B]=3-99 [UniProt coverage chain B]=96% [Name chain B]=Protein S100-A3 [UniProt sequence chain B]=MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.15 [Source organism]=Homo sapiens [Accession]=MF7000602 [Entry] [Entry number]=787 [Entry name]=Post-refolded S100A3 (R51A mutant) [PDB ID]=3nsk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P33764 [UniProt boundaries chain A]=3-99 [UniProt coverage chain A]=96% [Name chain A]=Protein S100-A3 [UniProt sequence chain A]=MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P33764 [UniProt boundaries chain B]=3-99 [UniProt coverage chain B]=96% [Name chain B]=Protein S100-A3 [UniProt sequence chain B]=MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.55 [Source organism]=Homo sapiens [Accession]=MF7000603 [Entry] [Entry number]=788 [Entry name]=S100A3 [PDB ID]=3nso [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P33764 [UniProt boundaries chain A]=2-99 [UniProt coverage chain A]=97% [Name chain A]=Protein S100-A3 [UniProt sequence chain A]=MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P33764 [UniProt boundaries chain B]=3-99 [UniProt coverage chain B]=96% [Name chain B]=Protein S100-A3 [UniProt sequence chain B]=MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.45 [Source organism]=Homo sapiens [Accession]=MF7000604 [Entry] [Entry number]=789 [Entry name]=Ca2+-loaded S100A2 with Ca [PDB ID]=4duq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P29034 [UniProt boundaries chain A]=3-90 [UniProt coverage chain A]=89% [Name chain A]=Protein S100-A2 [UniProt sequence chain A]=MMCSSLEQALAVLVTTFHKYSCQEGDKFKLSKGEMKELLHKELPSFVGEKVDEEGLKKLMGSLDENSDQQVDFQEYAVFLALITVMCNDFFQGCPDRP [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P29034 [UniProt boundaries chain B]=3-92 [UniProt coverage chain B]=91% [Name chain B]=Protein S100-A2 [UniProt sequence chain B]=MMCSSLEQALAVLVTTFHKYSCQEGDKFKLSKGEMKELLHKELPSFVGEKVDEEGLKKLMGSLDENSDQQVDFQEYAVFLALITVMCNDFFQGCPDRP [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.30 [Source organism]=Homo sapiens [Accession]=MF7000605 [Entry] [Entry number]=790 [Entry name]=Human S100A1 with post-translational S-nitrosylation [PDB ID]=2llt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P23297 [UniProt boundaries chain A]=2-94 [UniProt coverage chain A]=98% [Name chain A]=Protein S100-A1 [UniProt sequence chain A]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P23297 [UniProt boundaries chain B]=2-94 [UniProt coverage chain B]=98% [Name chain B]=Protein S100-A1 [UniProt sequence chain B]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000606 [Entry] [Entry number]=791 [Entry name]=S100A1 with post-translational S-nitrosylation [PDB ID]=2llu [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P23297 [UniProt boundaries chain A]=2-94 [UniProt coverage chain A]=98% [Name chain A]=Protein S100-A1 [UniProt sequence chain A]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P23297 [UniProt boundaries chain B]=2-94 [UniProt coverage chain B]=98% [Name chain B]=Protein S100-A1 [UniProt sequence chain B]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000607 [Entry] [Entry number]=792 [Entry name]=Human S100A14 [PDB ID]=2m0r [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q9HCY8 [UniProt boundaries chain A]=1-104 [UniProt coverage chain A]=100% [Name chain A]=Protein S100-A14 [UniProt sequence chain A]=MGQCRSANAEDAQEFSDVERAIETLIKNFHQYSVEGGKETLTPSELRDLVTQQLPHLMPSNCGLEEKIANLGSCNDSKLEFRSFWELIGEAAKSVKLERPVRGH [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9HCY8 [UniProt boundaries chain B]=1-104 [UniProt coverage chain B]=100% [Name chain B]=Protein S100-A14 [UniProt sequence chain B]=MGQCRSANAEDAQEFSDVERAIETLIKNFHQYSVEGGKETLTPSELRDLVTQQLPHLMPSNCGLEEKIANLGSCNDSKLEFRSFWELIGEAAKSVKLERPVRGH [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000608 [Entry] [Entry number]=793 [Entry name]=Human S100A1 protein (mutant) [PDB ID]=2lp2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P23297 [UniProt boundaries chain A]=2-94 [UniProt coverage chain A]=98% [Name chain A]=Protein S100-A1 [UniProt sequence chain A]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P23297 [UniProt boundaries chain B]=2-94 [UniProt coverage chain B]=98% [Name chain B]=Protein S100-A1 [UniProt sequence chain B]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000609 [Entry] [Entry number]=794 [Entry name]=S100A1 with Ca2+ [PDB ID]=2lp3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P23297 [UniProt boundaries chain A]=2-94 [UniProt coverage chain A]=98% [Name chain A]=Protein S100-A1 [UniProt sequence chain A]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P23297 [UniProt boundaries chain B]=2-94 [UniProt coverage chain B]=98% [Name chain B]=Protein S100-A1 [UniProt sequence chain B]=MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000610 [Entry] [Entry number]=795 [Entry name]=WT murine S100A9 with Ca and Zn [PDB ID]=6zdy [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P31725 [UniProt boundaries chain A]=5-112 [UniProt coverage chain A]=95% [Name chain A]=Protein S100-A9 [UniProt sequence chain A]=MANKAPSQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKRNEALINDIMEDLDTNQDNQLSFEECMMLMAKLIFACHEKLHENNPRGHGHSHGKGCGK [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=P31725 [UniProt boundaries chain A-2]=5-112 [UniProt coverage chain A-2]=95% [Name chain A-2]=Protein S100-A9 [UniProt sequence chain A-2]=MANKAPSQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKRNEALINDIMEDLDTNQDNQLSFEECMMLMAKLIFACHEKLHENNPRGHGHSHGKGCGK [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=1.45 [Source organism]=Mus musculus [Accession]=MF7000611 [Entry] [Entry number]=796 [Entry name]=Murine S100A9 (C80A mutant) with Ca and Zn [PDB ID]=6zfe [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=P31725 [UniProt boundaries chain A]=5-112 [UniProt coverage chain A]=95% [Name chain A]=Protein S100-A9 [UniProt sequence chain A]=MANKAPSQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKRNEALINDIMEDLDTNQDNQLSFEECMMLMAKLIFACHEKLHENNPRGHGHSHGKGCGK [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=P31725 [UniProt boundaries chain A-2]=5-112 [UniProt coverage chain A-2]=95% [Name chain A-2]=Protein S100-A9 [UniProt sequence chain A-2]=MANKAPSQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKRNEALINDIMEDLDTNQDNQLSFEECMMLMAKLIFACHEKLHENNPRGHGHSHGKGCGK [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Mus musculus [Accession]=MF7000612 [Entry] [Entry number]=797 [Entry name]=Murine S100A7/S100A15 [PDB ID]=8s9w [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=S100-type EF-hand dimers [Sequence domain]=S-100/ICaBP type EF hand dimer [Evidence level]=Direct evidence [Evidence text]=GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000580,MF2100013,MF7000581,MF7000582,MF7000583,MF7000584,MF7000585,MF7000586,MF7000587,MF7000588,MF7000589,MF7000590,MF7000591,MF7000592,MF7000593,MF7000594,MF7000595,MF7000596,MF7000597,MF7000598,MF7000599,MF7000600,MF7000186,MF7000187,MF7000601,MF7000602,MF7000603,MF7000604,MF7000605,MF7000606,MF7000607,MF7000608,MF7000609,MF7000610,MF7000611,MF7000612,MF7000613 [UniProt ID chain A]=Q6S5I3 [UniProt boundaries chain A]=2-99 [UniProt coverage chain A]=90% [Name chain A]=Protein S100-A15A [UniProt sequence chain A]=MPDTPVEDSLFQIIHCFHHYAAREGDKETLSLEELKALLLDSVPRFMDTLGRRQPYYITELFRAADKNKDNQICFDEFLYILGKLVKDYHLQFHRQLCAHYCTEHSLY [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q6S5I3 [UniProt boundaries chain B]=2-95 [UniProt coverage chain B]=87% [Name chain B]=Protein S100-A15A [UniProt sequence chain B]=MPDTPVEDSLFQIIHCFHHYAAREGDKETLSLEELKALLLDSVPRFMDTLGRRQPYYITELFRAADKNKDNQICFDEFLYILGKLVKDYHLQFHRQLCAHYCTEHSLY [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.69 [Source organism]=Mus musculus [Accession]=MF7000613 [Entry] [Entry number]=798 [Entry name]=MarR family protein. OhrRC15S (apo form) [PDB ID]=1z91 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=O34777 [UniProt boundaries chain A]=8-144 [UniProt coverage chain A]=93% [Name chain A]=Organic hydroperoxide resistance transcriptional regulator [UniProt sequence chain A]=MENKFDHMKLENQLCFLLYASSREMTKQYKPLLDKLNITYPQYLALLLLWEHETLTVKKMGEQLYLDSGTLTPMLKRMEQQGLITRKRSEEDERSVLISLTEDGALLKEKAVDIPGTILGLSKQSGEDLKQLKSALYTLLETLHQKN [Source organism chain A]=Bacillus subtilis [UniProt ID chain A-2]=O34777 [UniProt boundaries chain A-2]=8-144 [UniProt coverage chain A-2]=93% [Name chain A-2]=Organic hydroperoxide resistance transcriptional regulator [UniProt sequence chain A-2]=MENKFDHMKLENQLCFLLYASSREMTKQYKPLLDKLNITYPQYLALLLLWEHETLTVKKMGEQLYLDSGTLTPMLKRMEQQGLITRKRSEEDERSVLISLTEDGALLKEKAVDIPGTILGLSKQSGEDLKQLKSALYTLLETLHQKN [Source organism chain A-2]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Bacillus subtilis [Accession]=MF7000614 [Entry] [Entry number]=799 [Entry name]=MexR [PDB ID]=3mex [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=P52003 [UniProt boundaries chain A]=1-142 [UniProt coverage chain A]=96% [Name chain A]=Multidrug resistance operon repressor [UniProt sequence chain A]=MNYPVNPDLMPALMAVFQHVRTRIQSELDCQRLDLTPPDVHVLKLIDEQRGLNLQDLGRQMCRDKALITRKIRELEGRNLVRRERNPSDQRSFQLFLTDEGLAIHQHAEAIMSRVHDELFAPLTPVEQATLVHLLDQCLAAQPLEDI [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=P52003 [UniProt boundaries chain B]=1-142 [UniProt coverage chain B]=96% [Name chain B]=Multidrug resistance operon repressor [UniProt sequence chain B]=MNYPVNPDLMPALMAVFQHVRTRIQSELDCQRLDLTPPDVHVLKLIDEQRGLNLQDLGRQMCRDKALITRKIRELEGRNLVRRERNPSDQRSFQLFLTDEGLAIHQHAEAIMSRVHDELFAPLTPVEQATLVHLLDQCLAAQPLEDI [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000615 [Entry] [Entry number]=800 [Entry name]=MarR Family protein, AdcR with Zn [PDB ID]=3tgn [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=Q04I02 [UniProt boundaries chain A]=1-145 [UniProt coverage chain A]=99% [Name chain A]=Transcriptional regulator AdcR [UniProt sequence chain A]=MRQLAKDINAFLNEVILQAENQHEILIGHCTSEVALTNTQEHILMLLSEESLTNSELARRLNVSQAAVTKAIKSLVKEGMLETSKDSKDARVIFYQLTDLARPIAEEHHHHHEHTLLTYEQVATQFTPNEQKVIQRFLTALVGEIK [Source organism chain A]=Streptococcus pneumoniae serotype 2 [UniProt ID chain B]=Q04I02 [UniProt boundaries chain B]=1-146 [UniProt coverage chain B]=100% [Name chain B]=Transcriptional regulator AdcR [UniProt sequence chain B]=MRQLAKDINAFLNEVILQAENQHEILIGHCTSEVALTNTQEHILMLLSEESLTNSELARRLNVSQAAVTKAIKSLVKEGMLETSKDSKDARVIFYQLTDLARPIAEEHHHHHEHTLLTYEQVATQFTPNEQKVIQRFLTALVGEIK [Source organism chain B]=Streptococcus pneumoniae serotype 2 [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Streptococcus pneumoniae serotype 2 [Accession]=MF7000616 [Entry] [Entry number]=801 [Entry name]=MarR familz protein, Sco5413 (Streptomyces coelicolor) [PDB ID]=4b8x [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=Q9L2A7 [UniProt boundaries chain A]=25-168 [UniProt coverage chain A]=85% [Name chain A]=Possible MarR-transcriptional regulator [UniProt sequence chain A]=MPKPLSLSFDPIARADELWAQRWGGVPSMAAITSIMRAQQILLGEVDAVVKPYGLTFARYEALVLLTFSKSGELPMSKIGERLMVHPTSVTNTVDRLVRSGLVAKRPNPNDGRGTLATITDKGREVVEAATRDLMAMDFGLGAYDAEECGEIFAMLRPLRVAAGDFDED [Source organism chain A]=Streptomyces coelicolor [UniProt ID chain B]=Q9L2A7 [UniProt boundaries chain B]=25-168 [UniProt coverage chain B]=85% [Name chain B]=Possible MarR-transcriptional regulator [UniProt sequence chain B]=MPKPLSLSFDPIARADELWAQRWGGVPSMAAITSIMRAQQILLGEVDAVVKPYGLTFARYEALVLLTFSKSGELPMSKIGERLMVHPTSVTNTVDRLVRSGLVAKRPNPNDGRGTLATITDKGREVVEAATRDLMAMDFGLGAYDAEECGEIFAMLRPLRVAAGDFDED [Source organism chain B]=Streptomyces coelicolor [ExpTech]=X-ray [Resolution]=1.25 [Source organism]=Streptomyces coelicolor [Accession]=MF7000617 [Entry] [Entry number]=802 [Entry name]=MexR R21W derepressor mutant (Pseudomonas aeruginosa) [PDB ID]=4zzl [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=P52003 [UniProt boundaries chain A]=5-139 [UniProt coverage chain A]=91% [Name chain A]=Multidrug resistance operon repressor [UniProt sequence chain A]=MNYPVNPDLMPALMAVFQHVRTRIQSELDCQRLDLTPPDVHVLKLIDEQRGLNLQDLGRQMCRDKALITRKIRELEGRNLVRRERNPSDQRSFQLFLTDEGLAIHQHAEAIMSRVHDELFAPLTPVEQATLVHLLDQCLAAQPLEDI [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=P52003 [UniProt boundaries chain B]=5-139 [UniProt coverage chain B]=91% [Name chain B]=Multidrug resistance operon repressor [UniProt sequence chain B]=MNYPVNPDLMPALMAVFQHVRTRIQSELDCQRLDLTPPDVHVLKLIDEQRGLNLQDLGRQMCRDKALITRKIRELEGRNLVRRERNPSDQRSFQLFLTDEGLAIHQHAEAIMSRVHDELFAPLTPVEQATLVHLLDQCLAAQPLEDI [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.19 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000618 [Entry] [Entry number]=803 [Entry name]=Lactococcus lactis ZitR, C30S mutant [PDB ID]=5yhy [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=Q9CDU5 [UniProt boundaries chain A]=1-145 [UniProt coverage chain A]=100% [Name chain A]=Zinc transport transcriptional regulator [UniProt sequence chain A]=MSLANQIDQFLGTIMQFAENKHEILLGKCESDVKLTSTQEHILMLLAEQISTNAKIAEKLKISPAAVTKALKKLQEQELIKSSRATNDERVVLWSLTEKAVPVAKEHATHHEKTLSTYQELGNKFTDEEQEVISKFLSALTEEFQ [Source organism chain A]=Lactococcus lactis subsp lactis [UniProt ID chain A-2]=Q9CDU5 [UniProt boundaries chain A-2]=1-145 [UniProt coverage chain A-2]=100% [Name chain A-2]=Zinc transport transcriptional regulator [UniProt sequence chain A-2]=MSLANQIDQFLGTIMQFAENKHEILLGKCESDVKLTSTQEHILMLLAEQISTNAKIAEKLKISPAAVTKALKKLQEQELIKSSRATNDERVVLWSLTEKAVPVAKEHATHHEKTLSTYQELGNKFTDEEQEVISKFLSALTEEFQ [Source organism chain A-2]=Lactococcus lactis subsp lactis [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Lactococcus lactis subsp lactis [Accession]=MF7000619 [Entry] [Entry number]=804 [Entry name]=Lactococcus lactis ZitR, E41A mutant [PDB ID]=5yhz [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=Q9CDU5 [UniProt boundaries chain A]=1-145 [UniProt coverage chain A]=100% [Name chain A]=Zinc transport transcriptional regulator [UniProt sequence chain A]=MSLANQIDQFLGTIMQFAENKHEILLGKCESDVKLTSTQEHILMLLAEQISTNAKIAEKLKISPAAVTKALKKLQEQELIKSSRATNDERVVLWSLTEKAVPVAKEHATHHEKTLSTYQELGNKFTDEEQEVISKFLSALTEEFQ [Source organism chain A]=Lactococcus lactis subsp lactis [UniProt ID chain A-2]=Q9CDU5 [UniProt boundaries chain A-2]=1-145 [UniProt coverage chain A-2]=100% [Name chain A-2]=Zinc transport transcriptional regulator [UniProt sequence chain A-2]=MSLANQIDQFLGTIMQFAENKHEILLGKCESDVKLTSTQEHILMLLAEQISTNAKIAEKLKISPAAVTKALKKLQEQELIKSSRATNDERVVLWSLTEKAVPVAKEHATHHEKTLSTYQELGNKFTDEEQEVISKFLSALTEEFQ [Source organism chain A-2]=Lactococcus lactis subsp lactis [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Lactococcus lactis subsp lactis [Accession]=MF7000620 [Entry] [Entry number]=805 [Entry name]=Lactococcus lactis ZitR, C30AH42A mutant (apo form) [PDB ID]=5yi1 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=Q9CDU5 [UniProt boundaries chain A]=1-145 [UniProt coverage chain A]=100% [Name chain A]=Zinc transport transcriptional regulator [UniProt sequence chain A]=MSLANQIDQFLGTIMQFAENKHEILLGKCESDVKLTSTQEHILMLLAEQISTNAKIAEKLKISPAAVTKALKKLQEQELIKSSRATNDERVVLWSLTEKAVPVAKEHATHHEKTLSTYQELGNKFTDEEQEVISKFLSALTEEFQ [Source organism chain A]=Lactococcus lactis subsp lactis [UniProt ID chain A-2]=Q9CDU5 [UniProt boundaries chain A-2]=1-145 [UniProt coverage chain A-2]=100% [Name chain A-2]=Zinc transport transcriptional regulator [UniProt sequence chain A-2]=MSLANQIDQFLGTIMQFAENKHEILLGKCESDVKLTSTQEHILMLLAEQISTNAKIAEKLKISPAAVTKALKKLQEQELIKSSRATNDERVVLWSLTEKAVPVAKEHATHHEKTLSTYQELGNKFTDEEQEVISKFLSALTEEFQ [Source organism chain A-2]=Lactococcus lactis subsp lactis [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Lactococcus lactis subsp lactis [Accession]=MF7000621 [Entry] [Entry number]=806 [Entry name]=Transcriptional repressor, CouR [PDB ID]=6c9t [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=Q6N8V9 [UniProt boundaries chain A]=42-183 [UniProt coverage chain A]=77% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MTSSNRITSPAMTASKTAAVAKPTRAGRKAPAVETAPEASELKMGELSELLGYALKRAQLRVFEDFLHCVAPVQLTPAQFSVLLLLDANPGRNQTEIATTLGILRPNFVAMLDALEGRGLCVRTRSPSDRRSHILMLTDKGRATLARAKKLVATRHEDRLTELLGRDNRDALLSMLATIAREF [Source organism chain A]=Rhodopseudomonas palustris [UniProt ID chain B]=Q6N8V9 [UniProt boundaries chain B]=42-183 [UniProt coverage chain B]=77% [Name chain B]=Transcriptional regulator, MarR family [UniProt sequence chain B]=MTSSNRITSPAMTASKTAAVAKPTRAGRKAPAVETAPEASELKMGELSELLGYALKRAQLRVFEDFLHCVAPVQLTPAQFSVLLLLDANPGRNQTEIATTLGILRPNFVAMLDALEGRGLCVRTRSPSDRRSHILMLTDKGRATLARAKKLVATRHEDRLTELLGRDNRDALLSMLATIAREF [Source organism chain B]=Rhodopseudomonas palustris [ExpTech]=X-ray [Resolution]=2.07 [Source organism]=Rhodopseudomonas palustris [Accession]=MF7000622 [Entry] [Entry number]=807 [Entry name]=Transcriptional regulator (Bacillus subtilis, strain 168) [PDB ID]=7wze [Chains]=Y,A [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain Y]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain Y]=O31541 [UniProt boundaries chain Y]=2-167 [UniProt coverage chain Y]=99% [Name chain Y]=HTH-type transcriptional repressor YetL [UniProt sequence chain Y]=MELKHLPKYKHITEHAETYANIDAGSLELFLSLFDISKKMNHVMEHYFAGRGLSEGKFKILMLLFDAKDHRLSPTELAKRSNVTKATITGLLDGLARDGFVSRRHHTEDKRKISIELTTEGKARLEQFLPGHFSKISAVMENYSDEEKDMFVKMLGDLFERLSVFKD [Source organism chain Y]=Bacillus subtilis [UniProt ID chain A]=O31541 [UniProt boundaries chain A]=2-166 [UniProt coverage chain A]=98% [Name chain A]=HTH-type transcriptional repressor YetL [UniProt sequence chain A]=MELKHLPKYKHITEHAETYANIDAGSLELFLSLFDISKKMNHVMEHYFAGRGLSEGKFKILMLLFDAKDHRLSPTELAKRSNVTKATITGLLDGLARDGFVSRRHHTEDKRKISIELTTEGKARLEQFLPGHFSKISAVMENYSDEEKDMFVKMLGDLFERLSVFKD [Source organism chain A]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=2.65 [Source organism]=Bacillus subtilis [Accession]=MF7000623 [Entry] [Entry number]=808 [Entry name]=MarR family transcriptional regulator with3-IAA (Pseudomonas putida) [PDB ID]=7kua [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=B0FXI7 [UniProt boundaries chain A]=19-167 [UniProt coverage chain A]=89% [Name chain A]=HTH-type transcriptional repressor IacR [UniProt sequence chain A]=MSNAKNTSAASPARKGHSHHDPASDEFRKEDFPFYWLARVHGRYTQNMERLLKKIDLDVPRWRVLWILNENGESSISEISTHAIAKLSTITKIVYRMKEDGLVDTAPSPEDGRVTQVRITEVGLQNIERMQEVTRELFQRSFKGLTEAQVQRLNRMLEVVFHNLETL [Source organism chain A]=Pseudomonas putida [UniProt ID chain A-2]=B0FXI7 [UniProt boundaries chain A-2]=19-167 [UniProt coverage chain A-2]=89% [Name chain A-2]=HTH-type transcriptional repressor IacR [UniProt sequence chain A-2]=MSNAKNTSAASPARKGHSHHDPASDEFRKEDFPFYWLARVHGRYTQNMERLLKKIDLDVPRWRVLWILNENGESSISEISTHAIAKLSTITKIVYRMKEDGLVDTAPSPEDGRVTQVRITEVGLQNIERMQEVTRELFQRSFKGLTEAQVQRLNRMLEVVFHNLETL [Source organism chain A-2]=Pseudomonas putida [ExpTech]=X-ray [Resolution]=1.89 [Source organism]=Pseudomonas putida [Accession]=MF7000624 [Entry] [Entry number]=809 [Entry name]=MarR family transcriptional regulator with 1H-indole-3-carboxylic Acid (Variovorax paradoxus) [PDB ID]=7kfq [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=9-149 [UniProt coverage chain A]=89% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=9-149 [UniProt coverage chain A-2]=89% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=Variovorax paradoxus [Accession]=MF7000625 [Entry] [Entry number]=810 [Entry name]=MarR family transcriptional regulator with benzoic acid (Variovorax paradoxus) [PDB ID]=7kfs [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-149 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-149 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Variovorax paradoxus [Accession]=MF7000626 [Entry] [Entry number]=811 [Entry name]=MarR family transcriptional regulator with indole 3 propionic acid (Variovorax paradoxus) [PDB ID]=7kh3 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-149 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-149 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Variovorax paradoxus [Accession]=MF7000627 [Entry] [Entry number]=812 [Entry name]=MarR family transcriptional regulator with indole-3-butyric acid (Variovorax paradoxus) [PDB ID]=7kig [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-149 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-149 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Variovorax paradoxus [Accession]=MF7000628 [Entry] [Entry number]=813 [Entry name]=MarR family transcriptional regulator with salicylic acid (Variovorax paradoxus) [PDB ID]=7kjl [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-148 [UniProt coverage chain A]=87% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-148 [UniProt coverage chain A-2]=87% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Variovorax paradoxus [Accession]=MF7000629 [Entry] [Entry number]=814 [Entry name]=MarR family transcriptional regulator with Picloram (Variovorax paradoxus) [PDB ID]=7kjq [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-149 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-149 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=Variovorax paradoxus [Accession]=MF7000630 [Entry] [Entry number]=815 [Entry name]=MarR family transcriptional regulator, double mutant S28A and R46A (Variovorax paradoxus) [PDB ID]=7krh [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-149 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-149 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Variovorax paradoxus [Accession]=MF7000631 [Entry] [Entry number]=816 [Entry name]=MarR family transcriptional regulator with indole-3-acetic acid (Variovorax paradoxus) [PDB ID]=7kfo [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-149 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-149 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.30 [Source organism]=Variovorax paradoxus [Accession]=MF7000632 [Entry] [Entry number]=817 [Entry name]=MarR family transcriptional regulator with catechol (Variovorax paradoxus) [PDB ID]=7kk0 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-149 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-149 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Variovorax paradoxus [Accession]=MF7000633 [Entry] [Entry number]=818 [Entry name]=MarR family transcriptional regulator with 5-hydroxyindoleacetic acid (Variovorax paradoxus) [PDB ID]=7kkc [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-149 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-149 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Variovorax paradoxus [Accession]=MF7000634 [Entry] [Entry number]=819 [Entry name]=MarR family transcriptional regulator with 2,4-dichlorophenoxyacetic acid (Variovorax paradoxus) [PDB ID]=7kki [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type I) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=The MarR-type family transcriptional regulator, NadR is dimeric in solution (SE-HPLC/MALLS) as other MarR faimily proteins (PMID:18272181). Compared to ligand-stabilized holo-NadR, apo-NadR displayed an intrinsic flexibility focused in the DNA-binding region (PMID:27105075). The structural features of several family members have been described, they all have two subdomains: there is a helix-turn-helix (HTH) DNA-binding domain plus dimerization helices that form an interlocked dimerization domain. Dimerization is mediated by helices α1, α5, and α6 from each monomer resulting in an interlocked, tight dimer burying a large, hydrophobic solvent-accessible surface area. The structure of the dimerization region reveals domain swapping, where α1 of one subunit is inserted between α5′ and α6′ of the other subunit and forms a coiled coil with helix α6′ (PMID:19586910). The DNA-binding elements contain helices α3-α4 and strands β1-β2 from each monomer (PMID:29794028, PMID:35367827). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000246,MF7000614,MF7000243,MF7000244,MF7000615,MF7000616,MF7000617,MF7000157,MF7000618,MF7000255,MF7000249,MF7000250,MF7000619,MF7000620,MF7000621,MF7000622,MF7000623,MF7000624,MF7000625,MF7000626,MF7000627,MF7000628,MF7000629,MF7000630,MF7000631,MF7000632,MF7000633,MF7000634,MF7000635 [UniProt ID chain A]=C5CSP2 [UniProt boundaries chain A]=10-149 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A]=Variovorax paradoxus [UniProt ID chain A-2]=C5CSP2 [UniProt boundaries chain A-2]=10-149 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MAEQPPETHRFVDDYLPALLAQASQLISSEFHEVARQHGFSVSEWRVMASLAGSEPISIGQLAQVTVTKQPTVTRLLDRMEARGQVERLPHESDRRITLVRITRKGLKAVEHLMELAREHERRVLEPFGLRRAEELKQTLRQMIDLHVHVPVEEPEED [Source organism chain A-2]=Variovorax paradoxus [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Variovorax paradoxus [Accession]=MF7000635 [Entry] [Entry number]=820 [Entry name]=Selenomethionine substituted chalcone o-methyltransferase [PDB ID]=1fpq [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=P93324 [UniProt boundaries chain A]=20-372 [UniProt coverage chain A]=94% [Name chain A]=Isoliquiritigenin 2'-O-methyltransferase [UniProt sequence chain A]=MGNSYITKEDNQISATSEQTEDSACLSAMVLTTNLVYPAVLNAAIDLNLFEIIAKATPPGAFMSPSEIASKLPASTQHSDLPNRLDRMLRLLASYSVLTSTTRTIEDGGAERVYGLSMVGKYLVPDESRGYLASFTTFLCYPALLQVWMNFKEAVVDEDIDLFKNVHGVTKYEFMGKDKKMNQIFNKSMVDVCATEMKRMLEIYTGFEGISTLVDVGGGSGRNLELIISKYPLIKGINFDLPQVIENAPPLSGIEHVGGDMFASVPQGDAMILKAVCHNWSDEKCIEFLSNCHKALSPNGKVIIVEFILPEEPNTSEESKLVSTLDNLMFITVGGRERTEKQYEKLSKLSGFSKFQVACRAFNSLGVMEFYK [Source organism chain A]=Medicago sativa [UniProt ID chain A-2]=P93324 [UniProt boundaries chain A-2]=20-372 [UniProt coverage chain A-2]=94% [Name chain A-2]=Isoliquiritigenin 2'-O-methyltransferase [UniProt sequence chain A-2]=MGNSYITKEDNQISATSEQTEDSACLSAMVLTTNLVYPAVLNAAIDLNLFEIIAKATPPGAFMSPSEIASKLPASTQHSDLPNRLDRMLRLLASYSVLTSTTRTIEDGGAERVYGLSMVGKYLVPDESRGYLASFTTFLCYPALLQVWMNFKEAVVDEDIDLFKNVHGVTKYEFMGKDKKMNQIFNKSMVDVCATEMKRMLEIYTGFEGISTLVDVGGGSGRNLELIISKYPLIKGINFDLPQVIENAPPLSGIEHVGGDMFASVPQGDAMILKAVCHNWSDEKCIEFLSNCHKALSPNGKVIIVEFILPEEPNTSEESKLVSTLDNLMFITVGGRERTEKQYEKLSKLSGFSKFQVACRAFNSLGVMEFYK [Source organism chain A-2]=Medicago sativa [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Medicago sativa [Accession]=MF7000636 [Entry] [Entry number]=821 [Entry name]=Selenomethionine substituted isoflavone o-methyltransferase [PDB ID]=6cig [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=O24529 [UniProt boundaries chain A]=4-352 [UniProt coverage chain A]=99% [Name chain A]=Isoflavone-7-O-methyltransferase 8 [UniProt sequence chain A]=MASSINGRKPSEIFKAQALLYKHIYAFIDSMSLKWAVEMNIPNIIQNHGKPISLSNLVSILQVPSSKIGNVRRLMRYLAHNGFFEIITKEEESYALTVASELLVRGSDLCLAPMVECVLDPTLSGSYHELKKWIYEEDLTLFGVTLGSGFWDFLDKNPEYNTSFNDAMASDSKLINLALRDCDFVFDGLESIVDVGGGTGTTAKIICETFPKLKCIVFDRPQVVENLSGSNNLTYVGGDMFTSIPNADAVLLKYILHNWTDKDCLRILKKCKEAVTNDGKRGKVTIIDMVIDKKKDENQVTQIKLLMDVNMACLNGKERNEEEWKKLFIEAGFQHYKISPLTGFLSLIEIYP [Source organism chain A]=Medicago sativa [UniProt ID chain A-2]=O24529 [UniProt boundaries chain A-2]=4-352 [UniProt coverage chain A-2]=99% [Name chain A-2]=Isoflavone-7-O-methyltransferase 8 [UniProt sequence chain A-2]=MASSINGRKPSEIFKAQALLYKHIYAFIDSMSLKWAVEMNIPNIIQNHGKPISLSNLVSILQVPSSKIGNVRRLMRYLAHNGFFEIITKEEESYALTVASELLVRGSDLCLAPMVECVLDPTLSGSYHELKKWIYEEDLTLFGVTLGSGFWDFLDKNPEYNTSFNDAMASDSKLINLALRDCDFVFDGLESIVDVGGGTGTTAKIICETFPKLKCIVFDRPQVVENLSGSNNLTYVGGDMFTSIPNADAVLLKYILHNWTDKDCLRILKKCKEAVTNDGKRGKVTIIDMVIDKKKDENQVTQIKLLMDVNMACLNGKERNEEEWKKLFIEAGFQHYKISPLTGFLSLIEIYP [Source organism chain A-2]=Medicago sativa [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Medicago sativa [Accession]=MF7000637 [Entry] [Entry number]=822 [Entry name]=Isoflavone o-methyltransferase [PDB ID]=1fp2 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=O24529 [UniProt boundaries chain A]=8-352 [UniProt coverage chain A]=98% [Name chain A]=Isoflavone-7-O-methyltransferase 8 [UniProt sequence chain A]=MASSINGRKPSEIFKAQALLYKHIYAFIDSMSLKWAVEMNIPNIIQNHGKPISLSNLVSILQVPSSKIGNVRRLMRYLAHNGFFEIITKEEESYALTVASELLVRGSDLCLAPMVECVLDPTLSGSYHELKKWIYEEDLTLFGVTLGSGFWDFLDKNPEYNTSFNDAMASDSKLINLALRDCDFVFDGLESIVDVGGGTGTTAKIICETFPKLKCIVFDRPQVVENLSGSNNLTYVGGDMFTSIPNADAVLLKYILHNWTDKDCLRILKKCKEAVTNDGKRGKVTIIDMVIDKKKDENQVTQIKLLMDVNMACLNGKERNEEEWKKLFIEAGFQHYKISPLTGFLSLIEIYP [Source organism chain A]=Medicago sativa [UniProt ID chain A-2]=O24529 [UniProt boundaries chain A-2]=8-352 [UniProt coverage chain A-2]=98% [Name chain A-2]=Isoflavone-7-O-methyltransferase 8 [UniProt sequence chain A-2]=MASSINGRKPSEIFKAQALLYKHIYAFIDSMSLKWAVEMNIPNIIQNHGKPISLSNLVSILQVPSSKIGNVRRLMRYLAHNGFFEIITKEEESYALTVASELLVRGSDLCLAPMVECVLDPTLSGSYHELKKWIYEEDLTLFGVTLGSGFWDFLDKNPEYNTSFNDAMASDSKLINLALRDCDFVFDGLESIVDVGGGTGTTAKIICETFPKLKCIVFDRPQVVENLSGSNNLTYVGGDMFTSIPNADAVLLKYILHNWTDKDCLRILKKCKEAVTNDGKRGKVTIIDMVIDKKKDENQVTQIKLLMDVNMACLNGKERNEEEWKKLFIEAGFQHYKISPLTGFLSLIEIYP [Source organism chain A-2]=Medicago sativa [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Medicago sativa [Accession]=MF7000638 [Entry] [Entry number]=823 [Entry name]=Isoflavanone 4'-O-methyltransferase with SAH and 2,7,4'-trihydroxyisoflavanone [PDB ID]=1zg3 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=Q29U70 [UniProt boundaries chain A]=7-364 [UniProt coverage chain A]=98% [Name chain A]=Isoflavone 4'-O-methyltransferase [UniProt sequence chain A]=MAFSTNGSEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSELASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPPSKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGESFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVGGGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPSADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSDDRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFKSLIEVYP [Source organism chain A]=Medicago truncatula [UniProt ID chain A-2]=Q29U70 [UniProt boundaries chain A-2]=7-364 [UniProt coverage chain A-2]=98% [Name chain A-2]=Isoflavone 4'-O-methyltransferase [UniProt sequence chain A-2]=MAFSTNGSEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSELASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPPSKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGESFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVGGGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPSADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSDDRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFKSLIEVYP [Source organism chain A-2]=Medicago truncatula [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Medicago truncatula [Accession]=MF7000639 [Entry] [Entry number]=824 [Entry name]=Isoflavanone 4'-O-methyltransferase with (+)-6a-hydroxymaackiain [PDB ID]=1zga [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=Q29U70 [UniProt boundaries chain A]=8-364 [UniProt coverage chain A]=98% [Name chain A]=Isoflavone 4'-O-methyltransferase [UniProt sequence chain A]=MAFSTNGSEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSELASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPPSKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGESFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVGGGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPSADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSDDRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFKSLIEVYP [Source organism chain A]=Medicago truncatula [UniProt ID chain A-2]=Q29U70 [UniProt boundaries chain A-2]=8-364 [UniProt coverage chain A-2]=98% [Name chain A-2]=Isoflavone 4'-O-methyltransferase [UniProt sequence chain A-2]=MAFSTNGSEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSELASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPPSKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGESFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVGGGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPSADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSDDRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFKSLIEVYP [Source organism chain A-2]=Medicago truncatula [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Medicago truncatula [Accession]=MF7000640 [Entry] [Entry number]=825 [Entry name]=Isoflavanone 4'-O-methyltransferase with (+)-pisatin [PDB ID]=1zgj [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=Q29U70 [UniProt boundaries chain A]=11-364 [UniProt coverage chain A]=97% [Name chain A]=Isoflavone 4'-O-methyltransferase [UniProt sequence chain A]=MAFSTNGSEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSELASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPPSKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGESFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVGGGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPSADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSDDRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFKSLIEVYP [Source organism chain A]=Medicago truncatula [UniProt ID chain A-2]=Q29U70 [UniProt boundaries chain A-2]=11-364 [UniProt coverage chain A-2]=97% [Name chain A-2]=Isoflavone 4'-O-methyltransferase [UniProt sequence chain A-2]=MAFSTNGSEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSELASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPPSKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGESFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVGGGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPSADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSDDRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFKSLIEVYP [Source organism chain A-2]=Medicago truncatula [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Medicago truncatula [Accession]=MF7000641 [Entry] [Entry number]=826 [Entry name]=Selenomethionine substituted isoflavanone 4'-O-methyltransferase [PDB ID]=1zhf [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=Q29U70 [UniProt boundaries chain A]=8-364 [UniProt coverage chain A]=98% [Name chain A]=Isoflavone 4'-O-methyltransferase [UniProt sequence chain A]=MAFSTNGSEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSELASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPPSKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGESFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVGGGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPSADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSDDRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFKSLIEVYP [Source organism chain A]=Medicago truncatula [UniProt ID chain A-2]=Q29U70 [UniProt boundaries chain A-2]=8-364 [UniProt coverage chain A-2]=98% [Name chain A-2]=Isoflavone 4'-O-methyltransferase [UniProt sequence chain A-2]=MAFSTNGSEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSELASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTPPSKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATGESFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDVGGGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIPSADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETSDDRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGFKSLIEVYP [Source organism chain A-2]=Medicago truncatula [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Medicago truncatula [Accession]=MF7000642 [Entry] [Entry number]=827 [Entry name]=CalO1 with SAH [PDB ID]=3lst [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=Q8KNE5 [UniProt boundaries chain A]=13-345 [UniProt coverage chain A]=96% [Name chain A]=CalO1 [UniProt sequence chain A]=MQRQRPPSRAGGDMDRLQSALALYEEAMGYTYAAALRAAAAVGVADHLVDGPRTPAELAAATGTDADALRRVLRLLAVRDVVRESDGRFALTDKGAALRSDSPVPARAGILMFTDTMFWTMSHRVASALGPERPAFADIFGSSLDAYFDGDAEVEALYYEGMETVSAAEHLILARAGDFPATGTVADVGGGRGGFLLTVLREHPGLQGVLLDRAEVVARHRLDAPDVAGRWKVVEGDFLREVPHADVHVLKRILHNWGDEDSVRILTNCRRVMPAHGRVLVIDAVVPEGNDAHQSKEMDFMMLAARTGQERTAAELEPLFTAAGLRLDRVVGTSSVMSIAVGVPA [Source organism chain A]=Micromonospora echinospora [UniProt ID chain A-2]=Q8KNE5 [UniProt boundaries chain A-2]=13-345 [UniProt coverage chain A-2]=96% [Name chain A-2]=CalO1 [UniProt sequence chain A-2]=MQRQRPPSRAGGDMDRLQSALALYEEAMGYTYAAALRAAAAVGVADHLVDGPRTPAELAAATGTDADALRRVLRLLAVRDVVRESDGRFALTDKGAALRSDSPVPARAGILMFTDTMFWTMSHRVASALGPERPAFADIFGSSLDAYFDGDAEVEALYYEGMETVSAAEHLILARAGDFPATGTVADVGGGRGGFLLTVLREHPGLQGVLLDRAEVVARHRLDAPDVAGRWKVVEGDFLREVPHADVHVLKRILHNWGDEDSVRILTNCRRVMPAHGRVLVIDAVVPEGNDAHQSKEMDFMMLAARTGQERTAAELEPLFTAAGLRLDRVVGTSSVMSIAVGVPA [Source organism chain A-2]=Micromonospora echinospora [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Micromonospora echinospora [Accession]=MF7000643 [Entry] [Entry number]=828 [Entry name]=Coniferyl Alcohol 9-O-Methyltransferase with coniferyl alcohol (Linum Nodiflorum) [PDB ID]=4e70 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A6XNE6 [UniProt boundaries chain A]=1-368 [UniProt coverage chain A]=100% [Name chain A]=Coniferyl alcohol 9-O-methyltransferase [UniProt sequence chain A]=MDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIPQTKAPFLSRLMRMLVHLGYFTQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRTGKEDGKDTPNAFAFAHEGKKVYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAETFPNIHCTVFDLPHVVSGPKQTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMIADHVLDHESCNDSNSMGTSLILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP [Source organism chain A]=Linum nodiflorum [UniProt ID chain B]=A6XNE6 [UniProt boundaries chain B]=1-368 [UniProt coverage chain B]=100% [Name chain B]=Coniferyl alcohol 9-O-methyltransferase [UniProt sequence chain B]=MDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIPQTKAPFLSRLMRMLVHLGYFTQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRTGKEDGKDTPNAFAFAHEGKKVYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAETFPNIHCTVFDLPHVVSGPKQTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMIADHVLDHESCNDSNSMGTSLILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP [Source organism chain B]=Linum nodiflorum [ExpTech]=X-ray [Resolution]=1.61 [Source organism]=Linum nodiflorum [Accession]=MF7000644 [Entry] [Entry number]=829 [Entry name]=Coniferyl Alcohol 9-O-Methyltransferase (Linum Nodiflorum) [PDB ID]=4ems [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A6XNE6 [UniProt boundaries chain A]=1-368 [UniProt coverage chain A]=100% [Name chain A]=Coniferyl alcohol 9-O-methyltransferase [UniProt sequence chain A]=MDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIPQTKAPFLSRLMRMLVHLGYFTQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRTGKEDGKDTPNAFAFAHEGKKVYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAETFPNIHCTVFDLPHVVSGPKQTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMIADHVLDHESCNDSNSMGTSLILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP [Source organism chain A]=Linum nodiflorum [UniProt ID chain B]=A6XNE6 [UniProt boundaries chain B]=1-368 [UniProt coverage chain B]=100% [Name chain B]=Coniferyl alcohol 9-O-methyltransferase [UniProt sequence chain B]=MDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIPQTKAPFLSRLMRMLVHLGYFTQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRTGKEDGKDTPNAFAFAHEGKKVYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAETFPNIHCTVFDLPHVVSGPKQTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMIADHVLDHESCNDSNSMGTSLILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP [Source organism chain B]=Linum nodiflorum [ExpTech]=X-ray [Resolution]=1.75 [Source organism]=Linum nodiflorum [Accession]=MF7000645 [Entry] [Entry number]=830 [Entry name]=Coniferyl Alcohol 9-O-Methyltransferase (Linum Nodiflorum) [PDB ID]=4evi [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A6XNE6 [UniProt boundaries chain A]=1-368 [UniProt coverage chain A]=100% [Name chain A]=Coniferyl alcohol 9-O-methyltransferase [UniProt sequence chain A]=MDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIPQTKAPFLSRLMRMLVHLGYFTQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRTGKEDGKDTPNAFAFAHEGKKVYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAETFPNIHCTVFDLPHVVSGPKQTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMIADHVLDHESCNDSNSMGTSLILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP [Source organism chain A]=Linum nodiflorum [UniProt ID chain B]=A6XNE6 [UniProt boundaries chain B]=1-368 [UniProt coverage chain B]=100% [Name chain B]=Coniferyl alcohol 9-O-methyltransferase [UniProt sequence chain B]=MDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIPQTKAPFLSRLMRMLVHLGYFTQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRTGKEDGKDTPNAFAFAHEGKKVYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAETFPNIHCTVFDLPHVVSGPKQTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMIADHVLDHESCNDSNSMGTSLILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP [Source organism chain B]=Linum nodiflorum [ExpTech]=X-ray [Resolution]=2.02 [Source organism]=Linum nodiflorum [Accession]=MF7000646 [Entry] [Entry number]=831 [Entry name]=Methyltransferase CalO6 [PDB ID]=4z2y [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=Q8KND2 [UniProt boundaries chain A]=11-346 [UniProt coverage chain A]=94% [Name chain A]=CalO6 [UniProt sequence chain A]=MELTTTAARPGLRHRMQQLIYGFFTAQTLHVAVRLRIPDLLADGARDVGDLASATGADAPSLRRLLRALVFLEVLDEPAPGTFALTEQGEVLRADVTGSMRELVLLLSGPESWAAWGQLEHSVRTGEVAWEHVHGRSCFDHLMADPQRQAAFNAAMAEGSRAFVPTLLSAYDFGDLRTVVDVGGGSGALLAGVLAAHPHLRGTVFDTPDGVADAARTVAEQGVADRCGVETGDFFVSVPPGADAYVLKSVLHDWDDEQCVEVLRTVRRAVRPDSRVILVESLMPTTVTTAPSVAQVVMNDLNMMVCHGGRERTVAEFRELLRVAGFRLESVTPCPAPSVVGILEAAPAPATGPDGS [Source organism chain A]=Micromonospora echinospora [UniProt ID chain A-2]=Q8KND2 [UniProt boundaries chain A-2]=11-346 [UniProt coverage chain A-2]=94% [Name chain A-2]=CalO6 [UniProt sequence chain A-2]=MELTTTAARPGLRHRMQQLIYGFFTAQTLHVAVRLRIPDLLADGARDVGDLASATGADAPSLRRLLRALVFLEVLDEPAPGTFALTEQGEVLRADVTGSMRELVLLLSGPESWAAWGQLEHSVRTGEVAWEHVHGRSCFDHLMADPQRQAAFNAAMAEGSRAFVPTLLSAYDFGDLRTVVDVGGGSGALLAGVLAAHPHLRGTVFDTPDGVADAARTVAEQGVADRCGVETGDFFVSVPPGADAYVLKSVLHDWDDEQCVEVLRTVRRAVRPDSRVILVESLMPTTVTTAPSVAQVVMNDLNMMVCHGGRERTVAEFRELLRVAGFRLESVTPCPAPSVVGILEAAPAPATGPDGS [Source organism chain A-2]=Micromonospora echinospora [ExpTech]=X-ray [Resolution]=3.40 [Source organism]=Micromonospora echinospora [Accession]=MF7000647 [Entry] [Entry number]=832 [Entry name]=OxaC with SAH and oxaline [PDB ID]=5w7r [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A0A1B2TT09 [UniProt boundaries chain A]=8-405 [UniProt coverage chain A]=98% [Name chain A]=OxaC [UniProt sequence chain A]=MTFSNADAQKIAVQKDVDEVVAAAQRFLHGSGNATSDEAKVDLQKKASNLVQTIRGPIPAALSSMEDIVKVASLRTLFEAGVFHAMPKGGASMTASEISAQTGLDKGILIRLMRAVTPLGPFHEVGEEEYAHTPFSEAYLTADIAGCFPVMSNFIFGPVLQICDFLRQNNWKDAITTRNNPFTLAHNCPGETMFEHLYKNSKNVAPVTKAEAADVDQIAMDLYPWEERLSDAKGSNATLVDIAGSHGNGTRAIMALAPKLNGCRFIVQDLEPVIGEHSQALRAEGIEPQVYDFLKQEQPVHGASIYYFRRVFHDWPDLPEGKKILDNTRAAMSREHSRILIHDIIVPEIGATMSHAWQDLSLMAIGGMERTEKDFARLLDIAGLALVKVWRKPGDMMGIIEARLK [Source organism chain A]=Penicillium oxalicum [UniProt ID chain A-2]=A0A1B2TT09 [UniProt boundaries chain A-2]=8-405 [UniProt coverage chain A-2]=98% [Name chain A-2]=OxaC [UniProt sequence chain A-2]=MTFSNADAQKIAVQKDVDEVVAAAQRFLHGSGNATSDEAKVDLQKKASNLVQTIRGPIPAALSSMEDIVKVASLRTLFEAGVFHAMPKGGASMTASEISAQTGLDKGILIRLMRAVTPLGPFHEVGEEEYAHTPFSEAYLTADIAGCFPVMSNFIFGPVLQICDFLRQNNWKDAITTRNNPFTLAHNCPGETMFEHLYKNSKNVAPVTKAEAADVDQIAMDLYPWEERLSDAKGSNATLVDIAGSHGNGTRAIMALAPKLNGCRFIVQDLEPVIGEHSQALRAEGIEPQVYDFLKQEQPVHGASIYYFRRVFHDWPDLPEGKKILDNTRAAMSREHSRILIHDIIVPEIGATMSHAWQDLSLMAIGGMERTEKDFARLLDIAGLALVKVWRKPGDMMGIIEARLK [Source organism chain A-2]=Penicillium oxalicum [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Penicillium oxalicum [Accession]=MF7000648 [Entry] [Entry number]=833 [Entry name]=OxaC with sinefungin and meleagrin [PDB ID]=5w7s [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A0A1B2TT09 [UniProt boundaries chain A]=8-405 [UniProt coverage chain A]=98% [Name chain A]=OxaC [UniProt sequence chain A]=MTFSNADAQKIAVQKDVDEVVAAAQRFLHGSGNATSDEAKVDLQKKASNLVQTIRGPIPAALSSMEDIVKVASLRTLFEAGVFHAMPKGGASMTASEISAQTGLDKGILIRLMRAVTPLGPFHEVGEEEYAHTPFSEAYLTADIAGCFPVMSNFIFGPVLQICDFLRQNNWKDAITTRNNPFTLAHNCPGETMFEHLYKNSKNVAPVTKAEAADVDQIAMDLYPWEERLSDAKGSNATLVDIAGSHGNGTRAIMALAPKLNGCRFIVQDLEPVIGEHSQALRAEGIEPQVYDFLKQEQPVHGASIYYFRRVFHDWPDLPEGKKILDNTRAAMSREHSRILIHDIIVPEIGATMSHAWQDLSLMAIGGMERTEKDFARLLDIAGLALVKVWRKPGDMMGIIEARLK [Source organism chain A]=Penicillium oxalicum [UniProt ID chain A-2]=A0A1B2TT09 [UniProt boundaries chain A-2]=8-405 [UniProt coverage chain A-2]=98% [Name chain A-2]=OxaC [UniProt sequence chain A-2]=MTFSNADAQKIAVQKDVDEVVAAAQRFLHGSGNATSDEAKVDLQKKASNLVQTIRGPIPAALSSMEDIVKVASLRTLFEAGVFHAMPKGGASMTASEISAQTGLDKGILIRLMRAVTPLGPFHEVGEEEYAHTPFSEAYLTADIAGCFPVMSNFIFGPVLQICDFLRQNNWKDAITTRNNPFTLAHNCPGETMFEHLYKNSKNVAPVTKAEAADVDQIAMDLYPWEERLSDAKGSNATLVDIAGSHGNGTRAIMALAPKLNGCRFIVQDLEPVIGEHSQALRAEGIEPQVYDFLKQEQPVHGASIYYFRRVFHDWPDLPEGKKILDNTRAAMSREHSRILIHDIIVPEIGATMSHAWQDLSLMAIGGMERTEKDFARLLDIAGLALVKVWRKPGDMMGIIEARLK [Source organism chain A-2]=Penicillium oxalicum [ExpTech]=X-ray [Resolution]=2.95 [Source organism]=Penicillium oxalicum [Accession]=MF7000649 [Entry] [Entry number]=834 [Entry name]=LcCOMT with SAH [PDB ID]=7v6l [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A0A0K1YW34 [UniProt boundaries chain A]=13-362 [UniProt coverage chain A]=96% [Name chain A]=Caffeic acid 3-O-methyltransferase [UniProt sequence chain A]=MNTELIPPTFLEDEEEEACMFAMQLSSASVLPMVLKSAIELNLLESIAKAGPGVYVSPSHLAAGLPSSQPDTPVMLDRILRLLASYSVLNCQLRDLPQGRVERLYGLAPVCKFLTKNSDGVSMAPLLLMNQDKILMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGKDPRFNKVFNQGMSNHSTITMKKILQTYDGFGGLKTVVDVGGGTGATLNMIISKYPNLKGINFDLPHVVEDAPSYPGVEHVGGDMFVSVPKGDAIFMKWICHDWSDAHCLTFLKNCYKALPKDGKVILAECILPEAPDSKLTTKNVIHIDVIMLAHNPGGKERTEKDFEALGKEAGFKSFNKACCAYNTWVIEYYK [Source organism chain A]=Ligusticum sinense [UniProt ID chain B]=A0A0K1YW34 [UniProt boundaries chain B]=11-362 [UniProt coverage chain B]=97% [Name chain B]=Caffeic acid 3-O-methyltransferase [UniProt sequence chain B]=MNTELIPPTFLEDEEEEACMFAMQLSSASVLPMVLKSAIELNLLESIAKAGPGVYVSPSHLAAGLPSSQPDTPVMLDRILRLLASYSVLNCQLRDLPQGRVERLYGLAPVCKFLTKNSDGVSMAPLLLMNQDKILMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGKDPRFNKVFNQGMSNHSTITMKKILQTYDGFGGLKTVVDVGGGTGATLNMIISKYPNLKGINFDLPHVVEDAPSYPGVEHVGGDMFVSVPKGDAIFMKWICHDWSDAHCLTFLKNCYKALPKDGKVILAECILPEAPDSKLTTKNVIHIDVIMLAHNPGGKERTEKDFEALGKEAGFKSFNKACCAYNTWVIEYYK [Source organism chain B]=Ligusticum sinense [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Ligusticum sinense [Accession]=MF7000650 [Entry] [Entry number]=835 [Entry name]=LcCOMT with SAM [PDB ID]=7v6j [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A0A0K1YW34 [UniProt boundaries chain A]=12-362 [UniProt coverage chain A]=96% [Name chain A]=Caffeic acid 3-O-methyltransferase [UniProt sequence chain A]=MNTELIPPTFLEDEEEEACMFAMQLSSASVLPMVLKSAIELNLLESIAKAGPGVYVSPSHLAAGLPSSQPDTPVMLDRILRLLASYSVLNCQLRDLPQGRVERLYGLAPVCKFLTKNSDGVSMAPLLLMNQDKILMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGKDPRFNKVFNQGMSNHSTITMKKILQTYDGFGGLKTVVDVGGGTGATLNMIISKYPNLKGINFDLPHVVEDAPSYPGVEHVGGDMFVSVPKGDAIFMKWICHDWSDAHCLTFLKNCYKALPKDGKVILAECILPEAPDSKLTTKNVIHIDVIMLAHNPGGKERTEKDFEALGKEAGFKSFNKACCAYNTWVIEYYK [Source organism chain A]=Ligusticum sinense [UniProt ID chain B]=A0A0K1YW34 [UniProt boundaries chain B]=12-362 [UniProt coverage chain B]=96% [Name chain B]=Caffeic acid 3-O-methyltransferase [UniProt sequence chain B]=MNTELIPPTFLEDEEEEACMFAMQLSSASVLPMVLKSAIELNLLESIAKAGPGVYVSPSHLAAGLPSSQPDTPVMLDRILRLLASYSVLNCQLRDLPQGRVERLYGLAPVCKFLTKNSDGVSMAPLLLMNQDKILMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGKDPRFNKVFNQGMSNHSTITMKKILQTYDGFGGLKTVVDVGGGTGATLNMIISKYPNLKGINFDLPHVVEDAPSYPGVEHVGGDMFVSVPKGDAIFMKWICHDWSDAHCLTFLKNCYKALPKDGKVILAECILPEAPDSKLTTKNVIHIDVIMLAHNPGGKERTEKDFEALGKEAGFKSFNKACCAYNTWVIEYYK [Source organism chain B]=Ligusticum sinense [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Ligusticum sinense [Accession]=MF7000651 [Entry] [Entry number]=836 [Entry name]=MfnG, an L- and D-tyrosine O-methyltransferase with SAH (Streptomyces drozdowiczii) [PDB ID]=7ux6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A0A0D4WTP2 [UniProt boundaries chain A]=8-366 [UniProt coverage chain A]=95% [Name chain A]=MfnG [UniProt sequence chain A]=MTPEGNVSLVDESLLVGVTDEDRAVRSAHQFYERLIGLWAPAVMEAAHELGVFAALAEAPADSGELARRLDCDARAMRVLLDALYAYDVIDRIHDTNGFRYLLSAEARECLLPGTLFSLVGKFMHDINVAWPAWRNLAEVVRHGARDTSGAESPNGIAQEDYESLVGGINFWAPPIVTTLSRKLRASGRSGDATASVLDVGCGTGLYSQLLLREFPRWTATGLDVERIATLANAQALRLGVEERFATRAGDFWRGGWGTGYDLVLFANIFHLQTPASAVRLMRHAAACLAPDGLVAVVDQIVDADREPKTPQDRFALLFAASMTNTGGGDAYTFQEYEEWFTAAGLQRIETLDTPMHRILLARRATEPSAVPEGQ [Source organism chain A]=Streptomyces drozdowiczii [UniProt ID chain B]=A0A0D4WTP2 [UniProt boundaries chain B]=8-366 [UniProt coverage chain B]=95% [Name chain B]=MfnG [UniProt sequence chain B]=MTPEGNVSLVDESLLVGVTDEDRAVRSAHQFYERLIGLWAPAVMEAAHELGVFAALAEAPADSGELARRLDCDARAMRVLLDALYAYDVIDRIHDTNGFRYLLSAEARECLLPGTLFSLVGKFMHDINVAWPAWRNLAEVVRHGARDTSGAESPNGIAQEDYESLVGGINFWAPPIVTTLSRKLRASGRSGDATASVLDVGCGTGLYSQLLLREFPRWTATGLDVERIATLANAQALRLGVEERFATRAGDFWRGGWGTGYDLVLFANIFHLQTPASAVRLMRHAAACLAPDGLVAVVDQIVDADREPKTPQDRFALLFAASMTNTGGGDAYTFQEYEEWFTAAGLQRIETLDTPMHRILLARRATEPSAVPEGQ [Source organism chain B]=Streptomyces drozdowiczii [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=Streptomyces drozdowiczii [Accession]=MF7000652 [Entry] [Entry number]=837 [Entry name]=MfnG, an L- and D-tyrosine O-methyltransferase with SAH(Streptomyces drozdowiczii) [PDB ID]=7ux7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A0A0D4WTP2 [UniProt boundaries chain A]=6-375 [UniProt coverage chain A]=98% [Name chain A]=MfnG [UniProt sequence chain A]=MTPEGNVSLVDESLLVGVTDEDRAVRSAHQFYERLIGLWAPAVMEAAHELGVFAALAEAPADSGELARRLDCDARAMRVLLDALYAYDVIDRIHDTNGFRYLLSAEARECLLPGTLFSLVGKFMHDINVAWPAWRNLAEVVRHGARDTSGAESPNGIAQEDYESLVGGINFWAPPIVTTLSRKLRASGRSGDATASVLDVGCGTGLYSQLLLREFPRWTATGLDVERIATLANAQALRLGVEERFATRAGDFWRGGWGTGYDLVLFANIFHLQTPASAVRLMRHAAACLAPDGLVAVVDQIVDADREPKTPQDRFALLFAASMTNTGGGDAYTFQEYEEWFTAAGLQRIETLDTPMHRILLARRATEPSAVPEGQ [Source organism chain A]=Streptomyces drozdowiczii [UniProt ID chain B]=A0A0D4WTP2 [UniProt boundaries chain B]=6-366 [UniProt coverage chain B]=96% [Name chain B]=MfnG [UniProt sequence chain B]=MTPEGNVSLVDESLLVGVTDEDRAVRSAHQFYERLIGLWAPAVMEAAHELGVFAALAEAPADSGELARRLDCDARAMRVLLDALYAYDVIDRIHDTNGFRYLLSAEARECLLPGTLFSLVGKFMHDINVAWPAWRNLAEVVRHGARDTSGAESPNGIAQEDYESLVGGINFWAPPIVTTLSRKLRASGRSGDATASVLDVGCGTGLYSQLLLREFPRWTATGLDVERIATLANAQALRLGVEERFATRAGDFWRGGWGTGYDLVLFANIFHLQTPASAVRLMRHAAACLAPDGLVAVVDQIVDADREPKTPQDRFALLFAASMTNTGGGDAYTFQEYEEWFTAAGLQRIETLDTPMHRILLARRATEPSAVPEGQ [Source organism chain B]=Streptomyces drozdowiczii [ExpTech]=X-ray [Resolution]=1.14 [Source organism]=Streptomyces drozdowiczii [Accession]=MF7000653 [Entry] [Entry number]=838 [Entry name]=MfnG, an L- and D-tyrosine O-methyltransferase with SAH and L-Tyrosine (Streptomyces drozdowiczii) [PDB ID]=7ux8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A0A0D4WTP2 [UniProt boundaries chain A]=6-375 [UniProt coverage chain A]=98% [Name chain A]=MfnG [UniProt sequence chain A]=MTPEGNVSLVDESLLVGVTDEDRAVRSAHQFYERLIGLWAPAVMEAAHELGVFAALAEAPADSGELARRLDCDARAMRVLLDALYAYDVIDRIHDTNGFRYLLSAEARECLLPGTLFSLVGKFMHDINVAWPAWRNLAEVVRHGARDTSGAESPNGIAQEDYESLVGGINFWAPPIVTTLSRKLRASGRSGDATASVLDVGCGTGLYSQLLLREFPRWTATGLDVERIATLANAQALRLGVEERFATRAGDFWRGGWGTGYDLVLFANIFHLQTPASAVRLMRHAAACLAPDGLVAVVDQIVDADREPKTPQDRFALLFAASMTNTGGGDAYTFQEYEEWFTAAGLQRIETLDTPMHRILLARRATEPSAVPEGQ [Source organism chain A]=Streptomyces drozdowiczii [UniProt ID chain B]=A0A0D4WTP2 [UniProt boundaries chain B]=6-366 [UniProt coverage chain B]=96% [Name chain B]=MfnG [UniProt sequence chain B]=MTPEGNVSLVDESLLVGVTDEDRAVRSAHQFYERLIGLWAPAVMEAAHELGVFAALAEAPADSGELARRLDCDARAMRVLLDALYAYDVIDRIHDTNGFRYLLSAEARECLLPGTLFSLVGKFMHDINVAWPAWRNLAEVVRHGARDTSGAESPNGIAQEDYESLVGGINFWAPPIVTTLSRKLRASGRSGDATASVLDVGCGTGLYSQLLLREFPRWTATGLDVERIATLANAQALRLGVEERFATRAGDFWRGGWGTGYDLVLFANIFHLQTPASAVRLMRHAAACLAPDGLVAVVDQIVDADREPKTPQDRFALLFAASMTNTGGGDAYTFQEYEEWFTAAGLQRIETLDTPMHRILLARRATEPSAVPEGQ [Source organism chain B]=Streptomyces drozdowiczii [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Streptomyces drozdowiczii [Accession]=MF7000654 [Entry] [Entry number]=839 [Entry name]=SbSOMT with pinostilbene and NAD+ [PDB ID]=7war [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain B]=A0A1B6PFV1 [UniProt boundaries chain B]=16-377 [UniProt coverage chain B]=96% [Name chain B]=O-methyltransferase domain-containing protein [UniProt sequence chain B]=MGSYDSSSSSSNDSSARNEEDESCMFALKLLGGFAVPFTIKAVIELGVMDQLLTAERAMSAEELVAAAVAAQLPRPEVACTMVDRLLRFLASHSVVRCTTEVVVGTDDATTTTCCRRSYAASPVCKWFARNGVEDSVLPLGMMILNKTFLDSWQNITDAVLEGAAPFEKTYGMPMFEYLSTNGPLNTVFHEAMANHSMIITKKLLKFFRGFEGLDVLVDVGGGNGTTLQMIRGQYKNMRGINYDLPHVIAQAAPVEGVEHVGGSMFDNIPRGNAVLLKWILHDWDDKACIKILKNCYTALHVRGKVIVLEYVVPDEPEPTLAAQGAFELDLTMLVTFGSGKERTQREFSELAMEAGFSREFKATYIFANVWALEFTK [Source organism chain B]=Sorghum bicolor [UniProt ID chain A]=A0A1B6PFV1 [UniProt boundaries chain A]=15-377 [UniProt coverage chain A]=96% [Name chain A]=O-methyltransferase domain-containing protein [UniProt sequence chain A]=MGSYDSSSSSSNDSSARNEEDESCMFALKLLGGFAVPFTIKAVIELGVMDQLLTAERAMSAEELVAAAVAAQLPRPEVACTMVDRLLRFLASHSVVRCTTEVVVGTDDATTTTCCRRSYAASPVCKWFARNGVEDSVLPLGMMILNKTFLDSWQNITDAVLEGAAPFEKTYGMPMFEYLSTNGPLNTVFHEAMANHSMIITKKLLKFFRGFEGLDVLVDVGGGNGTTLQMIRGQYKNMRGINYDLPHVIAQAAPVEGVEHVGGSMFDNIPRGNAVLLKWILHDWDDKACIKILKNCYTALHVRGKVIVLEYVVPDEPEPTLAAQGAFELDLTMLVTFGSGKERTQREFSELAMEAGFSREFKATYIFANVWALEFTK [Source organism chain A]=Sorghum bicolor [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Sorghum bicolor [Accession]=MF7000655 [Entry] [Entry number]=840 [Entry name]=SbSOMT with resveratrol and NAD+ [PDB ID]=7vb8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain B]=A0A1B6PFV1 [UniProt boundaries chain B]=15-377 [UniProt coverage chain B]=96% [Name chain B]=O-methyltransferase domain-containing protein [UniProt sequence chain B]=MGSYDSSSSSSNDSSARNEEDESCMFALKLLGGFAVPFTIKAVIELGVMDQLLTAERAMSAEELVAAAVAAQLPRPEVACTMVDRLLRFLASHSVVRCTTEVVVGTDDATTTTCCRRSYAASPVCKWFARNGVEDSVLPLGMMILNKTFLDSWQNITDAVLEGAAPFEKTYGMPMFEYLSTNGPLNTVFHEAMANHSMIITKKLLKFFRGFEGLDVLVDVGGGNGTTLQMIRGQYKNMRGINYDLPHVIAQAAPVEGVEHVGGSMFDNIPRGNAVLLKWILHDWDDKACIKILKNCYTALHVRGKVIVLEYVVPDEPEPTLAAQGAFELDLTMLVTFGSGKERTQREFSELAMEAGFSREFKATYIFANVWALEFTK [Source organism chain B]=Sorghum bicolor [UniProt ID chain A]=A0A1B6PFV1 [UniProt boundaries chain A]=15-377 [UniProt coverage chain A]=96% [Name chain A]=O-methyltransferase domain-containing protein [UniProt sequence chain A]=MGSYDSSSSSSNDSSARNEEDESCMFALKLLGGFAVPFTIKAVIELGVMDQLLTAERAMSAEELVAAAVAAQLPRPEVACTMVDRLLRFLASHSVVRCTTEVVVGTDDATTTTCCRRSYAASPVCKWFARNGVEDSVLPLGMMILNKTFLDSWQNITDAVLEGAAPFEKTYGMPMFEYLSTNGPLNTVFHEAMANHSMIITKKLLKFFRGFEGLDVLVDVGGGNGTTLQMIRGQYKNMRGINYDLPHVIAQAAPVEGVEHVGGSMFDNIPRGNAVLLKWILHDWDDKACIKILKNCYTALHVRGKVIVLEYVVPDEPEPTLAAQGAFELDLTMLVTFGSGKERTQREFSELAMEAGFSREFKATYIFANVWALEFTK [Source organism chain A]=Sorghum bicolor [ExpTech]=X-ray [Resolution]=1.72 [Source organism]=Sorghum bicolor [Accession]=MF7000656 [Entry] [Entry number]=841 [Entry name]=SbSOMT with pterostilbene and NAD+ [PDB ID]=7was [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dimeric O-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000636,MF7000637,MF7000638,MF7000639,MF7000640,MF7000641,MF7000642,MF7000643,MF7000644,MF7000645,MF7000646,MF7000647,MF7000648,MF7000649,MF7000650,MF7000651,MF7000652,MF7000653,MF7000654,MF7000655,MF7000656,MF7000657 [UniProt ID chain A]=A0A1B6PFV1 [UniProt boundaries chain A]=15-377 [UniProt coverage chain A]=96% [Name chain A]=O-methyltransferase domain-containing protein [UniProt sequence chain A]=MGSYDSSSSSSNDSSARNEEDESCMFALKLLGGFAVPFTIKAVIELGVMDQLLTAERAMSAEELVAAAVAAQLPRPEVACTMVDRLLRFLASHSVVRCTTEVVVGTDDATTTTCCRRSYAASPVCKWFARNGVEDSVLPLGMMILNKTFLDSWQNITDAVLEGAAPFEKTYGMPMFEYLSTNGPLNTVFHEAMANHSMIITKKLLKFFRGFEGLDVLVDVGGGNGTTLQMIRGQYKNMRGINYDLPHVIAQAAPVEGVEHVGGSMFDNIPRGNAVLLKWILHDWDDKACIKILKNCYTALHVRGKVIVLEYVVPDEPEPTLAAQGAFELDLTMLVTFGSGKERTQREFSELAMEAGFSREFKATYIFANVWALEFTK [Source organism chain A]=Sorghum bicolor [UniProt ID chain B]=A0A1B6PFV1 [UniProt boundaries chain B]=15-377 [UniProt coverage chain B]=96% [Name chain B]=O-methyltransferase domain-containing protein [UniProt sequence chain B]=MGSYDSSSSSSNDSSARNEEDESCMFALKLLGGFAVPFTIKAVIELGVMDQLLTAERAMSAEELVAAAVAAQLPRPEVACTMVDRLLRFLASHSVVRCTTEVVVGTDDATTTTCCRRSYAASPVCKWFARNGVEDSVLPLGMMILNKTFLDSWQNITDAVLEGAAPFEKTYGMPMFEYLSTNGPLNTVFHEAMANHSMIITKKLLKFFRGFEGLDVLVDVGGGNGTTLQMIRGQYKNMRGINYDLPHVIAQAAPVEGVEHVGGSMFDNIPRGNAVLLKWILHDWDDKACIKILKNCYTALHVRGKVIVLEYVVPDEPEPTLAAQGAFELDLTMLVTFGSGKERTQREFSELAMEAGFSREFKATYIFANVWALEFTK [Source organism chain B]=Sorghum bicolor [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Sorghum bicolor [Accession]=MF7000657 [Entry] [Entry number]=842 [Entry name]=Circadian clock modifier, Pex (Cyanobacterium) [PDB ID]=2e1n [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q31QG0 [UniProt boundaries chain A]=1-110 [UniProt coverage chain A]=87% [Name chain A]=Transcriptional regulator, PadR family [UniProt sequence chain A]=MDFEDIYRFFQDPPPHYLSKELAVCYVLAVLRHEDSYGTELIQHLETHWPNYRLSDTVLYTALKFLEDEQIISGYWKKVEGRGRPRRMYQLAQANDDRSRDLAQLWERYLSSSAATDRQLIPVEAR [Source organism chain A]= [UniProt ID chain B]=Q31QG0 [UniProt boundaries chain B]=1-112 [UniProt coverage chain B]=88% [Name chain B]=Transcriptional regulator, PadR family [UniProt sequence chain B]=MDFEDIYRFFQDPPPHYLSKELAVCYVLAVLRHEDSYGTELIQHLETHWPNYRLSDTVLYTALKFLEDEQIISGYWKKVEGRGRPRRMYQLAQANDDRSRDLAQLWERYLSSSAATDRQLIPVEAR [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.80 [Source organism]= [Accession]=MF7000658 [Entry] [Entry number]=843 [Entry name]=PadR-like transcriptional regulator (BCE3449) (Bacillus cereus strain ATCC 10987) [PDB ID]=4esf [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q734F6 [UniProt boundaries chain A]=3-105 [UniProt coverage chain A]=97% [Name chain A]=Transcription regulator PadR N-terminal domain-containing protein [UniProt sequence chain A]=MENLTEMLKGSLEGCVLEIISRRETYGYEITRHLNDLGFTEVVEGTVYTILVRLEKKKLVNIEKKPSDMGPPRKFYSLNEAGRQELELFWKKWDFVSSKINVLKSN [Source organism chain A]=Bacillus cereus [UniProt ID chain A-2]=Q734F6 [UniProt boundaries chain A-2]=3-105 [UniProt coverage chain A-2]=97% [Name chain A-2]=Transcription regulator PadR N-terminal domain-containing protein [UniProt sequence chain A-2]=MENLTEMLKGSLEGCVLEIISRRETYGYEITRHLNDLGFTEVVEGTVYTILVRLEKKKLVNIEKKPSDMGPPRKFYSLNEAGRQELELFWKKWDFVSSKINVLKSN [Source organism chain A-2]=Bacillus cereus [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Bacillus cereus [Accession]=MF7000659 [Entry] [Entry number]=844 [Entry name]=PadR (Bacillus subtilis) [PDB ID]=5x12 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=E0TW95 [UniProt boundaries chain A]=1-182 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MRVLKYAILGLLRKGELSGYDITSYFKEELGQFWSAKHSQIYPELKKLTDEGFITFRTTIQGTKLEKKMYTLTDSGKQELHDWLIRHQPIPETVKDEFMLKAYFISSLSRQEASDLFTDQLLKRKAKLSDLQGSYEKLMASAEPMSFSSPDFGHYLVLTKALEREKNYVSWLESILAMIDED [Source organism chain A]=subtilis subsp spizizenii) [UniProt ID chain A-2]=E0TW95 [UniProt boundaries chain A-2]=1-182 [UniProt coverage chain A-2]=100% [Name chain A-2]=Transcriptional regulator [UniProt sequence chain A-2]=MRVLKYAILGLLRKGELSGYDITSYFKEELGQFWSAKHSQIYPELKKLTDEGFITFRTTIQGTKLEKKMYTLTDSGKQELHDWLIRHQPIPETVKDEFMLKAYFISSLSRQEASDLFTDQLLKRKAKLSDLQGSYEKLMASAEPMSFSSPDFGHYLVLTKALEREKNYVSWLESILAMIDED [Source organism chain A-2]=subtilis subsp spizizenii) [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=subtilis subsp spizizenii) [Accession]=MF7000660 [Entry] [Entry number]=845 [Entry name]=PadR with p-coumaric acid (Bacillus subtilis) [PDB ID]=5x13 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=E0TW95 [UniProt boundaries chain A]=1-182 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MRVLKYAILGLLRKGELSGYDITSYFKEELGQFWSAKHSQIYPELKKLTDEGFITFRTTIQGTKLEKKMYTLTDSGKQELHDWLIRHQPIPETVKDEFMLKAYFISSLSRQEASDLFTDQLLKRKAKLSDLQGSYEKLMASAEPMSFSSPDFGHYLVLTKALEREKNYVSWLESILAMIDED [Source organism chain A]=subtilis subsp spizizenii) [UniProt ID chain A-2]=E0TW95 [UniProt boundaries chain A-2]=1-182 [UniProt coverage chain A-2]=100% [Name chain A-2]=Transcriptional regulator [UniProt sequence chain A-2]=MRVLKYAILGLLRKGELSGYDITSYFKEELGQFWSAKHSQIYPELKKLTDEGFITFRTTIQGTKLEKKMYTLTDSGKQELHDWLIRHQPIPETVKDEFMLKAYFISSLSRQEASDLFTDQLLKRKAKLSDLQGSYEKLMASAEPMSFSSPDFGHYLVLTKALEREKNYVSWLESILAMIDED [Source organism chain A-2]=subtilis subsp spizizenii) [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=subtilis subsp spizizenii) [Accession]=MF7000661 [Entry] [Entry number]=846 [Entry name]=PadR with ferulic acid (Bacillus subtilis) [PDB ID]=5x14 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=E0TW95 [UniProt boundaries chain A]=1-182 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MRVLKYAILGLLRKGELSGYDITSYFKEELGQFWSAKHSQIYPELKKLTDEGFITFRTTIQGTKLEKKMYTLTDSGKQELHDWLIRHQPIPETVKDEFMLKAYFISSLSRQEASDLFTDQLLKRKAKLSDLQGSYEKLMASAEPMSFSSPDFGHYLVLTKALEREKNYVSWLESILAMIDED [Source organism chain A]=subtilis subsp spizizenii) [UniProt ID chain A-2]=E0TW95 [UniProt boundaries chain A-2]=1-182 [UniProt coverage chain A-2]=100% [Name chain A-2]=Transcriptional regulator [UniProt sequence chain A-2]=MRVLKYAILGLLRKGELSGYDITSYFKEELGQFWSAKHSQIYPELKKLTDEGFITFRTTIQGTKLEKKMYTLTDSGKQELHDWLIRHQPIPETVKDEFMLKAYFISSLSRQEASDLFTDQLLKRKAKLSDLQGSYEKLMASAEPMSFSSPDFGHYLVLTKALEREKNYVSWLESILAMIDED [Source organism chain A-2]=subtilis subsp spizizenii) [ExpTech]=X-ray [Resolution]=1.68 [Source organism]=subtilis subsp spizizenii) [Accession]=MF7000662 [Entry] [Entry number]=847 [Entry name]=VanR transcription factor with vanillate [PDB ID]=5z7b [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q8NN31 [UniProt boundaries chain A]=1-192 [UniProt coverage chain A]=100% [Name chain A]=Predicted transcriptional regulators [UniProt sequence chain A]=MTLRSALLALLSSGPLTGYDASQRFGASVGFVWSGSDSQIYPELRKMEAEELLVGSDVPWGSKGATKTEYALSEKGWEALRKAWYEPVTYGPTRDPARLKAAYFEVGTNGDARRHLRAHIAHFEQQKIQSESMIDELKAKTHPTLARRLERSPKKEHERIVAFKVLAYEGQIARAQAEIEWAEKGLKLLDTL [Source organism chain A]=534) [UniProt ID chain B]=Q8NN31 [UniProt boundaries chain B]=1-192 [UniProt coverage chain B]=100% [Name chain B]=Predicted transcriptional regulators [UniProt sequence chain B]=MTLRSALLALLSSGPLTGYDASQRFGASVGFVWSGSDSQIYPELRKMEAEELLVGSDVPWGSKGATKTEYALSEKGWEALRKAWYEPVTYGPTRDPARLKAAYFEVGTNGDARRHLRAHIAHFEQQKIQSESMIDELKAKTHPTLARRLERSPKKEHERIVAFKVLAYEGQIARAQAEIEWAEKGLKLLDTL [Source organism chain B]=534) [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=534) [Accession]=MF7000663 [Entry] [Entry number]=848 [Entry name]=RosR (vng0258) grown from NaCl (Halobacterium salinarum) [PDB ID]=6f5c [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q9HSF4 [UniProt boundaries chain A]=11-116 [UniProt coverage chain A]=91% [Name chain A]=PadR family transcription regulator RosR [UniProt sequence chain A]=MSEAQPDARSDARDLTAFQKNILTVLGEEARYGLAIKRELEEYYGEEVNHGRLYPNLDDLVNKGLVEKSELDKRTNEYALTNEGFDAVVDDLEWTLSKFVADADRRERVETIVADD [Source organism chain A]= [UniProt ID chain B]=Q9HSF4 [UniProt boundaries chain B]=11-116 [UniProt coverage chain B]=91% [Name chain B]=PadR family transcription regulator RosR [UniProt sequence chain B]=MSEAQPDARSDARDLTAFQKNILTVLGEEARYGLAIKRELEEYYGEEVNHGRLYPNLDDLVNKGLVEKSELDKRTNEYALTNEGFDAVVDDLEWTLSKFVADADRRERVETIVADD [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.55 [Source organism]= [Accession]=MF7000664 [Entry] [Entry number]=849 [Entry name]=RosR (vng0258) grown from NaBr (Halobacterium salinarum) [PDB ID]=6ez1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q9HSF4 [UniProt boundaries chain A]=11-116 [UniProt coverage chain A]=91% [Name chain A]=PadR family transcription regulator RosR [UniProt sequence chain A]=MSEAQPDARSDARDLTAFQKNILTVLGEEARYGLAIKRELEEYYGEEVNHGRLYPNLDDLVNKGLVEKSELDKRTNEYALTNEGFDAVVDDLEWTLSKFVADADRRERVETIVADD [Source organism chain A]= [UniProt ID chain B]=Q9HSF4 [UniProt boundaries chain B]=11-116 [UniProt coverage chain B]=91% [Name chain B]=PadR family transcription regulator RosR [UniProt sequence chain B]=MSEAQPDARSDARDLTAFQKNILTVLGEEARYGLAIKRELEEYYGEEVNHGRLYPNLDDLVNKGLVEKSELDKRTNEYALTNEGFDAVVDDLEWTLSKFVADADRRERVETIVADD [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.75 [Source organism]= [Accession]=MF7000665 [Entry] [Entry number]=850 [Entry name]=RosR (vng0258) grown from KBr (Halobacterium salinarum) [PDB ID]=6faq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q9HSF4 [UniProt boundaries chain A]=11-116 [UniProt coverage chain A]=91% [Name chain A]=PadR family transcription regulator RosR [UniProt sequence chain A]=MSEAQPDARSDARDLTAFQKNILTVLGEEARYGLAIKRELEEYYGEEVNHGRLYPNLDDLVNKGLVEKSELDKRTNEYALTNEGFDAVVDDLEWTLSKFVADADRRERVETIVADD [Source organism chain A]= [UniProt ID chain B]=Q9HSF4 [UniProt boundaries chain B]=11-116 [UniProt coverage chain B]=91% [Name chain B]=PadR family transcription regulator RosR [UniProt sequence chain B]=MSEAQPDARSDARDLTAFQKNILTVLGEEARYGLAIKRELEEYYGEEVNHGRLYPNLDDLVNKGLVEKSELDKRTNEYALTNEGFDAVVDDLEWTLSKFVADADRRERVETIVADD [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.95 [Source organism]= [Accession]=MF7000666 [Entry] [Entry number]=851 [Entry name]=RosR (vng0258) grown from KCl (Halobacterium salinarum) [PDB ID]=6fdh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q9HSF4 [UniProt boundaries chain A]=11-116 [UniProt coverage chain A]=91% [Name chain A]=PadR family transcription regulator RosR [UniProt sequence chain A]=MSEAQPDARSDARDLTAFQKNILTVLGEEARYGLAIKRELEEYYGEEVNHGRLYPNLDDLVNKGLVEKSELDKRTNEYALTNEGFDAVVDDLEWTLSKFVADADRRERVETIVADD [Source organism chain A]= [UniProt ID chain B]=Q9HSF4 [UniProt boundaries chain B]=11-116 [UniProt coverage chain B]=91% [Name chain B]=PadR family transcription regulator RosR [UniProt sequence chain B]=MSEAQPDARSDARDLTAFQKNILTVLGEEARYGLAIKRELEEYYGEEVNHGRLYPNLDDLVNKGLVEKSELDKRTNEYALTNEGFDAVVDDLEWTLSKFVADADRRERVETIVADD [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.85 [Source organism]= [Accession]=MF7000667 [Entry] [Entry number]=852 [Entry name]=Transcription factor (Listeria monocytogenes) [PDB ID]=6abq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain B]=L8DXR9 [UniProt boundaries chain B]=3-108 [UniProt coverage chain B]=98% [Name chain B]=PadR family transcriptional regulator [UniProt sequence chain B]=MKGLTELLKGSLEGMILERISRGETYGYEITKYLNDLGFDEIVEGTVYTILVRLEKKGLVEIEKKKSELGPPRKFYTLSPAGEEELAIFWKRWDFIQGKIMQVKGGQA [Source organism chain B]=Listeria monocytogenes [UniProt ID chain A]=L8DXR9 [UniProt boundaries chain A]=1-105 [UniProt coverage chain A]=97% [Name chain A]=PadR family transcriptional regulator [UniProt sequence chain A]=MKGLTELLKGSLEGMILERISRGETYGYEITKYLNDLGFDEIVEGTVYTILVRLEKKGLVEIEKKKSELGPPRKFYTLSPAGEEELAIFWKRWDFIQGKIMQVKGGQA [Source organism chain A]=Listeria monocytogenes [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Listeria monocytogenes [Accession]=MF7000668 [Entry] [Entry number]=853 [Entry name]=VanR with vanillate [PDB ID]=6lg2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=Q8NN31 [UniProt boundaries chain A]=1-192 [UniProt coverage chain A]=100% [Name chain A]=Predicted transcriptional regulators [UniProt sequence chain A]=MTLRSALLALLSSGPLTGYDASQRFGASVGFVWSGSDSQIYPELRKMEAEELLVGSDVPWGSKGATKTEYALSEKGWEALRKAWYEPVTYGPTRDPARLKAAYFEVGTNGDARRHLRAHIAHFEQQKIQSESMIDELKAKTHPTLARRLERSPKKEHERIVAFKVLAYEGQIARAQAEIEWAEKGLKLLDTL [Source organism chain A]=534) [UniProt ID chain B]=Q8NN31 [UniProt boundaries chain B]=1-192 [UniProt coverage chain B]=100% [Name chain B]=Predicted transcriptional regulators [UniProt sequence chain B]=MTLRSALLALLSSGPLTGYDASQRFGASVGFVWSGSDSQIYPELRKMEAEELLVGSDVPWGSKGATKTEYALSEKGWEALRKAWYEPVTYGPTRDPARLKAAYFEVGTNGDARRHLRAHIAHFEQQKIQSESMIDELKAKTHPTLARRLERSPKKEHERIVAFKVLAYEGQIARAQAEIEWAEKGLKLLDTL [Source organism chain B]=534) [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=534) [Accession]=MF7000669 [Entry] [Entry number]=854 [Entry name]=Streptococcus transcriptional regulator [PDB ID]=5zqh [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (PadR family) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000139,MF7000658,MF7000659,MF7000313,MF7000315,MF7000660,MF7000661,MF7000662,MF7000663,MF7000664,MF7000665,MF7000666,MF7000667,MF7000316,MF7000317,MF7000318,MF7000668,MF7000398,MF7000669,MF7000670,MF7000314 [UniProt ID chain A]=A0A229FJD3 [UniProt boundaries chain A]=4-105 [UniProt coverage chain A]=95% [Name chain A]=PadR family transcriptional regulator [UniProt sequence chain A]=MMKETQLLKGVLEGCVLDMIGQKERYGYELVQTLREAGFDTIVPGTIYPLLQKLEKNQWIRGDMRPSPDGPDRKYFSLMKEGEERVSVFWQQWDDLSQKVEGIKNGG [Source organism chain A]=Streptococcus pneumoniae [UniProt ID chain A-2]=A0A229FJD3 [UniProt boundaries chain A-2]=4-105 [UniProt coverage chain A-2]=95% [Name chain A-2]=PadR family transcriptional regulator [UniProt sequence chain A-2]=MMKETQLLKGVLEGCVLDMIGQKERYGYELVQTLREAGFDTIVPGTIYPLLQKLEKNQWIRGDMRPSPDGPDRKYFSLMKEGEERVSVFWQQWDDLSQKVEGIKNGG [Source organism chain A-2]=Streptococcus pneumoniae [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Streptococcus pneumoniae [Accession]=MF7000670 [Entry] [Entry number]=855 [Entry name]=Human TGF-B1 [PDB ID]=1kla [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P01137 [UniProt boundaries chain A]=279-390 [UniProt coverage chain A]=28% [Name chain A]=Transforming growth factor beta-1 proprotein [UniProt sequence chain A]=MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P01137 [UniProt boundaries chain B]=279-390 [UniProt coverage chain B]=28% [Name chain B]=Transforming growth factor beta-1 proprotein [UniProt sequence chain B]=MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000671 [Entry] [Entry number]=856 [Entry name]=Human TGF-B1 [PDB ID]=1klc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P01137 [UniProt boundaries chain A]=279-390 [UniProt coverage chain A]=28% [Name chain A]=Transforming growth factor beta-1 proprotein [UniProt sequence chain A]=MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P01137 [UniProt boundaries chain B]=279-390 [UniProt coverage chain B]=28% [Name chain B]=Transforming growth factor beta-1 proprotein [UniProt sequence chain B]=MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000672 [Entry] [Entry number]=857 [Entry name]=Human TGF-B1 [PDB ID]=1kld [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P01137 [UniProt boundaries chain A]=279-390 [UniProt coverage chain A]=28% [Name chain A]=Transforming growth factor beta-1 proprotein [UniProt sequence chain A]=MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P01137 [UniProt boundaries chain B]=279-390 [UniProt coverage chain B]=28% [Name chain B]=Transforming growth factor beta-1 proprotein [UniProt sequence chain B]=MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000673 [Entry] [Entry number]=858 [Entry name]=Human TGF-B3 [PDB ID]=1tgj [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P10600 [UniProt boundaries chain A]=301-412 [UniProt coverage chain A]=27% [Name chain A]=Transforming growth factor beta-3 proprotein [UniProt sequence chain A]=MKMHLQRALVVLALLNFATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNRTNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P10600 [UniProt boundaries chain A-2]=301-412 [UniProt coverage chain A-2]=27% [Name chain A-2]=Transforming growth factor beta-3 proprotein [UniProt sequence chain A-2]=MKMHLQRALVVLALLNFATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNRTNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000674 [Entry] [Entry number]=859 [Entry name]=Human TGF-B3 [PDB ID]=1tgk [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P10600 [UniProt boundaries chain A]=301-412 [UniProt coverage chain A]=27% [Name chain A]=Transforming growth factor beta-3 proprotein [UniProt sequence chain A]=MKMHLQRALVVLALLNFATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNRTNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P10600 [UniProt boundaries chain A-2]=301-412 [UniProt coverage chain A-2]=27% [Name chain A-2]=Transforming growth factor beta-3 proprotein [UniProt sequence chain A-2]=MKMHLQRALVVLALLNFATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNRTNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.30 [Source organism]=Homo sapiens [Accession]=MF7000675 [Entry] [Entry number]=860 [Entry name]=BMP9 [PDB ID]=1zkz [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=Q9UK05 [UniProt boundaries chain A]=323-429 [UniProt coverage chain A]=24% [Name chain A]=Growth/differentiation factor 2 [UniProt sequence chain A]=MCPGALWVALPLLSLLAGSLQGKPLQSWGRGSAGGNAHSPLGVPGGGLPEHTFNLKMFLENVKVDFLRSLNLSGVPSQDKTRVEPPQYMIDLYNRYTSDKSTTPASNIVRSFSMEDAISITATEDFPFQKHILLFNISIPRHEQITRAELRLYVSCQNHVDPSHDLKGSVVIYDVLDGTDAWDSATETKTFLVSQDIQDEGWETLEVSSAVKRWVRSDSTKSKNKLEVTVESHRKGCDTLDISVPPGSRNLPFFVVFSNDHSSGTKETRLELREMISHEQESVLKKLSKDGSTEAGESSHEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q9UK05 [UniProt boundaries chain A-2]=323-429 [UniProt coverage chain A-2]=24% [Name chain A-2]=Growth/differentiation factor 2 [UniProt sequence chain A-2]=MCPGALWVALPLLSLLAGSLQGKPLQSWGRGSAGGNAHSPLGVPGGGLPEHTFNLKMFLENVKVDFLRSLNLSGVPSQDKTRVEPPQYMIDLYNRYTSDKSTTPASNIVRSFSMEDAISITATEDFPFQKHILLFNISIPRHEQITRAELRLYVSCQNHVDPSHDLKGSVVIYDVLDGTDAWDSATETKTFLVSQDIQDEGWETLEVSSAVKRWVRSDSTKSKNKLEVTVESHRKGCDTLDISVPPGSRNLPFFVVFSNDHSSGTKETRLELREMISHEQESVLKKLSKDGSTEAGESSHEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.33 [Source organism]=Homo sapiens [Accession]=MF7000676 [Entry] [Entry number]=861 [Entry name]=Human artemin (ARTN) [PDB ID]=2ask [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=Q5T4W7 [UniProt boundaries chain A]=120-220 [UniProt coverage chain A]=45% [Name chain A]=Artemin [UniProt sequence chain A]=MELGLGGLSTLSHCPWPRQQPALWPTLAALALLSSVAEASLGSAPRSPAPREGPPPVLASPAGHLPGGRTARWCSGRARRPPPQPSRPAPPPPAPPSALPRGGRAARAGGPGSRARAAGARGCRLRSQLVPVRALGLGHRSDELVRFRFCSGSCRRARSPHDLSLASLLGAGALRPPPGSRPVSQPCCRPTRYEAVSFMDVNSTWRTVDRLSATACGCLG [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q5T4W7 [UniProt boundaries chain B]=120-220 [UniProt coverage chain B]=45% [Name chain B]=Artemin [UniProt sequence chain B]=MELGLGGLSTLSHCPWPRQQPALWPTLAALALLSSVAEASLGSAPRSPAPREGPPPVLASPAGHLPGGRTARWCSGRARRPPPQPSRPAPPPPAPPSALPRGGRAARAGGPGSRARAAGARGCRLRSQLVPVRALGLGHRSDELVRFRFCSGSCRRARSPHDLSLASLLGAGALRPPPGSRPVSQPCCRPTRYEAVSFMDVNSTWRTVDRLSATACGCLG [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.55 [Source organism]=Homo sapiens [Accession]=MF7000677 [Entry] [Entry number]=862 [Entry name]=Human artemin (ARTN) [PDB ID]=2gyz [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=Q5T4W7 [UniProt boundaries chain A]=122-218 [UniProt coverage chain A]=44% [Name chain A]=Artemin [UniProt sequence chain A]=MELGLGGLSTLSHCPWPRQQPALWPTLAALALLSSVAEASLGSAPRSPAPREGPPPVLASPAGHLPGGRTARWCSGRARRPPPQPSRPAPPPPAPPSALPRGGRAARAGGPGSRARAAGARGCRLRSQLVPVRALGLGHRSDELVRFRFCSGSCRRARSPHDLSLASLLGAGALRPPPGSRPVSQPCCRPTRYEAVSFMDVNSTWRTVDRLSATACGCLG [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q5T4W7 [UniProt boundaries chain A-2]=122-218 [UniProt coverage chain A-2]=44% [Name chain A-2]=Artemin [UniProt sequence chain A-2]=MELGLGGLSTLSHCPWPRQQPALWPTLAALALLSSVAEASLGSAPRSPAPREGPPPVLASPAGHLPGGRTARWCSGRARRPPPQPSRPAPPPPAPPSALPRGGRAARAGGPGSRARAAGARGCRLRSQLVPVRALGLGHRSDELVRFRFCSGSCRRARSPHDLSLASLLGAGALRPPPGSRPVSQPCCRPTRYEAVSFMDVNSTWRTVDRLSATACGCLG [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.76 [Source organism]=Homo sapiens [Accession]=MF7000678 [Entry] [Entry number]=863 [Entry name]=Bone morphogenetic protein-3 (BMP-3) [PDB ID]=2qcq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P12645 [UniProt boundaries chain A]=366-472 [UniProt coverage chain A]=22% [Name chain A]=Bone morphogenetic protein 3 [UniProt sequence chain A]=MAGASRLLFLWLGCFCVSLAQGERPKPPFPELRKAVPGDRTAGGGPDSELQPQDKVSEHMLRLYDRYSTVQAARTPGSLEGGSQPWRPRLLREGNTVRSFRAAAAETLERKGLYIFNLTSLTKSENILSATLYFCIGELGNISLSCPVSGGCSHHAQRKHIQIDLSAWTLKFSRNQSQLLGHLSVDMAKSHRDIMSWLSKDITQLLRKAKENEEFLIGFNITSKGRQLPKRRLPFPEPYILVYANDAAISEPESVVSSLQGHRNFPTGTVPKWDSHIRAALSIERRKKRSTGVLLPLQNNELPGAEYQYKKDEVWEERKPYKTLQAQAPEKSKNKKKQRKGPHRKSQTLQFDEQTLKKARRKQWIEPRNCARRYLKVDFADIGWSEWIISPKSFDAYYCSGACQFPMPKSLKPSNHATIQSIVRAVGVVPGIPEPCCVPEKMSSLSILFFDENKNVVLKVYPNMTVESCACR [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P12645 [UniProt boundaries chain B]=365-472 [UniProt coverage chain B]=22% [Name chain B]=Bone morphogenetic protein 3 [UniProt sequence chain B]=MAGASRLLFLWLGCFCVSLAQGERPKPPFPELRKAVPGDRTAGGGPDSELQPQDKVSEHMLRLYDRYSTVQAARTPGSLEGGSQPWRPRLLREGNTVRSFRAAAAETLERKGLYIFNLTSLTKSENILSATLYFCIGELGNISLSCPVSGGCSHHAQRKHIQIDLSAWTLKFSRNQSQLLGHLSVDMAKSHRDIMSWLSKDITQLLRKAKENEEFLIGFNITSKGRQLPKRRLPFPEPYILVYANDAAISEPESVVSSLQGHRNFPTGTVPKWDSHIRAALSIERRKKRSTGVLLPLQNNELPGAEYQYKKDEVWEERKPYKTLQAQAPEKSKNKKKQRKGPHRKSQTLQFDEQTLKKARRKQWIEPRNCARRYLKVDFADIGWSEWIISPKSFDAYYCSGACQFPMPKSLKPSNHATIQSIVRAVGVVPGIPEPCCVPEKMSSLSILFFDENKNVVLKVYPNMTVESCACR [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.21 [Source organism]=Homo sapiens [Accession]=MF7000679 [Entry] [Entry number]=864 [Entry name]=Bone morphogenetic protein-6 (BMP-6) [PDB ID]=2qcw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P22004 [UniProt boundaries chain A]=410-513 [UniProt coverage chain A]=20% [Name chain A]=Bone morphogenetic protein 6 [UniProt sequence chain A]=MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P22004 [UniProt boundaries chain B]=410-513 [UniProt coverage chain B]=20% [Name chain B]=Bone morphogenetic protein 6 [UniProt sequence chain B]=MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.49 [Source organism]=Homo sapiens [Accession]=MF7000680 [Entry] [Entry number]=865 [Entry name]=Bone morphogenetic protein-6 variant B2 (B2-BMP-6) [PDB ID]=2r53 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P22004 [UniProt boundaries chain A]=406-513 [UniProt coverage chain A]=21% [Name chain A]=Bone morphogenetic protein 6 [UniProt sequence chain A]=MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P22004 [UniProt boundaries chain B]=406-513 [UniProt coverage chain B]=21% [Name chain B]=Bone morphogenetic protein 6 [UniProt sequence chain B]=MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Homo sapiens [Accession]=MF7000681 [Entry] [Entry number]=866 [Entry name]=Bone morphogenetic protein-6 (BMP-6) [PDB ID]=2r52 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=P22004 [UniProt boundaries chain A]=409-513 [UniProt coverage chain A]=20% [Name chain A]=Bone morphogenetic protein 6 [UniProt sequence chain A]=MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P22004 [UniProt boundaries chain B]=409-513 [UniProt coverage chain B]=20% [Name chain B]=Bone morphogenetic protein 6 [UniProt sequence chain B]=MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Homo sapiens [Accession]=MF7000682 [Entry] [Entry number]=867 [Entry name]=Bone morphogenetic protein-9 (BMP9) [PDB ID]=4mpl [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=Q9UK05 [UniProt boundaries chain A]=323-429 [UniProt coverage chain A]=24% [Name chain A]=Growth/differentiation factor 2 [UniProt sequence chain A]=MCPGALWVALPLLSLLAGSLQGKPLQSWGRGSAGGNAHSPLGVPGGGLPEHTFNLKMFLENVKVDFLRSLNLSGVPSQDKTRVEPPQYMIDLYNRYTSDKSTTPASNIVRSFSMEDAISITATEDFPFQKHILLFNISIPRHEQITRAELRLYVSCQNHVDPSHDLKGSVVIYDVLDGTDAWDSATETKTFLVSQDIQDEGWETLEVSSAVKRWVRSDSTKSKNKLEVTVESHRKGCDTLDISVPPGSRNLPFFVVFSNDHSSGTKETRLELREMISHEQESVLKKLSKDGSTEAGESSHEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q9UK05 [UniProt boundaries chain A-2]=323-429 [UniProt coverage chain A-2]=24% [Name chain A-2]=Growth/differentiation factor 2 [UniProt sequence chain A-2]=MCPGALWVALPLLSLLAGSLQGKPLQSWGRGSAGGNAHSPLGVPGGGLPEHTFNLKMFLENVKVDFLRSLNLSGVPSQDKTRVEPPQYMIDLYNRYTSDKSTTPASNIVRSFSMEDAISITATEDFPFQKHILLFNISIPRHEQITRAELRLYVSCQNHVDPSHDLKGSVVIYDVLDGTDAWDSATETKTFLVSQDIQDEGWETLEVSSAVKRWVRSDSTKSKNKLEVTVESHRKGCDTLDISVPPGSRNLPFFVVFSNDHSSGTKETRLELREMISHEQESVLKKLSKDGSTEAGESSHEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Homo sapiens [Accession]=MF7000683 [Entry] [Entry number]=868 [Entry name]=Human growth differentiation factor 11 (GDF-11) [PDB ID]=5e4g [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=O95390 [UniProt boundaries chain A]=300-407 [UniProt coverage chain A]=26% [Name chain A]=Growth/differentiation factor 11 [UniProt sequence chain A]=MVLAAPLLLGFLLLALELRPRGEAAEGPAAAAAAAAAAAAAGVGGERSSRPAPSVAPEPDGCPVCVWRQHSRELRLESIKSQILSKLRLKEAPNISREVVKQLLPKAPPLQQILDLHDFQGDALQPEDFLEEDEYHATTETVISMAQETDPAVQTDGSPLCCHFHFSPKVMFTKVLKAQLWVYLRPVPRPATVYLQILRLKPLTGEGTAGGGGGGRRHIRIRSLKIELHSRSGHWQSIDFKQVLHSWFRQPQSNWGIEINAFDPSGTDLAVTSLGPGAEGLHPFMELRVLENTKRSRRNLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=O95390 [UniProt boundaries chain A-2]=300-407 [UniProt coverage chain A-2]=26% [Name chain A-2]=Growth/differentiation factor 11 [UniProt sequence chain A-2]=MVLAAPLLLGFLLLALELRPRGEAAEGPAAAAAAAAAAAAAGVGGERSSRPAPSVAPEPDGCPVCVWRQHSRELRLESIKSQILSKLRLKEAPNISREVVKQLLPKAPPLQQILDLHDFQGDALQPEDFLEEDEYHATTETVISMAQETDPAVQTDGSPLCCHFHFSPKVMFTKVLKAQLWVYLRPVPRPATVYLQILRLKPLTGEGTAGGGGGGRRHIRIRSLKIELHSRSGHWQSIDFKQVLHSWFRQPQSNWGIEINAFDPSGTDLAVTSLGPGAEGLHPFMELRVLENTKRSRRNLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Homo sapiens [Accession]=MF7000684 [Entry] [Entry number]=869 [Entry name]=Bone morhogenetic protein-9 (BMP9) (human) [PDB ID]=5i05 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain A]=Q9UK05 [UniProt boundaries chain A]=323-429 [UniProt coverage chain A]=24% [Name chain A]=Growth/differentiation factor 2 [UniProt sequence chain A]=MCPGALWVALPLLSLLAGSLQGKPLQSWGRGSAGGNAHSPLGVPGGGLPEHTFNLKMFLENVKVDFLRSLNLSGVPSQDKTRVEPPQYMIDLYNRYTSDKSTTPASNIVRSFSMEDAISITATEDFPFQKHILLFNISIPRHEQITRAELRLYVSCQNHVDPSHDLKGSVVIYDVLDGTDAWDSATETKTFLVSQDIQDEGWETLEVSSAVKRWVRSDSTKSKNKLEVTVESHRKGCDTLDISVPPGSRNLPFFVVFSNDHSSGTKETRLELREMISHEQESVLKKLSKDGSTEAGESSHEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q9UK05 [UniProt boundaries chain A-2]=323-429 [UniProt coverage chain A-2]=24% [Name chain A-2]=Growth/differentiation factor 2 [UniProt sequence chain A-2]=MCPGALWVALPLLSLLAGSLQGKPLQSWGRGSAGGNAHSPLGVPGGGLPEHTFNLKMFLENVKVDFLRSLNLSGVPSQDKTRVEPPQYMIDLYNRYTSDKSTTPASNIVRSFSMEDAISITATEDFPFQKHILLFNISIPRHEQITRAELRLYVSCQNHVDPSHDLKGSVVIYDVLDGTDAWDSATETKTFLVSQDIQDEGWETLEVSSAVKRWVRSDSTKSKNKLEVTVESHRKGCDTLDISVPPGSRNLPFFVVFSNDHSSGTKETRLELREMISHEQESVLKKLSKDGSTEAGESSHEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.87 [Source organism]=Homo sapiens [Accession]=MF7000685 [Entry] [Entry number]=870 [Entry name]=Bone morphogenetic protein-6 (BMP-6) (human) [PDB ID]=6omo [Chains]=I,J [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=TGFb-like [Sequence domain]=Cystine-knot cytokine/TGFb-like [Evidence level]=Direct evidence [Evidence text]=The two monomers of the TGF-1 homodimer display indistinguishable 1 H, 13C, and 15N chemical shifts, so in solution the protein is symmetric on the chemical shift time scale (microsecond to millisecond) (PMID:8679613). Reversible disassociation of the monomers cannot be done with significant recovery of TGF-1 due to the presence of a disulfide bond linking Cys77 in the two monomers (PMID:8679613). Two-state unfolding from dimers to unfolded monomers was proved experimentally for other Cystine-knot cytokines with a very similar fold (e.g. for VEGFR1D2) (PMID:34689403). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain I]=N/A [Evidence chain J]=N/A [Similar structures]=MF7000671,MF7000672,MF7000673,MF7000674,MF7000675,MF7000676,MF7000677,MF7000678,MF7000679,MF7000680,MF7000681,MF7000682,MF7000683,MF7000684,MF7000685,MF7000123,MF7000122,MF7000686,MF7000121 [UniProt ID chain I]=P22004 [UniProt boundaries chain I]=410-513 [UniProt coverage chain I]=20% [Name chain I]=Bone morphogenetic protein 6 [UniProt sequence chain I]=MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH [Source organism chain I]=Homo sapiens [UniProt ID chain J]=P22004 [UniProt boundaries chain J]=410-513 [UniProt coverage chain J]=20% [Name chain J]=Bone morphogenetic protein 6 [UniProt sequence chain J]=MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH [Source organism chain J]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Homo sapiens [Accession]=MF7000686 [Entry] [Entry number]=871 [Entry name]=EFC domain of Cdc42-interacting protein 4 [PDB ID]=2efk [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q15642 [UniProt boundaries chain A]=10-288 [UniProt coverage chain A]=46% [Name chain A]=Cdc42-interacting protein 4 [UniProt sequence chain A]=MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q15642 [UniProt boundaries chain A-2]=10-288 [UniProt coverage chain A-2]=46% [Name chain A-2]=Cdc42-interacting protein 4 [UniProt sequence chain A-2]=MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Homo sapiens [Accession]=MF7000687 [Entry] [Entry number]=872 [Entry name]=EFC domain of formin-binding protein 17 [PDB ID]=2efl [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q96RU3 [UniProt boundaries chain A]=1-288 [UniProt coverage chain A]=46% [Name chain A]=Formin-binding protein 1 [UniProt sequence chain A]=MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKDS [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q96RU3 [UniProt boundaries chain A-2]=1-288 [UniProt coverage chain A-2]=46% [Name chain A-2]=Formin-binding protein 1 [UniProt sequence chain A-2]=MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKDS [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.61 [Source organism]=Homo sapiens [Accession]=MF7000688 [Entry] [Entry number]=873 [Entry name]=Human PACSIN1 F-BAR domain (C2 lattice) [PDB ID]=3hah [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q9BY11 [UniProt boundaries chain A]=16-304 [UniProt coverage chain A]=65% [Name chain A]=Protein kinase C and casein kinase substrate in neurons protein 1 [UniProt sequence chain A]=MSSSYDEASLAPEETTDSFWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAENSSYIHVYRELEQAIRGADAQEDLRWFRSTSGPGMPMNWPQFEEWNPDLPHTTTKKEKQPKKAEGVALTNATGAVESTSQAGDRGSVSSYDRGQPYATEWSDDESGNPFGGSETNGGANPFEDDSKGVRVRALYDYDGQEQDELSFKAGDELTKLGEEDEQGWCRGRLDSGQLGLYPANYVEAI [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9BY11 [UniProt boundaries chain B]=16-305 [UniProt coverage chain B]=65% [Name chain B]=Protein kinase C and casein kinase substrate in neurons protein 1 [UniProt sequence chain B]=MSSSYDEASLAPEETTDSFWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAENSSYIHVYRELEQAIRGADAQEDLRWFRSTSGPGMPMNWPQFEEWNPDLPHTTTKKEKQPKKAEGVALTNATGAVESTSQAGDRGSVSSYDRGQPYATEWSDDESGNPFGGSETNGGANPFEDDSKGVRVRALYDYDGQEQDELSFKAGDELTKLGEEDEQGWCRGRLDSGQLGLYPANYVEAI [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.77 [Source organism]=Homo sapiens [Accession]=MF7000689 [Entry] [Entry number]=874 [Entry name]=Human PACSIN2 F-BAR domain (p212121 lattice) [PDB ID]=3haj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q9UNF0 [UniProt boundaries chain A]=16-301 [UniProt coverage chain A]=58% [Name chain A]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain A]=MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCSDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAFMSEAERVSELHLEVKASLMNDDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHAACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKEKYEKSLKELDQGTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVAGYKAIYHDLEQSIRAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKATDGVTLTGINQTGDQSLPSKPSSTLNVPSNPAQSAQSQSSYNPFEDEDDTGSTVSEKDDTKAKNVSSYEKTQSYPTDWSDDESNNPFSSTDANGDSNPFDDDATSGTEVRVRALYDYEGQEHDELSFKAGDELTKMEDEDEQGWCKGRLDNGQVGLYPANYVEAIQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9UNF0 [UniProt boundaries chain B]=16-299 [UniProt coverage chain B]=58% [Name chain B]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain B]=MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCSDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAFMSEAERVSELHLEVKASLMNDDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHAACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKEKYEKSLKELDQGTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVAGYKAIYHDLEQSIRAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKATDGVTLTGINQTGDQSLPSKPSSTLNVPSNPAQSAQSQSSYNPFEDEDDTGSTVSEKDDTKAKNVSSYEKTQSYPTDWSDDESNNPFSSTDANGDSNPFDDDATSGTEVRVRALYDYEGQEHDELSFKAGDELTKMEDEDEQGWCKGRLDNGQVGLYPANYVEAIQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.78 [Source organism]=Homo sapiens [Accession]=MF7000690 [Entry] [Entry number]=875 [Entry name]=EFC/F-BAR domain (Drosophila Syndapin/PACSIN) [PDB ID]=3i2w [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q9VDI1 [UniProt boundaries chain A]=14-303 [UniProt coverage chain A]=58% [Name chain A]=LD46328p [UniProt sequence chain A]=MSHHSDDQLLQAGSDSFWEPGNYKRTTKRIEDGYKLCNDLQQLIQERADIEKGYAKSLRTWSKKWGELIEKGPEYGTTEAAWKGVLTESERISDVHMKIKDNLCNDVNSQIKTWQKENYHHTLMQIKERKDLEDLFKKAQKPWAKLLAKVEKAKADYHSACKTERSATNQERNANADSSLSPDQVKKMHDRVQKTKDQVQKCREKYEQAIAEITKYNSVYIEDMTSVFEKCQTFEKTRLQFFKEILFNVHSCLDLTKVQSLPQIYEEFSHTINNADQQKDLKWWSNNHGINMAMNWPSFVEYTEEFRDIAKGNKSKEALPAAPITLINQRPVAEDVHEYPQTNSLKKNTSTLSSVSSRASVKSEIATTQSSVTTSEAKTSAAVAGAATATAAATAASAASNRNSSVTNGNGKVDANPFDEEEEWDESDNVLVDNGEPGVPVKALYDYEGAESDELTFKQGDVFEKLEDEDEQGWCKGRMNGRVGLYPANYVETA [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=Q9VDI1 [UniProt boundaries chain B]=14-298 [UniProt coverage chain B]=57% [Name chain B]=LD46328p [UniProt sequence chain B]=MSHHSDDQLLQAGSDSFWEPGNYKRTTKRIEDGYKLCNDLQQLIQERADIEKGYAKSLRTWSKKWGELIEKGPEYGTTEAAWKGVLTESERISDVHMKIKDNLCNDVNSQIKTWQKENYHHTLMQIKERKDLEDLFKKAQKPWAKLLAKVEKAKADYHSACKTERSATNQERNANADSSLSPDQVKKMHDRVQKTKDQVQKCREKYEQAIAEITKYNSVYIEDMTSVFEKCQTFEKTRLQFFKEILFNVHSCLDLTKVQSLPQIYEEFSHTINNADQQKDLKWWSNNHGINMAMNWPSFVEYTEEFRDIAKGNKSKEALPAAPITLINQRPVAEDVHEYPQTNSLKKNTSTLSSVSSRASVKSEIATTQSSVTTSEAKTSAAVAGAATATAAATAASAASNRNSSVTNGNGKVDANPFDEEEEWDESDNVLVDNGEPGVPVKALYDYEGAESDELTFKQGDVFEKLEDEDEQGWCKGRMNGRVGLYPANYVETA [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=2.67 [Source organism]=Drosophila melanogaster [Accession]=MF7000691 [Entry] [Entry number]=876 [Entry name]=EFC/F-BAR domain of human PACSIN2/Syndapin II [PDB ID]=3abh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q9UNF0 [UniProt boundaries chain A]=16-303 [UniProt coverage chain A]=59% [Name chain A]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain A]=MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCSDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAFMSEAERVSELHLEVKASLMNDDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHAACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKEKYEKSLKELDQGTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVAGYKAIYHDLEQSIRAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKATDGVTLTGINQTGDQSLPSKPSSTLNVPSNPAQSAQSQSSYNPFEDEDDTGSTVSEKDDTKAKNVSSYEKTQSYPTDWSDDESNNPFSSTDANGDSNPFDDDATSGTEVRVRALYDYEGQEHDELSFKAGDELTKMEDEDEQGWCKGRLDNGQVGLYPANYVEAIQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9UNF0 [UniProt boundaries chain B]=16-303 [UniProt coverage chain B]=59% [Name chain B]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain B]=MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCSDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAFMSEAERVSELHLEVKASLMNDDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHAACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKEKYEKSLKELDQGTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVAGYKAIYHDLEQSIRAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKATDGVTLTGINQTGDQSLPSKPSSTLNVPSNPAQSAQSQSSYNPFEDEDDTGSTVSEKDDTKAKNVSSYEKTQSYPTDWSDDESNNPFSSTDANGDSNPFDDDATSGTEVRVRALYDYEGQEHDELSFKAGDELTKMEDEDEQGWCKGRLDNGQVGLYPANYVEAIQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000692 [Entry] [Entry number]=877 [Entry name]=EFC/F-BAR domain of human PACSIN2/Syndapin II [PDB ID]=3aco [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q9UNF0 [UniProt boundaries chain A]=16-299 [UniProt coverage chain A]=58% [Name chain A]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain A]=MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCSDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAFMSEAERVSELHLEVKASLMNDDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHAACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKEKYEKSLKELDQGTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVAGYKAIYHDLEQSIRAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKATDGVTLTGINQTGDQSLPSKPSSTLNVPSNPAQSAQSQSSYNPFEDEDDTGSTVSEKDDTKAKNVSSYEKTQSYPTDWSDDESNNPFSSTDANGDSNPFDDDATSGTEVRVRALYDYEGQEHDELSFKAGDELTKMEDEDEQGWCKGRLDNGQVGLYPANYVEAIQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9UNF0 [UniProt boundaries chain B]=16-299 [UniProt coverage chain B]=58% [Name chain B]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain B]=MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCSDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAFMSEAERVSELHLEVKASLMNDDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHAACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKEKYEKSLKELDQGTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVAGYKAIYHDLEQSIRAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKATDGVTLTGINQTGDQSLPSKPSSTLNVPSNPAQSAQSQSSYNPFEDEDDTGSTVSEKDDTKAKNVSSYEKTQSYPTDWSDDESNNPFSSTDANGDSNPFDDDATSGTEVRVRALYDYEGQEHDELSFKAGDELTKMEDEDEQGWCKGRLDNGQVGLYPANYVEAIQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Homo sapiens [Accession]=MF7000693 [Entry] [Entry number]=878 [Entry name]=Mouse PACSIN2 F-BAR domain [PDB ID]=3lll [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q9WVE8 [UniProt boundaries chain A]=16-302 [UniProt coverage chain A]=59% [Name chain A]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain A]=MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCGDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWIAVMSEAERVSELHLEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHTACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKDKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKTIYRELEQSIKAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKAVDGVTLTGINQTGDQSGQNKPGSNLSVPSNPAQSTQLQSSYNPFEDEDDTGSSISEKEDIKAKNVSSYEKTQTYPTDWSDDESNNPFSSTDANGDSNPFDEDTTSGTEVRVRALYDYEGQEHDELSFKAGDELTKIEDEDEQGWCKGRLDSGQVGLYPANYVEAIQ [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9WVE8 [UniProt boundaries chain B]=16-302 [UniProt coverage chain B]=59% [Name chain B]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain B]=MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCGDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWIAVMSEAERVSELHLEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHTACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKDKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKTIYRELEQSIKAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKAVDGVTLTGINQTGDQSGQNKPGSNLSVPSNPAQSTQLQSSYNPFEDEDDTGSSISEKEDIKAKNVSSYEKTQTYPTDWSDDESNNPFSSTDANGDSNPFDEDTTSGTEVRVRALYDYEGQEHDELSFKAGDELTKIEDEDEQGWCKGRLDSGQVGLYPANYVEAIQ [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=3.30 [Source organism]=Mus musculus [Accession]=MF7000694 [Entry] [Entry number]=879 [Entry name]=Mouse PACSIN3 BAR domain, mutant [PDB ID]=3m3w [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q99JB8 [UniProt boundaries chain A]=14-301 [UniProt coverage chain A]=67% [Name chain A]=Protein kinase C and casein kinase II substrate protein 3 [UniProt sequence chain A]=MAPEEDAGGEVLGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGAVEKGPQYGTLEKAWHAFFTAAERLSELHLEVREKLHGPDSERVRTWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHTARKDEKTAQTRESHAKADSSMSQEQLRKLQERVGRCTKEAEKMKTQYEQTLAELNRYTPRYMEDMEQAFESCQAAERQRLLFFKDVLLTLHQHLDLSSSDKFHELHRDLQQSIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRAISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPSSPGSGQDEDWSDEESPRKVATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQLQSGRIGLYPANYVECVGA [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q99JB8 [UniProt boundaries chain B]=14-302 [UniProt coverage chain B]=68% [Name chain B]=Protein kinase C and casein kinase II substrate protein 3 [UniProt sequence chain B]=MAPEEDAGGEVLGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGAVEKGPQYGTLEKAWHAFFTAAERLSELHLEVREKLHGPDSERVRTWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHTARKDEKTAQTRESHAKADSSMSQEQLRKLQERVGRCTKEAEKMKTQYEQTLAELNRYTPRYMEDMEQAFESCQAAERQRLLFFKDVLLTLHQHLDLSSSDKFHELHRDLQQSIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRAISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPSSPGSGQDEDWSDEESPRKVATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQLQSGRIGLYPANYVECVGA [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Mus musculus [Accession]=MF7000695 [Entry] [Entry number]=880 [Entry name]=Mouse PACSIN3 F-BAR domain [PDB ID]=3qe6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q99JB8 [UniProt boundaries chain A]=14-303 [UniProt coverage chain A]=68% [Name chain A]=Protein kinase C and casein kinase II substrate protein 3 [UniProt sequence chain A]=MAPEEDAGGEVLGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGAVEKGPQYGTLEKAWHAFFTAAERLSELHLEVREKLHGPDSERVRTWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHTARKDEKTAQTRESHAKADSSMSQEQLRKLQERVGRCTKEAEKMKTQYEQTLAELNRYTPRYMEDMEQAFESCQAAERQRLLFFKDVLLTLHQHLDLSSSDKFHELHRDLQQSIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRAISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPSSPGSGQDEDWSDEESPRKVATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQLQSGRIGLYPANYVECVGA [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q99JB8 [UniProt boundaries chain B]=12-302 [UniProt coverage chain B]=68% [Name chain B]=Protein kinase C and casein kinase II substrate protein 3 [UniProt sequence chain B]=MAPEEDAGGEVLGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGAVEKGPQYGTLEKAWHAFFTAAERLSELHLEVREKLHGPDSERVRTWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHTARKDEKTAQTRESHAKADSSMSQEQLRKLQERVGRCTKEAEKMKTQYEQTLAELNRYTPRYMEDMEQAFESCQAAERQRLLFFKDVLLTLHQHLDLSSSDKFHELHRDLQQSIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRAISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPSSPGSGQDEDWSDEESPRKVATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQLQSGRIGLYPANYVECVGA [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Mus musculus [Accession]=MF7000696 [Entry] [Entry number]=881 [Entry name]=Pacsin2 [PDB ID]=4bne [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=O13154 [UniProt boundaries chain A]=15-304 [UniProt coverage chain A]=64% [Name chain A]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain A]=MSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKKKASDGVTLTGINQTGDQVSQPNKHSSVSSYEKNQSYPTDWSDEESNNPFSSTDAKGDTNPFDEDTSPVMEVRVRALYDYEGQEQDELSFKAGDELTKMENEDEQGWCKGRLDNGQVGLYPANYVEPIQ [Source organism chain A]=Gallus gallus [UniProt ID chain B]=O13154 [UniProt boundaries chain B]=15-303 [UniProt coverage chain B]=64% [Name chain B]=Protein kinase C and casein kinase substrate in neurons protein 2 [UniProt sequence chain B]=MSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKKKASDGVTLTGINQTGDQVSQPNKHSSVSSYEKNQSYPTDWSDEESNNPFSSTDAKGDTNPFDEDTSPVMEVRVRALYDYEGQEQDELSFKAGDELTKMENEDEQGWCKGRLDNGQVGLYPANYVEPIQ [Source organism chain B]=Gallus gallus [ExpTech]=X-ray [Resolution]=2.57 [Source organism]=Gallus gallus [Accession]=MF7000697 [Entry] [Entry number]=882 [Entry name]=Rgd1p F-BAR domain [PDB ID]=4wpc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=P38339 [UniProt boundaries chain A]=30-326 [UniProt coverage chain A]=44% [Name chain A]=RHO GTPase-activating protein RGD1 [UniProt sequence chain A]=MEETAKKPASATVSAKSSHDGGTDDLAHLFSTPEIKKVLNSDVAINALLSRLKQSLLTCEEFMKFIRKKYAFEEEHVQELSKQYKHFFNIQGSTNSSLKKMIHEVLGFDGKMAQVKQSYITALQKMYSEISSLLLTMTKLRKSVKENSKRLEKDVSDAIHSAEKAQSRYNSLCQDWDKLRMTDPTKTKLTLRGSKTTKEQEEELLRKIDNADLEYKQKVDHSNSLRNTFITKERPRIVQELKDLILEIDTAMTIQLQKYTIWTENLVLNTGVTISPLDSTKSMKSFAGSVSNERDLYSFLNKYNQTGKHSLLINKNLIPVSYKKHPSMNHGQKNKSPPKFAVDPSRNSIPKRMISTHNESPFLSSSSNTAAVPNANLNSATPSLNTNKQLPPTMASSISSTSNAAGAMSPSSSIVTSDTTSSITKTLDPGNNSPQIPEELINSLDSDRPISHIQTNNNMPPGVQKNFKTFGVPLESLIEFEQDMVPAIVRQCIYVIDKFGLDQEGIYRKSANVLDVSKLKEEIDKDPANISMILPSKPHSDSDIYLVGSLLKTFFASLPDSVLPKALSSEIKVCLQIEDPTTRKNFMHGLIYNLPDAQYWTLRALVFHLKRVLAHEAQNRMNLRALCIIWGPTIAPANPDDANDVNFQIMAMEVLLEVSDQAFEPE [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P38339 [UniProt boundaries chain B]=25-326 [UniProt coverage chain B]=45% [Name chain B]=RHO GTPase-activating protein RGD1 [UniProt sequence chain B]=MEETAKKPASATVSAKSSHDGGTDDLAHLFSTPEIKKVLNSDVAINALLSRLKQSLLTCEEFMKFIRKKYAFEEEHVQELSKQYKHFFNIQGSTNSSLKKMIHEVLGFDGKMAQVKQSYITALQKMYSEISSLLLTMTKLRKSVKENSKRLEKDVSDAIHSAEKAQSRYNSLCQDWDKLRMTDPTKTKLTLRGSKTTKEQEEELLRKIDNADLEYKQKVDHSNSLRNTFITKERPRIVQELKDLILEIDTAMTIQLQKYTIWTENLVLNTGVTISPLDSTKSMKSFAGSVSNERDLYSFLNKYNQTGKHSLLINKNLIPVSYKKHPSMNHGQKNKSPPKFAVDPSRNSIPKRMISTHNESPFLSSSSNTAAVPNANLNSATPSLNTNKQLPPTMASSISSTSNAAGAMSPSSSIVTSDTTSSITKTLDPGNNSPQIPEELINSLDSDRPISHIQTNNNMPPGVQKNFKTFGVPLESLIEFEQDMVPAIVRQCIYVIDKFGLDQEGIYRKSANVLDVSKLKEEIDKDPANISMILPSKPHSDSDIYLVGSLLKTFFASLPDSVLPKALSSEIKVCLQIEDPTTRKNFMHGLIYNLPDAQYWTLRALVFHLKRVLAHEAQNRMNLRALCIIWGPTIAPANPDDANDVNFQIMAMEVLLEVSDQAFEPE [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=3.34 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000698 [Entry] [Entry number]=883 [Entry name]=Hof1p F-BAR domain [PDB ID]=4wpe [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q05080 [UniProt boundaries chain A]=2-275 [UniProt coverage chain A]=40% [Name chain A]=Cytokinesis protein 2 [UniProt sequence chain A]=MSYSYEACFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQSHSKQSEILFRQIYTDTKAFAANLQARYTTLSGKIERLRMDKFNKKKGCEVLQKKLQDAQIRFRDLQLNENNMIGAKRVEHNKRELLKWESNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFATSSMETYILEQTKMDMLTNHLNSFTAADEISTFSKENGTGRLKHKTSKGDMNSSANWAQMSSISTTSKKTESYMDNIRKLSSQLKETENKRKLASIDKYEKPLPSPEVTMATQFRNSTPVIRNETKVVANPTLSLRSSPVQLQSNVDDSVLRQKPDKPRPIVGEEQLKPDEDSKNPDEKGLMVHKRNQSLSSPSESSSSNPTDFSHIKKRQSMESMTTSVSSMANSIDDSQRFAKSWNSSNRKRKSMSHLQVPSSASSRSDDGGRTPNSAHNLNEDDYNTRRDTSTSTILFKPPVAVRGTSRGHTHRQSMIMQDSSNPIEDALYEMERIQSSSKPGTKTGNIMDERGVVRDRGITVTLPIVTSEGFPVIEYAKAMYPLIGNEAPGLANFHKGDYLLITEIVNKDWYKGEVYDNDRIDRNHRIGLIPYNFIQLLHQGL [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=Q05080 [UniProt boundaries chain A-2]=2-275 [UniProt coverage chain A-2]=40% [Name chain A-2]=Cytokinesis protein 2 [UniProt sequence chain A-2]=MSYSYEACFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQSHSKQSEILFRQIYTDTKAFAANLQARYTTLSGKIERLRMDKFNKKKGCEVLQKKLQDAQIRFRDLQLNENNMIGAKRVEHNKRELLKWESNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFATSSMETYILEQTKMDMLTNHLNSFTAADEISTFSKENGTGRLKHKTSKGDMNSSANWAQMSSISTTSKKTESYMDNIRKLSSQLKETENKRKLASIDKYEKPLPSPEVTMATQFRNSTPVIRNETKVVANPTLSLRSSPVQLQSNVDDSVLRQKPDKPRPIVGEEQLKPDEDSKNPDEKGLMVHKRNQSLSSPSESSSSNPTDFSHIKKRQSMESMTTSVSSMANSIDDSQRFAKSWNSSNRKRKSMSHLQVPSSASSRSDDGGRTPNSAHNLNEDDYNTRRDTSTSTILFKPPVAVRGTSRGHTHRQSMIMQDSSNPIEDALYEMERIQSSSKPGTKTGNIMDERGVVRDRGITVTLPIVTSEGFPVIEYAKAMYPLIGNEAPGLANFHKGDYLLITEIVNKDWYKGEVYDNDRIDRNHRIGLIPYNFIQLLHQGL [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000699 [Entry] [Entry number]=884 [Entry name]=Imp2 F-BAR domain [PDB ID]=5c1f [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q10199 [UniProt boundaries chain A]=15-311 [UniProt coverage chain A]=44% [Name chain A]=Septation protein imp2 [UniProt sequence chain A]=MSQQLSFNASSAKPDKSFSNYFWGANDEGYHALLSRFSDVKHINEELRSFYHERANIEEDYAKRMAKLSRTTFSSLETGCLKESVQVMKAEVDNMAKSHLQISQLLQDDVENAFTRYAASLKDKKKMIVSGIEKVHKDKLSKHQALVKAQDKYHYLCKKVNYYVSQQNMLFGKELEKNNAKLNKTQNAITASSSDYQSAVAAVRDSYARWTNEWRSTCDKLQDIEEERRHFLKSVMWTFTLLISRSCFNDDQACERIRKNLEQCSVSQDVLEFIDAKSTGTGIPQPPKFYDYYKGEVPDDSVELVQANFQRAQTKIENDNMPLNRPYVLSATARNESSFENTLPNTPSAIQSLTTVSSNSSQNGRSSPKKSFLSKFKLTSRPSTPNVGNTAPDALSSPRNDSPLTSAADEQMKHLSLQEEPKQNPTPAAPGAFPNSNTLPPRYNELGSLPSPNSVSFTEDSRPNVNTPSRRQQIQEEFGSVLQMENRAVSPVYDSRKNGSRSSFTLRKSRSPKRPSSSLSQNASRLPRSLTPGNLEPNYDFGVRVDPASGTAPTDDEPYTDRDSSFVDDTINTKATGNTSNRLSLPAYPTDGGDTSIDNPTSTDGQRILGYVSALYDYDAAIPEEISFRKGDTIAVLKLYEDGWWEGFVVGEDDHNRGQFPSNFVREIEV [Source organism chain A]=Schizosaccharomyces pombe [UniProt ID chain B]=Q10199 [UniProt boundaries chain B]=15-311 [UniProt coverage chain B]=44% [Name chain B]=Septation protein imp2 [UniProt sequence chain B]=MSQQLSFNASSAKPDKSFSNYFWGANDEGYHALLSRFSDVKHINEELRSFYHERANIEEDYAKRMAKLSRTTFSSLETGCLKESVQVMKAEVDNMAKSHLQISQLLQDDVENAFTRYAASLKDKKKMIVSGIEKVHKDKLSKHQALVKAQDKYHYLCKKVNYYVSQQNMLFGKELEKNNAKLNKTQNAITASSSDYQSAVAAVRDSYARWTNEWRSTCDKLQDIEEERRHFLKSVMWTFTLLISRSCFNDDQACERIRKNLEQCSVSQDVLEFIDAKSTGTGIPQPPKFYDYYKGEVPDDSVELVQANFQRAQTKIENDNMPLNRPYVLSATARNESSFENTLPNTPSAIQSLTTVSSNSSQNGRSSPKKSFLSKFKLTSRPSTPNVGNTAPDALSSPRNDSPLTSAADEQMKHLSLQEEPKQNPTPAAPGAFPNSNTLPPRYNELGSLPSPNSVSFTEDSRPNVNTPSRRQQIQEEFGSVLQMENRAVSPVYDSRKNGSRSSFTLRKSRSPKRPSSSLSQNASRLPRSLTPGNLEPNYDFGVRVDPASGTAPTDDEPYTDRDSSFVDDTINTKATGNTSNRLSLPAYPTDGGDTSIDNPTSTDGQRILGYVSALYDYDAAIPEEISFRKGDTIAVLKLYEDGWWEGFVVGEDDHNRGQFPSNFVREIEV [Source organism chain B]=Schizosaccharomyces pombe [ExpTech]=X-ray [Resolution]=2.36 [Source organism]=Schizosaccharomyces pombe [Accession]=MF7000700 [Entry] [Entry number]=885 [Entry name]=SRGAP2 F-BARx [PDB ID]=5i6j [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=O75044 [UniProt boundaries chain A]=8-481 [UniProt coverage chain A]=44% [Name chain A]=SLIT-ROBO Rho GTPase-activating protein 2 [UniProt sequence chain A]=MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLQHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLMACVTMDNLQERALHIRKVLLVLPKTTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVISEPPEEKVTARAGASCPSGGHVADIYLANINKQRKRPESGSIRKTFRSDSHGLSSSLTDSSSPGVGASCRPSSQPIMSQSLPKEGPDKCSISGHGSLNSISRHSSLKNRLDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELRELERQSSVKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSTSPQSTDKSCTV [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=O75044 [UniProt boundaries chain A-2]=8-481 [UniProt coverage chain A-2]=44% [Name chain A-2]=SLIT-ROBO Rho GTPase-activating protein 2 [UniProt sequence chain A-2]=MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLQHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLMACVTMDNLQERALHIRKVLLVLPKTTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVISEPPEEKVTARAGASCPSGGHVADIYLANINKQRKRPESGSIRKTFRSDSHGLSSSLTDSSSPGVGASCRPSSQPIMSQSLPKEGPDKCSISGHGSLNSISRHSSLKNRLDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELRELERQSSVKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSTSPQSTDKSCTV [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.70 [Source organism]=Homo sapiens [Accession]=MF7000701 [Entry] [Entry number]=886 [Entry name]=Mouse GAS7cb [PDB ID]=6iko [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q60780 [UniProt boundaries chain A]=117-419 [UniProt coverage chain A]=71% [Name chain A]=Growth arrest-specific protein 7 [UniProt sequence chain A]=MATALQKPGMVPPPPGEESQTVILPPGWHSYLSPQGRRYYVNTTTNETTWERPSSSPGISASPAPHRSSLPTTVNGYHASGTPAHPPETAHMSLRKSTGDSQNLGSSSPGRKQSKENTITINCVTFPHPDTMPEQQLLKPTEWSYCDYFWADKKDPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQLLRKVDPAKDRELWVREHKTGNIRPVDMEI [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q60780 [UniProt boundaries chain B]=118-420 [UniProt coverage chain B]=71% [Name chain B]=Growth arrest-specific protein 7 [UniProt sequence chain B]=MATALQKPGMVPPPPGEESQTVILPPGWHSYLSPQGRRYYVNTTTNETTWERPSSSPGISASPAPHRSSLPTTVNGYHASGTPAHPPETAHMSLRKSTGDSQNLGSSSPGRKQSKENTITINCVTFPHPDTMPEQQLLKPTEWSYCDYFWADKKDPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQLLRKVDPAKDRELWVREHKTGNIRPVDMEI [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=3.76 [Source organism]=Mus musculus [Accession]=MF7000702 [Entry] [Entry number]=887 [Entry name]=CDC15 F-BAR Domain (Schizosaccharomyces pombe) [PDB ID]=6xj1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=Q09822 [UniProt boundaries chain A]=35-300 [UniProt coverage chain A]=28% [Name chain A]=Cell division control protein 15 [UniProt sequence chain A]=MEVNGVSQSEAAPYVTKSSVKFRDNFWGSEDAGMDALMSRTKSSLSVLESIDEFYAKRASIEREYASKLQELAASSADIPEVGSTLNNILSMRTETGSMAKAHEEVSQQINTELRNKIREYIDQTEQQKVVAANAIEELYQKKTALEIDLSEKKDAYEYSCNKLNSYMRQTKKMTGRELDKYNLKIRQAALAVKKMDAEYRETNELLLTVTREWIDRWTEVCDAFQHIEEYRLEFLKTNMWAYANIISTACVKDDESCEKIRLTLENTNIDEDITQMIQNEGTGTTIPPLPEFNDYFKENGLNYDIDQLISKAPSYPYSSSRPSASASLASSPTRSAFRPKTSETVSSEVVSSPPTSPLHSPVKPVSNEQVEQVTEVELSIPVPSIQEAESQKPVLTGSSMRRPSVTSPTFEVAARPLTSMDVRSSHNAETEVQAIPAATDISPEVKEGKNSENAITKDNDDIILSSQLQPTATGSRSSRLSFSRHGHGSQTSLGSIKRKSIMERMGRPTSPFMGSSFSNMGSRSTSPTKEGFASNQHATGASVQSDELEDIDPRANVVLNVGPNMLSVGEAPVESTSKEEDKDVPDPIANAMAELSSSMRRRQSTSVDDEAPVSLSKTSSSTRLNGLGYHSRNTSIASDIDGVPKKSTLGAPPAAHTSAQMQRMSNSFASQTKQVFGEQRTENSARESLRHSRSNMSRSPSPMLSRRSSTLRPSFERSASSLSVRQSDVVSPAPSTRARGQSVSGQQRPSSSMSLYGEYNKSQPQLSMQRSVSPNPLGPNRRSSSVLQSQKSTSSNTSNRNNGGYSGSRPSSEMGHRYGSMSGRSMRQVSQRSTSRARSPEPTNRNSVQSKNVDPRATFTAEGEPILGYVIALYDYQAQIPEEISFQKGDTLMVLRTQEDGWWDGEIINVPNSKRGLFPSNFVQTV [Source organism chain A]=Schizosaccharomyces pombe [UniProt ID chain B]=Q09822 [UniProt boundaries chain B]=22-298 [UniProt coverage chain B]=29% [Name chain B]=Cell division control protein 15 [UniProt sequence chain B]=MEVNGVSQSEAAPYVTKSSVKFRDNFWGSEDAGMDALMSRTKSSLSVLESIDEFYAKRASIEREYASKLQELAASSADIPEVGSTLNNILSMRTETGSMAKAHEEVSQQINTELRNKIREYIDQTEQQKVVAANAIEELYQKKTALEIDLSEKKDAYEYSCNKLNSYMRQTKKMTGRELDKYNLKIRQAALAVKKMDAEYRETNELLLTVTREWIDRWTEVCDAFQHIEEYRLEFLKTNMWAYANIISTACVKDDESCEKIRLTLENTNIDEDITQMIQNEGTGTTIPPLPEFNDYFKENGLNYDIDQLISKAPSYPYSSSRPSASASLASSPTRSAFRPKTSETVSSEVVSSPPTSPLHSPVKPVSNEQVEQVTEVELSIPVPSIQEAESQKPVLTGSSMRRPSVTSPTFEVAARPLTSMDVRSSHNAETEVQAIPAATDISPEVKEGKNSENAITKDNDDIILSSQLQPTATGSRSSRLSFSRHGHGSQTSLGSIKRKSIMERMGRPTSPFMGSSFSNMGSRSTSPTKEGFASNQHATGASVQSDELEDIDPRANVVLNVGPNMLSVGEAPVESTSKEEDKDVPDPIANAMAELSSSMRRRQSTSVDDEAPVSLSKTSSSTRLNGLGYHSRNTSIASDIDGVPKKSTLGAPPAAHTSAQMQRMSNSFASQTKQVFGEQRTENSARESLRHSRSNMSRSPSPMLSRRSSTLRPSFERSASSLSVRQSDVVSPAPSTRARGQSVSGQQRPSSSMSLYGEYNKSQPQLSMQRSVSPNPLGPNRRSSSVLQSQKSTSSNTSNRNNGGYSGSRPSSEMGHRYGSMSGRSMRQVSQRSTSRARSPEPTNRNSVQSKNVDPRATFTAEGEPILGYVIALYDYQAQIPEEISFQKGDTLMVLRTQEDGWWDGEIINVPNSKRGLFPSNFVQTV [Source organism chain B]=Schizosaccharomyces pombe [ExpTech]=X-ray [Resolution]=3.52 [Source organism]=Schizosaccharomyces pombe [Accession]=MF7000703 [Entry] [Entry number]=888 [Entry name]=F-BAR domain of PSTIPIP1 [PDB ID]=7aan [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=O43586 [UniProt boundaries chain A]=5-289 [UniProt coverage chain A]=68% [Name chain A]=Proline-serine-threonine phosphatase-interacting protein 1 [UniProt sequence chain A]=MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPKTTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVERNGQRGFVPGSYLEKL [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O43586 [UniProt boundaries chain B]=4-289 [UniProt coverage chain B]=68% [Name chain B]=Proline-serine-threonine phosphatase-interacting protein 1 [UniProt sequence chain B]=MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPKTTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVERNGQRGFVPGSYLEKL [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.14 [Source organism]=Homo sapiens [Accession]=MF7000704 [Entry] [Entry number]=889 [Entry name]=F-BAR domain of PSTIPIP1, G258A mutant [PDB ID]=7aal [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=F-BAR domain [Sequence domain]=F-BAR domain [Evidence level]=Direct evidence [Evidence text]=F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000687,MF7000688,MF7000689,MF7000690,MF7000691,MF7000692,MF7000693,MF7000694,MF7000695,MF7000696,MF7000697,MF7000698,MF7000699,MF7000700,MF7000701,MF7000702,MF7000703,MF7000704,MF7000705 [UniProt ID chain A]=O43586 [UniProt boundaries chain A]=5-289 [UniProt coverage chain A]=68% [Name chain A]=Proline-serine-threonine phosphatase-interacting protein 1 [UniProt sequence chain A]=MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPKTTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVERNGQRGFVPGSYLEKL [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O43586 [UniProt boundaries chain B]=5-289 [UniProt coverage chain B]=68% [Name chain B]=Proline-serine-threonine phosphatase-interacting protein 1 [UniProt sequence chain B]=MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPKTTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVERNGQRGFVPGSYLEKL [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.97 [Source organism]=Homo sapiens [Accession]=MF7000705 [Entry] [Entry number]=890 [Entry name]=SMTB repressor (Synechococcus elongatus PCC 7942) [PDB ID]=1smt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=P30340 [UniProt boundaries chain A]=24-121 [UniProt coverage chain A]=80% [Name chain A]=Transcriptional repressor SmtB [UniProt sequence chain A]=MTKPVLQDGETVVCQGTHAAIASELQAIAPEVAQSLAEFFAVLADPNRLRLLSLLARSELCVGDLAQAIGVSESAVSHQLRSLRNLRLVSYRKQGRHVYYQLQDHHIVALYQNALDHLQECR [Source organism chain A]= [UniProt ID chain B]=P30340 [UniProt boundaries chain B]=20-120 [UniProt coverage chain B]=82% [Name chain B]=Transcriptional repressor SmtB [UniProt sequence chain B]=MTKPVLQDGETVVCQGTHAAIASELQAIAPEVAQSLAEFFAVLADPNRLRLLSLLARSELCVGDLAQAIGVSESAVSHQLRSLRNLRLVSYRKQGRHVYYQLQDHHIVALYQNALDHLQECR [Source organism chain B]= [ExpTech]=X-ray [Resolution]=2.20 [Source organism]= [Accession]=MF7000706 [Entry] [Entry number]=891 [Entry name]=Cyanobacterial metallothionein repressor SmtB (C14S/C61S/C121S mutant) in the Zn2alpha5-form [PDB ID]=1r22 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=P30340 [UniProt boundaries chain A]=25-121 [UniProt coverage chain A]=79% [Name chain A]=Transcriptional repressor SmtB [UniProt sequence chain A]=MTKPVLQDGETVVCQGTHAAIASELQAIAPEVAQSLAEFFAVLADPNRLRLLSLLARSELCVGDLAQAIGVSESAVSHQLRSLRNLRLVSYRKQGRHVYYQLQDHHIVALYQNALDHLQECR [Source organism chain A]= [UniProt ID chain B]=P30340 [UniProt boundaries chain B]=26-122 [UniProt coverage chain B]=79% [Name chain B]=Transcriptional repressor SmtB [UniProt sequence chain B]=MTKPVLQDGETVVCQGTHAAIASELQAIAPEVAQSLAEFFAVLADPNRLRLLSLLARSELCVGDLAQAIGVSESAVSHQLRSLRNLRLVSYRKQGRHVYYQLQDHHIVALYQNALDHLQECR [Source organism chain B]= [ExpTech]=X-ray [Resolution]=2.30 [Source organism]= [Accession]=MF7000707 [Entry] [Entry number]=892 [Entry name]=Cyanobacterial metallothionein repressor SmtB in the Zn1-form [PDB ID]=1r23 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=P30340 [UniProt boundaries chain A]=18-121 [UniProt coverage chain A]=85% [Name chain A]=Transcriptional repressor SmtB [UniProt sequence chain A]=MTKPVLQDGETVVCQGTHAAIASELQAIAPEVAQSLAEFFAVLADPNRLRLLSLLARSELCVGDLAQAIGVSESAVSHQLRSLRNLRLVSYRKQGRHVYYQLQDHHIVALYQNALDHLQECR [Source organism chain A]= [UniProt ID chain B]=P30340 [UniProt boundaries chain B]=25-121 [UniProt coverage chain B]=79% [Name chain B]=Transcriptional repressor SmtB [UniProt sequence chain B]=MTKPVLQDGETVVCQGTHAAIASELQAIAPEVAQSLAEFFAVLADPNRLRLLSLLARSELCVGDLAQAIGVSESAVSHQLRSLRNLRLVSYRKQGRHVYYQLQDHHIVALYQNALDHLQECR [Source organism chain B]= [ExpTech]=X-ray [Resolution]=2.00 [Source organism]= [Accession]=MF7000708 [Entry] [Entry number]=893 [Entry name]=Cyanobacterial metallothionein repressor SmtB (apo form) [PDB ID]=1r1t [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=P30340 [UniProt boundaries chain A]=24-121 [UniProt coverage chain A]=80% [Name chain A]=Transcriptional repressor SmtB [UniProt sequence chain A]=MTKPVLQDGETVVCQGTHAAIASELQAIAPEVAQSLAEFFAVLADPNRLRLLSLLARSELCVGDLAQAIGVSESAVSHQLRSLRNLRLVSYRKQGRHVYYQLQDHHIVALYQNALDHLQECR [Source organism chain A]= [UniProt ID chain B]=P30340 [UniProt boundaries chain B]=20-118 [UniProt coverage chain B]=81% [Name chain B]=Transcriptional repressor SmtB [UniProt sequence chain B]=MTKPVLQDGETVVCQGTHAAIASELQAIAPEVAQSLAEFFAVLADPNRLRLLSLLARSELCVGDLAQAIGVSESAVSHQLRSLRNLRLVSYRKQGRHVYYQLQDHHIVALYQNALDHLQECR [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.70 [Source organism]= [Accession]=MF7000709 [Entry] [Entry number]=894 [Entry name]=Metal-sensing transcriptional repressor CzrA (Staphylococcus aureus) [PDB ID]=1r1v [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=O85142 [UniProt boundaries chain A]=9-103 [UniProt coverage chain A]=89% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A]=Staphylococcus aureus [UniProt ID chain A-2]=O85142 [UniProt boundaries chain A-2]=9-104 [UniProt coverage chain A-2]=90% [Name chain A-2]=Transcriptional regulator [UniProt sequence chain A-2]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A-2]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Staphylococcus aureus [Accession]=MF7000710 [Entry] [Entry number]=895 [Entry name]=Cadmium metal-sensor CMTR (Mycobacterium tuberculosis) [PDB ID]=2jsc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=P9WMI9 [UniProt boundaries chain A]=11-106 [UniProt coverage chain A]=81% [Name chain A]=HTH-type transcriptional regulator CmtR [UniProt sequence chain A]=MLTCEMRESALARLGRALADPTRCRILVALLDGVCYPGQLAAHLGLTRSNVSNHLSCLRGCGLVVATYEGRQVRYALADSHLARALGELVQVVLAVDTDQPCVAERAASGEAVEMTGS [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WMI9 [UniProt boundaries chain B]=10-106 [UniProt coverage chain B]=82% [Name chain B]=HTH-type transcriptional regulator CmtR [UniProt sequence chain B]=MLTCEMRESALARLGRALADPTRCRILVALLDGVCYPGQLAAHLGLTRSNVSNHLSCLRGCGLVVATYEGRQVRYALADSHLARALGELVQVVLAVDTDQPCVAERAASGEAVEMTGS [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000711 [Entry] [Entry number]=896 [Entry name]=CzrA with Zn [PDB ID]=2kjc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=O85142 [UniProt boundaries chain A]=9-103 [UniProt coverage chain A]=89% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=O85142 [UniProt boundaries chain B]=9-103 [UniProt coverage chain B]=89% [Name chain B]=Transcriptional regulator [UniProt sequence chain B]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain B]=Staphylococcus aureus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Staphylococcus aureus [Accession]=MF7000712 [Entry] [Entry number]=897 [Entry name]=NmtR (apo form) [PDB ID]=2lkp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=Q7D4Y3 [UniProt boundaries chain A]=17-135 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator, ArsR family [UniProt sequence chain A]=MIICSFISLGIGCLTMGHGVEGRNRPSAPLDSQAAAQVASTLQALATPSRLMILTQLRNGPLPVTDLAEAIGMEQSAVSHQLRVLRNLGLVVGDRAGRSIVYSLYDTHVAQLLDEAIYHSEHLHLGLSDRHPSAG [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=Q7D4Y3 [UniProt boundaries chain B]=17-135 [UniProt coverage chain B]=88% [Name chain B]=Transcriptional regulator, ArsR family [UniProt sequence chain B]=MIICSFISLGIGCLTMGHGVEGRNRPSAPLDSQAAAQVASTLQALATPSRLMILTQLRNGPLPVTDLAEAIGMEQSAVSHQLRVLRNLGLVVGDRAGRSIVYSLYDTHVAQLLDEAIYHSEHLHLGLSDRHPSAG [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000713 [Entry] [Entry number]=898 [Entry name]=V66A/L68V CzrA with Zn [PDB ID]=4ggg [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=A0A0H3JNF1 [UniProt boundaries chain A]=11-102 [UniProt coverage chain A]=86% [Name chain A]=Repressor protein [UniProt sequence chain A]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A]=Staphylococcus aureus [UniProt ID chain A-2]=A0A0H3JNF1 [UniProt boundaries chain A-2]=9-101 [UniProt coverage chain A-2]=87% [Name chain A-2]=Repressor protein [UniProt sequence chain A-2]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A-2]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Staphylococcus aureus [Accession]=MF7000714 [Entry] [Entry number]=899 [Entry name]=CzrA (Staphylococcus aureus) [PDB ID]=2m30 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=O85142 [UniProt boundaries chain A]=9-103 [UniProt coverage chain A]=89% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=O85142 [UniProt boundaries chain B]=9-103 [UniProt coverage chain B]=89% [Name chain B]=Transcriptional regulator [UniProt sequence chain B]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain B]=Staphylococcus aureus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Staphylococcus aureus [Accession]=MF7000715 [Entry] [Entry number]=900 [Entry name]=L34A CzrA in the Zn(II)bound state [PDB ID]=6cda [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=O85142 [UniProt boundaries chain A]=8-102 [UniProt coverage chain A]=89% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A]=Staphylococcus aureus [UniProt ID chain A-2]=O85142 [UniProt boundaries chain A-2]=8-102 [UniProt coverage chain A-2]=89% [Name chain A-2]=Transcriptional regulator [UniProt sequence chain A-2]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A-2]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Staphylococcus aureus [Accession]=MF7000716 [Entry] [Entry number]=901 [Entry name]=CM14-treated HlyU (Vibrio vulnificus) [PDB ID]=5znx [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=A0A3Q0L222 [UniProt boundaries chain A]=4-98 [UniProt coverage chain A]=96% [Name chain A]=Transcriptional activator HlyU [UniProt sequence chain A]=MNLKDMEQNSAKAVVLLKAMANERRLQILCMLHNQELSVGELCAKLQLSQSALSQHLAWLRRDGLVTTRKEAQTVYYTLKSEEVKAMIKLLHSLYCEE [Source organism chain A]=Vibrio vulnificus [UniProt ID chain A-2]=A0A3Q0L222 [UniProt boundaries chain A-2]=4-98 [UniProt coverage chain A-2]=96% [Name chain A-2]=Transcriptional activator HlyU [UniProt sequence chain A-2]=MNLKDMEQNSAKAVVLLKAMANERRLQILCMLHNQELSVGELCAKLQLSQSALSQHLAWLRRDGLVTTRKEAQTVYYTLKSEEVKAMIKLLHSLYCEE [Source organism chain A-2]=Vibrio vulnificus [ExpTech]=X-ray [Resolution]=2.11 [Source organism]=Vibrio vulnificus [Accession]=MF7000717 [Entry] [Entry number]=902 [Entry name]=ArsR As(III)-responsive repressors [PDB ID]=6j0e [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=A0A5H1ZR36 [UniProt boundaries chain A]=2-127 [UniProt coverage chain A]=99% [Name chain A]=Arsenic responsive repressor ArsR [UniProt sequence chain A]=MTTLHTIQLANPTECCTLATGPLSSDESEHYADLFKVLGDPVRLRILSQLAAGGCGPVSVNELTDLMGLSQPTISHHLKKMTEAGFLDRVPEGRVVLHRVRPELFAELRTVLQIGSMELLEHHHHHH [Source organism chain A]=534) [UniProt ID chain B]=A0A5H1ZR36 [UniProt boundaries chain B]=3-127 [UniProt coverage chain B]=98% [Name chain B]=Arsenic responsive repressor ArsR [UniProt sequence chain B]=MTTLHTIQLANPTECCTLATGPLSSDESEHYADLFKVLGDPVRLRILSQLAAGGCGPVSVNELTDLMGLSQPTISHHLKKMTEAGFLDRVPEGRVVLHRVRPELFAELRTVLQIGSMELLEHHHHHH [Source organism chain B]=534) [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=534) [Accession]=MF7000718 [Entry] [Entry number]=903 [Entry name]=Apo and reduced sulfide-responsive transcriptional repressor (SqrR) (Rhodobacter capsulatus) [PDB ID]=6o8k [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=D5AT91 [UniProt boundaries chain A]=30-122 [UniProt coverage chain A]=75% [Name chain A]=Transcriptional regulator, ArsR family [UniProt sequence chain A]=MDTAQDPQDDFDPEMGSDTDERCAALDAEEMATRARAASNLLKALAHEGRLMIMCYLASGEKSVTELETRLSTRQAAVSQQLARLRLEGLVQSRREGKTIYYSLSDPRAARVVQTVYEQFCSGD [Source organism chain A]=Rhodobacter capsulatus [UniProt ID chain A-2]=D5AT91 [UniProt boundaries chain A-2]=30-122 [UniProt coverage chain A-2]=75% [Name chain A-2]=Transcriptional regulator, ArsR family [UniProt sequence chain A-2]=MDTAQDPQDDFDPEMGSDTDERCAALDAEEMATRARAASNLLKALAHEGRLMIMCYLASGEKSVTELETRLSTRQAAVSQQLARLRLEGLVQSRREGKTIYYSLSDPRAARVVQTVYEQFCSGD [Source organism chain A-2]=Rhodobacter capsulatus [ExpTech]=X-ray [Resolution]=2.12 [Source organism]=Rhodobacter capsulatus [Accession]=MF7000719 [Entry] [Entry number]=904 [Entry name]=C9S apo and reduced sulfide-responsive transcriptional repressor (SqrR) (Rhodobacter capsulatus) [PDB ID]=6o8l [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=D5AT91 [UniProt boundaries chain A]=32-123 [UniProt coverage chain A]=74% [Name chain A]=Transcriptional regulator, ArsR family [UniProt sequence chain A]=MDTAQDPQDDFDPEMGSDTDERCAALDAEEMATRARAASNLLKALAHEGRLMIMCYLASGEKSVTELETRLSTRQAAVSQQLARLRLEGLVQSRREGKTIYYSLSDPRAARVVQTVYEQFCSGD [Source organism chain A]=Rhodobacter capsulatus [UniProt ID chain A-2]=D5AT91 [UniProt boundaries chain A-2]=32-123 [UniProt coverage chain A-2]=74% [Name chain A-2]=Transcriptional regulator, ArsR family [UniProt sequence chain A-2]=MDTAQDPQDDFDPEMGSDTDERCAALDAEEMATRARAASNLLKALAHEGRLMIMCYLASGEKSVTELETRLSTRQAAVSQQLARLRLEGLVQSRREGKTIYYSLSDPRAARVVQTVYEQFCSGD [Source organism chain A-2]=Rhodobacter capsulatus [ExpTech]=X-ray [Resolution]=1.36 [Source organism]=Rhodobacter capsulatus [Accession]=MF7000720 [Entry] [Entry number]=905 [Entry name]=C9S apo sulfide-responsive transcriptional repressor (SqrR) with diamide (Rhodobacter capsulatus) [PDB ID]=6o8m [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=D5AT91 [UniProt boundaries chain A]=30-124 [UniProt coverage chain A]=76% [Name chain A]=Transcriptional regulator, ArsR family [UniProt sequence chain A]=MDTAQDPQDDFDPEMGSDTDERCAALDAEEMATRARAASNLLKALAHEGRLMIMCYLASGEKSVTELETRLSTRQAAVSQQLARLRLEGLVQSRREGKTIYYSLSDPRAARVVQTVYEQFCSGD [Source organism chain A]=Rhodobacter capsulatus [UniProt ID chain A-2]=D5AT91 [UniProt boundaries chain A-2]=30-124 [UniProt coverage chain A-2]=76% [Name chain A-2]=Transcriptional regulator, ArsR family [UniProt sequence chain A-2]=MDTAQDPQDDFDPEMGSDTDERCAALDAEEMATRARAASNLLKALAHEGRLMIMCYLASGEKSVTELETRLSTRQAAVSQQLARLRLEGLVQSRREGKTIYYSLSDPRAARVVQTVYEQFCSGD [Source organism chain A-2]=Rhodobacter capsulatus [ExpTech]=X-ray [Resolution]=1.46 [Source organism]=Rhodobacter capsulatus [Accession]=MF7000721 [Entry] [Entry number]=906 [Entry name]=Sulfide-responsive transcriptional repressor (SqrR), C9S tetrasulfide state (Rhodobacter capsulatus) [PDB ID]=6o8n [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArsR family) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000706,MF7000085,MF7000707,MF7000708,MF7000709,MF7000710,MF7000711,MF7000712,MF7000713,MF7000714,MF7000715,MF7000716,MF7000717,MF7000718,MF7000719,MF7000720,MF7000721,MF7000722 [UniProt ID chain A]=D5AT91 [UniProt boundaries chain A]=29-123 [UniProt coverage chain A]=76% [Name chain A]=Transcriptional regulator, ArsR family [UniProt sequence chain A]=MDTAQDPQDDFDPEMGSDTDERCAALDAEEMATRARAASNLLKALAHEGRLMIMCYLASGEKSVTELETRLSTRQAAVSQQLARLRLEGLVQSRREGKTIYYSLSDPRAARVVQTVYEQFCSGD [Source organism chain A]=Rhodobacter capsulatus [UniProt ID chain B]=D5AT91 [UniProt boundaries chain B]=27-123 [UniProt coverage chain B]=78% [Name chain B]=Transcriptional regulator, ArsR family [UniProt sequence chain B]=MDTAQDPQDDFDPEMGSDTDERCAALDAEEMATRARAASNLLKALAHEGRLMIMCYLASGEKSVTELETRLSTRQAAVSQQLARLRLEGLVQSRREGKTIYYSLSDPRAARVVQTVYEQFCSGD [Source organism chain B]=Rhodobacter capsulatus [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Rhodobacter capsulatus [Accession]=MF7000722 [Entry] [Entry number]=907 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase (Mycobacterium abscessus) [PDB ID]=6qqv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=93% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-232 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.71 [Source organism]=abscessus) [Accession]=MF7000723 [Entry] [Entry number]=908 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase (Mycobacterium abscessus) [PDB ID]=6qqw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=93% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-232 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=abscessus) [Accession]=MF7000724 [Entry] [Entry number]=909 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase (Mycobacterium abscessus) [PDB ID]=6qrf [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=93% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-232 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.86 [Source organism]=abscessus) [Accession]=MF7000725 [Entry] [Entry number]=910 [Entry name]=TrmD (apo form) (Mycobacterium abscessus) [PDB ID]=5zhi [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=P9WFY7 [UniProt boundaries chain A]=1-226 [UniProt coverage chain A]=98% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MRIDIVTIFPACLDPLRQSLPGKAIESGLVDLNVHDLRRWTHDVHHSVDDAPYGGGPGMVMKAPVWGEALDEICSSETLLIVPTPAGVLFTQATAQRWTTESHLVFACGRYEGIDQRVVQDAARRMRVEEVSIGDYVLPGGESAAVVMVEAVLRLLAGVLGNPASHQDDSHSTGLDGLLEGPSYTRPASWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPDLSHPD [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WFY7 [UniProt boundaries chain B]=1-226 [UniProt coverage chain B]=98% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MRIDIVTIFPACLDPLRQSLPGKAIESGLVDLNVHDLRRWTHDVHHSVDDAPYGGGPGMVMKAPVWGEALDEICSSETLLIVPTPAGVLFTQATAQRWTTESHLVFACGRYEGIDQRVVQDAARRMRVEEVSIGDYVLPGGESAAVVMVEAVLRLLAGVLGNPASHQDDSHSTGLDGLLEGPSYTRPASWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPDLSHPD [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000726 [Entry] [Entry number]=911 [Entry name]=TrmD with SAH (Mycobacterium tuberculosis) [PDB ID]=5zhj [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=P9WFY7 [UniProt boundaries chain A]=1-226 [UniProt coverage chain A]=98% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MRIDIVTIFPACLDPLRQSLPGKAIESGLVDLNVHDLRRWTHDVHHSVDDAPYGGGPGMVMKAPVWGEALDEICSSETLLIVPTPAGVLFTQATAQRWTTESHLVFACGRYEGIDQRVVQDAARRMRVEEVSIGDYVLPGGESAAVVMVEAVLRLLAGVLGNPASHQDDSHSTGLDGLLEGPSYTRPASWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPDLSHPD [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=P9WFY7 [UniProt boundaries chain A-2]=1-226 [UniProt coverage chain A-2]=98% [Name chain A-2]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A-2]=MRIDIVTIFPACLDPLRQSLPGKAIESGLVDLNVHDLRRWTHDVHHSVDDAPYGGGPGMVMKAPVWGEALDEICSSETLLIVPTPAGVLFTQATAQRWTTESHLVFACGRYEGIDQRVVQDAARRMRVEEVSIGDYVLPGGESAAVVMVEAVLRLLAGVLGNPASHQDDSHSTGLDGLLEGPSYTRPASWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPDLSHPD [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.75 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000727 [Entry] [Entry number]=912 [Entry name]=TrmD with active-site inhibitor (Mycobacterium tuberculosis) [PDB ID]=5zhk [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=P9WFY7 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=98% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MRIDIVTIFPACLDPLRQSLPGKAIESGLVDLNVHDLRRWTHDVHHSVDDAPYGGGPGMVMKAPVWGEALDEICSSETLLIVPTPAGVLFTQATAQRWTTESHLVFACGRYEGIDQRVVQDAARRMRVEEVSIGDYVLPGGESAAVVMVEAVLRLLAGVLGNPASHQDDSHSTGLDGLLEGPSYTRPASWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPDLSHPD [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=P9WFY7 [UniProt boundaries chain A-2]=1-227 [UniProt coverage chain A-2]=98% [Name chain A-2]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A-2]=MRIDIVTIFPACLDPLRQSLPGKAIESGLVDLNVHDLRRWTHDVHHSVDDAPYGGGPGMVMKAPVWGEALDEICSSETLLIVPTPAGVLFTQATAQRWTTESHLVFACGRYEGIDQRVVQDAARRMRVEEVSIGDYVLPGGESAAVVMVEAVLRLLAGVLGNPASHQDDSHSTGLDGLLEGPSYTRPASWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPDLSHPD [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000728 [Entry] [Entry number]=913 [Entry name]=TrmD with active-site inhibitor (Mycobacterium tuberculosis) [PDB ID]=5zhl [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=P9WFY7 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=98% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MRIDIVTIFPACLDPLRQSLPGKAIESGLVDLNVHDLRRWTHDVHHSVDDAPYGGGPGMVMKAPVWGEALDEICSSETLLIVPTPAGVLFTQATAQRWTTESHLVFACGRYEGIDQRVVQDAARRMRVEEVSIGDYVLPGGESAAVVMVEAVLRLLAGVLGNPASHQDDSHSTGLDGLLEGPSYTRPASWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPDLSHPD [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=P9WFY7 [UniProt boundaries chain A-2]=1-227 [UniProt coverage chain A-2]=98% [Name chain A-2]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A-2]=MRIDIVTIFPACLDPLRQSLPGKAIESGLVDLNVHDLRRWTHDVHHSVDDAPYGGGPGMVMKAPVWGEALDEICSSETLLIVPTPAGVLFTQATAQRWTTESHLVFACGRYEGIDQRVVQDAARRMRVEEVSIGDYVLPGGESAAVVMVEAVLRLLAGVLGNPASHQDDSHSTGLDGLLEGPSYTRPASWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPDLSHPD [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000729 [Entry] [Entry number]=914 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase with Fragment 18 (Isoxazole-5-carbothioamide) (Mycobacteroides abscessus) [PDB ID]=6qoo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=93% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-231 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.94 [Source organism]=abscessus) [Accession]=MF7000730 [Entry] [Entry number]=915 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase with Fragment 5 (Isoxazole-5-carboxamide) (Mycobacteroides abscessus) [PDB ID]=6qoa [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-228 [UniProt coverage chain A]=94% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-231 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.93 [Source organism]=abscessus) [Accession]=MF7000731 [Entry] [Entry number]=916 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase with Fragment 9 (Adenine) (Mycobacteroides abscessus) [PDB ID]=6qof [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-229 [UniProt coverage chain A]=94% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-231 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.76 [Source organism]=abscessus) [Accession]=MF7000732 [Entry] [Entry number]=917 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase with Fragment 12 (2-Aminobenzothiazole) (Mycobacteroides abscessus) [PDB ID]=6qoi [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=93% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-231 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.86 [Source organism]=abscessus) [Accession]=MF7000733 [Entry] [Entry number]=918 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase with Fragment 13 (4-Hydroxyquinazoline) (Mycobacteroides abscessus) [PDB ID]=6qoj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-231 [UniProt coverage chain A]=95% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-228 [UniProt coverage chain B]=94% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=2.02 [Source organism]=abscessus) [Accession]=MF7000734 [Entry] [Entry number]=919 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferasewith Fragment 16 (2-Amino-3-nitropyridine) (Mycobacteroides abscessus) [PDB ID]=6qom [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-228 [UniProt coverage chain A]=94% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-232 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=abscessus) [Accession]=MF7000735 [Entry] [Entry number]=920 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase with Fragment 19 (5-fluoroquinazolin-4-ol) (Mycobacteroides abscessus) [PDB ID]=6qop [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=93% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-231 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.91 [Source organism]=abscessus) [Accession]=MF7000736 [Entry] [Entry number]=921 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase with Fragment 22 (Ethyl 1H-pyrazole-4-carboxylate) (Mycobacteroides abscessus) [PDB ID]=6qos [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=93% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-232 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=abscessus) [Accession]=MF7000737 [Entry] [Entry number]=922 [Entry name]=TrmD, a tRNA-(N1G37) methyltransferase with inhibitor (Mycobacteroides abscessus) [PDB ID]=6qqs [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=tRNA (Guanine-1)-methyltransferase [Evidence level]=Indirect evidence [Evidence text]=Multisubdomain structure, where both subdomains participate in dimerization. The C-terminal domain is TRP repressor-like. The structure suggests that the dimer is the functional form of the protein since it has an extensive and tight hydrophobic interface and a large buried surface area. DLS data of the protein solution suggest that the A. aeolicus tRNA (m1G37) methyltransferase is oligomeric (dimer or trimer) in solution (PMID:12773376). The active site is also located at the subunit interface (PMID:14517984). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000723,MF7000724,MF7000725,MF7000726,MF7000727,MF7000728,MF7000729,MF7000730,MF7000731,MF7000732,MF7000733,MF7000734,MF7000735,MF7000736,MF7000737,MF7000738 [UniProt ID chain A]=B1MDI3 [UniProt boundaries chain A]=1-227 [UniProt coverage chain A]=93% [Name chain A]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain A]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain A]=abscessus) [UniProt ID chain B]=B1MDI3 [UniProt boundaries chain B]=1-232 [UniProt coverage chain B]=95% [Name chain B]=tRNA (guanine-N(1)-)-methyltransferase [UniProt sequence chain B]=MKIDVVTIFPEYLQPVRQSLPGKAIDAGLVDVAVHDLRRWTHDVHKSVDDSPYGGGPGMVMKPTVWGDALDEICTSETLLVVPTPAGYPFTQETAWQWSTEDHLVIACGRYEGIDQRVADDAATRMRVREVSIGDYVLNGGEAAALVIIEAVLRLVPGVLGNALSAQEDSHSEGMASLLEGPSYTRPPSWRGMDVPPVLLSGDHAKIAAWRAEQSRQRTIERRPDLLGFDSPTGEHGGDGLS [Source organism chain B]=abscessus) [ExpTech]=X-ray [Resolution]=1.76 [Source organism]=abscessus) [Accession]=MF7000738 [Entry] [Entry number]=923 [Entry name]=MitoNEET [PDB ID]=2qh7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=42-106 [UniProt coverage chain A]=60% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9NZ45 [UniProt boundaries chain B]=43-107 [UniProt coverage chain B]=60% [Name chain B]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain B]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Homo sapiens [Accession]=MF7000739 [Entry] [Entry number]=924 [Entry name]=N-terminal cytoplasmic tethering domain of mitoNEET [PDB ID]=3ew0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=33-107 [UniProt coverage chain A]=69% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9NZ45 [UniProt boundaries chain B]=33-104 [UniProt coverage chain B]=66% [Name chain B]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain B]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Homo sapiens [Accession]=MF7000740 [Entry] [Entry number]=925 [Entry name]=Miner1 [PDB ID]=3fnv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q8N5K1 [UniProt boundaries chain A]=68-134 [UniProt coverage chain A]=49% [Name chain A]=CDGSH iron-sulfur domain-containing protein 2 [UniProt sequence chain A]=MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q8N5K1 [UniProt boundaries chain B]=68-135 [UniProt coverage chain B]=50% [Name chain B]=CDGSH iron-sulfur domain-containing protein 2 [UniProt sequence chain B]=MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Homo sapiens [Accession]=MF7000741 [Entry] [Entry number]=926 [Entry name]=MitoNEET [PDB ID]=3ree [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=32-105 [UniProt coverage chain A]=68% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q9NZ45 [UniProt boundaries chain A-2]=32-105 [UniProt coverage chain A-2]=68% [Name chain A-2]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A-2]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.76 [Source organism]=Homo sapiens [Accession]=MF7000742 [Entry] [Entry number]=927 [Entry name]=Human MitoNEET with 2Fe-2S Coordinating Ligand (mutant) [PDB ID]=3lpq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=33-107 [UniProt coverage chain A]=69% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9NZ45 [UniProt boundaries chain B]=34-107 [UniProt coverage chain B]=68% [Name chain B]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain B]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Homo sapiens [Accession]=MF7000743 [Entry] [Entry number]=928 [Entry name]=Type 3 CDGSH iron-sulfur protein [PDB ID]=3tbo [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=A3MW14 [UniProt boundaries chain A]=3-53 [UniProt coverage chain A]=96% [Name chain A]=Zinc finger, CDGSH-type domain protein [UniProt sequence chain A]=MAVEIRAIENGPYEVKIGGRAIYLCRCGHSGSKPHCDGTHAKVGFKAPGAKIV [Source organism chain A]=Pyrobaculum calidifontis [UniProt ID chain A-2]=A3MW14 [UniProt boundaries chain A-2]=3-53 [UniProt coverage chain A-2]=96% [Name chain A-2]=Zinc finger, CDGSH-type domain protein [UniProt sequence chain A-2]=MAVEIRAIENGPYEVKIGGRAIYLCRCGHSGSKPHCDGTHAKVGFKAPGAKIV [Source organism chain A-2]=Pyrobaculum calidifontis [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Pyrobaculum calidifontis [Accession]=MF7000744 [Entry] [Entry number]=929 [Entry name]=Type 4 CDGSH iron-sulfur protein [PDB ID]=3tbm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q8XVB9 [UniProt boundaries chain A]=5-65 [UniProt coverage chain A]=81% [Name chain A]=Iron-binding zinc finger CDGSH type domain-containing protein [UniProt sequence chain A]=MADDVVITARNNGPYHIKGSFRIVTQGGRELPVEQGQAWLCRCGHSLNKPFCDGSHKRVEFDSNLDAPAAPEPPA [Source organism chain A]=solanacearum) [UniProt ID chain B]=Q8XVB9 [UniProt boundaries chain B]=5-65 [UniProt coverage chain B]=81% [Name chain B]=Iron-binding zinc finger CDGSH type domain-containing protein [UniProt sequence chain B]=MADDVVITARNNGPYHIKGSFRIVTQGGRELPVEQGQAWLCRCGHSLNKPFCDGSHKRVEFDSNLDAPAAPEPPA [Source organism chain B]=solanacearum) [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=solanacearum) [Accession]=MF7000745 [Entry] [Entry number]=930 [Entry name]=Human MitoNEET, mutant M62G [PDB ID]=4f28 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=42-104 [UniProt coverage chain A]=58% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9NZ45 [UniProt boundaries chain B]=43-106 [UniProt coverage chain B]=59% [Name chain B]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain B]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.55 [Source organism]=Homo sapiens [Accession]=MF7000746 [Entry] [Entry number]=931 [Entry name]=Human MitoNEET, double mutant G66A, D67A [PDB ID]=4f2c [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=40-108 [UniProt coverage chain A]=63% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9NZ45 [UniProt boundaries chain B]=42-105 [UniProt coverage chain B]=59% [Name chain B]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain B]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=Homo sapiens [Accession]=MF7000747 [Entry] [Entry number]=932 [Entry name]=NAF1 (MINER1) [PDB ID]=4oo7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q8N5K1 [UniProt boundaries chain A]=69-132 [UniProt coverage chain A]=47% [Name chain A]=CDGSH iron-sulfur domain-containing protein 2 [UniProt sequence chain A]=MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q8N5K1 [UniProt boundaries chain B]=69-135 [UniProt coverage chain B]=49% [Name chain B]=CDGSH iron-sulfur domain-containing protein 2 [UniProt sequence chain B]=MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Homo sapiens [Accession]=MF7000748 [Entry] [Entry number]=933 [Entry name]=MitoNEET with Furosemide [PDB ID]=6de9 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=32-105 [UniProt coverage chain A]=68% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q9NZ45 [UniProt boundaries chain A-2]=32-105 [UniProt coverage chain A-2]=68% [Name chain A-2]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A-2]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Homo sapiens [Accession]=MF7000749 [Entry] [Entry number]=934 [Entry name]=mitoNEET with M1 molecule [PDB ID]=7p0o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, CDGSH type [Sequence domain]=Iron-binding zinc finger CDGSH type [Evidence level]=Indirect evidence [Evidence text]=Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000213,MF7000739,MF7000214,MF7000740,MF7000741,MF7000742,MF7000743,MF7000744,MF7000745,MF7000746,MF7000747,MF7000748,MF7000749,MF7000750 [UniProt ID chain A]=Q9NZ45 [UniProt boundaries chain A]=42-107 [UniProt coverage chain A]=61% [Name chain A]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain A]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9NZ45 [UniProt boundaries chain B]=41-106 [UniProt coverage chain B]=61% [Name chain B]=CDGSH iron-sulfur domain-containing protein 1 [UniProt sequence chain B]=MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Homo sapiens [Accession]=MF7000750 [Entry] [Entry number]=935 [Entry name]=HucR (Deinococcus radiodurans) [PDB ID]=2fbk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=Q9RV71 [UniProt boundaries chain A]=8-179 [UniProt coverage chain A]=95% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MSARMDNDTAALLERIRSDWARLNHGQGPDSDGLTPSAGPMLTLLLLERLHAALGREIERTYAASGLNAAGWDLLLTLYRSAPPEGLRPTELSALAAISGPSTSNRIVRLLEKGLIERREDERDRRSASIRLTPQGRALVTHLLPAHLATTQRVLAPLSAQEQRTLEELAGRMLAGLEQGV [Source organism chain A]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [UniProt ID chain B]=Q9RV71 [UniProt boundaries chain B]=8-179 [UniProt coverage chain B]=95% [Name chain B]=Transcriptional regulator, MarR family [UniProt sequence chain B]=MSARMDNDTAALLERIRSDWARLNHGQGPDSDGLTPSAGPMLTLLLLERLHAALGREIERTYAASGLNAAGWDLLLTLYRSAPPEGLRPTELSALAAISGPSTSNRIVRLLEKGLIERREDERDRRSASIRLTPQGRALVTHLLPAHLATTQRVLAPLSAQEQRTLEELAGRMLAGLEQGV [Source organism chain B]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [Accession]=MF7000751 [Entry] [Entry number]=936 [Entry name]=MepR (Staphylococcus aureus) [PDB ID]=3eco [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=A0A0H3JPT9 [UniProt boundaries chain A]=3-139 [UniProt coverage chain A]=98% [Name chain A]=HTH marR-type domain-containing protein [UniProt sequence chain A]=MEFTYSYLFRMISHEMKQKADQKLEQFDITNEQGHTLGYLYAHQQDGLTQNDIAKALQRTGPTVSNLLRNLERKKLIYRYVDAQDTRRKNIGLTTSGIKLVEAFTSIFDEMEQTLVSQLSEEENEQMKANLTKMLSSLQ [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=A0A0H3JPT9 [UniProt boundaries chain B]=4-139 [UniProt coverage chain B]=97% [Name chain B]=HTH marR-type domain-containing protein [UniProt sequence chain B]=MEFTYSYLFRMISHEMKQKADQKLEQFDITNEQGHTLGYLYAHQQDGLTQNDIAKALQRTGPTVSNLLRNLERKKLIYRYVDAQDTRRKNIGLTTSGIKLVEAFTSIFDEMEQTLVSQLSEEENEQMKANLTKMLSSLQ [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Staphylococcus aureus [Accession]=MF7000752 [Entry] [Entry number]=937 [Entry name]=NMB1585, a MarR family regulator (Neisseria meningitidis) [PDB ID]=3g3z [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=Q9JYH5 [UniProt boundaries chain A]=1-142 [UniProt coverage chain A]=99% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MNQLDQLGTRINLICNVFDKWIGQQDLNYNLFAVLYTLATEGSRTQKHIGEKWSLPKQTVSGVCKTLAGQGLIEWQEGEQDRRKRLLSLTETGKAYAAPLTESAQEFSDKVFATFGDKRTTRLFADLDALAEVMEKTISENKK [Source organism chain A]=Neisseria meningitidis serogroup B [UniProt ID chain B]=Q9JYH5 [UniProt boundaries chain B]=1-142 [UniProt coverage chain B]=99% [Name chain B]=Transcriptional regulator, MarR family [UniProt sequence chain B]=MNQLDQLGTRINLICNVFDKWIGQQDLNYNLFAVLYTLATEGSRTQKHIGEKWSLPKQTVSGVCKTLAGQGLIEWQEGEQDRRKRLLSLTETGKAYAAPLTESAQEFSDKVFATFGDKRTTRLFADLDALAEVMEKTISENKK [Source organism chain B]=Neisseria meningitidis serogroup B [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Neisseria meningitidis serogroup B [Accession]=MF7000753 [Entry] [Entry number]=938 [Entry name]=Transcriptional regulator BldR (Sulfolobus solfataricus) [PDB ID]=3f3x [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=Q97YG9 [UniProt boundaries chain A]=1-140 [UniProt coverage chain A]=97% [Name chain A]=Transcriptional regulator, marR family, putative [UniProt sequence chain A]=MQKIDEKLQLMNTIAKIYRGSIKEFNNRLGKLMNLSYLDFSILKATSEEPRSMVYLANRYFVTQSAITAAVDKLEAKGLVRRIRDSKDRRIVIVEITPKGRQVLLEANEVLRNLVNEMLSDVENVEELLEGLNKILSRIGSSKD [Source organism chain A]= [UniProt ID chain A-2]=Q97YG9 [UniProt boundaries chain A-2]=1-140 [UniProt coverage chain A-2]=97% [Name chain A-2]=Transcriptional regulator, marR family, putative [UniProt sequence chain A-2]=MQKIDEKLQLMNTIAKIYRGSIKEFNNRLGKLMNLSYLDFSILKATSEEPRSMVYLANRYFVTQSAITAAVDKLEAKGLVRRIRDSKDRRIVIVEITPKGRQVLLEANEVLRNLVNEMLSDVENVEELLEGLNKILSRIGSSKD [Source organism chain A-2]= [ExpTech]=X-ray [Resolution]=1.90 [Source organism]= [Accession]=MF7000754 [Entry] [Entry number]=939 [Entry name]=PcaV transcriptional regulator (Streptomyces coelicolor) [PDB ID]=4fht [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=Q9XAM6 [UniProt boundaries chain A]=1-141 [UniProt coverage chain A]=91% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MAAVDLATHPGHLARRLQQAHYLLWNTMVSEETTSPQYAVLNALVAEPGLDQRTVGERVGLDRSTIAEVVSRLGRRGLLDKVRDPQDGRRSLLRLTDEGLRVHRRLGVRIARMNQVFLAPLAADEQAVFFDLIRRVADAAEGLRNPAEPAVAPG [Source organism chain A]=Streptomyces coelicolor [UniProt ID chain B]=Q9XAM6 [UniProt boundaries chain B]=1-141 [UniProt coverage chain B]=91% [Name chain B]=Transcriptional regulator [UniProt sequence chain B]=MAAVDLATHPGHLARRLQQAHYLLWNTMVSEETTSPQYAVLNALVAEPGLDQRTVGERVGLDRSTIAEVVSRLGRRGLLDKVRDPQDGRRSLLRLTDEGLRVHRRLGVRIARMNQVFLAPLAADEQAVFFDLIRRVADAAEGLRNPAEPAVAPG [Source organism chain B]=Streptomyces coelicolor [ExpTech]=X-ray [Resolution]=2.15 [Source organism]=Streptomyces coelicolor [Accession]=MF7000755 [Entry] [Entry number]=940 [Entry name]=PcaV transcriptional regulator (Streptomyces coelicolor) [PDB ID]=4g9y [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=Q9XAM6 [UniProt boundaries chain A]=8-143 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MAAVDLATHPGHLARRLQQAHYLLWNTMVSEETTSPQYAVLNALVAEPGLDQRTVGERVGLDRSTIAEVVSRLGRRGLLDKVRDPQDGRRSLLRLTDEGLRVHRRLGVRIARMNQVFLAPLAADEQAVFFDLIRRVADAAEGLRNPAEPAVAPG [Source organism chain A]=Streptomyces coelicolor [UniProt ID chain A-2]=Q9XAM6 [UniProt boundaries chain A-2]=8-143 [UniProt coverage chain A-2]=88% [Name chain A-2]=Transcriptional regulator [UniProt sequence chain A-2]=MAAVDLATHPGHLARRLQQAHYLLWNTMVSEETTSPQYAVLNALVAEPGLDQRTVGERVGLDRSTIAEVVSRLGRRGLLDKVRDPQDGRRSLLRLTDEGLRVHRRLGVRIARMNQVFLAPLAADEQAVFFDLIRRVADAAEGLRNPAEPAVAPG [Source organism chain A-2]=Streptomyces coelicolor [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Streptomyces coelicolor [Accession]=MF7000756 [Entry] [Entry number]=941 [Entry name]=CouR with p-coumaroyl-CoA (Rhodococcus jostii RHA1) [PDB ID]=5cyv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=Q0S6D0 [UniProt boundaries chain A]=4-146 [UniProt coverage chain A]=97% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MAESQALSDDIGFLLSRVGGMVLGAVNKALVPTGLRVRSYSVLVLACEQAEGVNQRGVAATMGLDPSQIVGLVDELEERGLVVRTLDPSDRRNKLIAATEEGRRLRDDAKARVDAAHGRYFEGIPDTVVNQMRDTLQSIAFPTFVE [Source organism chain A]=Rhodococcus jostii [UniProt ID chain B]=Q0S6D0 [UniProt boundaries chain B]=4-146 [UniProt coverage chain B]=97% [Name chain B]=Transcriptional regulator [UniProt sequence chain B]=MAESQALSDDIGFLLSRVGGMVLGAVNKALVPTGLRVRSYSVLVLACEQAEGVNQRGVAATMGLDPSQIVGLVDELEERGLVVRTLDPSDRRNKLIAATEEGRRLRDDAKARVDAAHGRYFEGIPDTVVNQMRDTLQSIAFPTFVE [Source organism chain B]=Rhodococcus jostii [ExpTech]=X-ray [Resolution]=1.52 [Source organism]=Rhodococcus jostii [Accession]=MF7000757 [Entry] [Entry number]=942 [Entry name]=HucR mutant (HucR-E48Q) (Deinococcus radiodurans) [PDB ID]=5dd8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=Q9RV71 [UniProt boundaries chain A]=8-179 [UniProt coverage chain A]=95% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MSARMDNDTAALLERIRSDWARLNHGQGPDSDGLTPSAGPMLTLLLLERLHAALGREIERTYAASGLNAAGWDLLLTLYRSAPPEGLRPTELSALAAISGPSTSNRIVRLLEKGLIERREDERDRRSASIRLTPQGRALVTHLLPAHLATTQRVLAPLSAQEQRTLEELAGRMLAGLEQGV [Source organism chain A]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [UniProt ID chain B]=Q9RV71 [UniProt boundaries chain B]=8-179 [UniProt coverage chain B]=95% [Name chain B]=Transcriptional regulator, MarR family [UniProt sequence chain B]=MSARMDNDTAALLERIRSDWARLNHGQGPDSDGLTPSAGPMLTLLLLERLHAALGREIERTYAASGLNAAGWDLLLTLYRSAPPEGLRPTELSALAAISGPSTSNRIVRLLEKGLIERREDERDRRSASIRLTPQGRALVTHLLPAHLATTQRVLAPLSAQEQRTLEELAGRMLAGLEQGV [Source organism chain B]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [Accession]=MF7000758 [Entry] [Entry number]=943 [Entry name]=HucR with urate [PDB ID]=7xl9 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (MarR type II) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000751,MF7000156,MF7000752,MF7000753,MF7000754,MF7000755,MF7000756,MF7000757,MF7000758,MF7000759,MF7000256 [UniProt ID chain A]=Q9RV71 [UniProt boundaries chain A]=8-181 [UniProt coverage chain A]=96% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MSARMDNDTAALLERIRSDWARLNHGQGPDSDGLTPSAGPMLTLLLLERLHAALGREIERTYAASGLNAAGWDLLLTLYRSAPPEGLRPTELSALAAISGPSTSNRIVRLLEKGLIERREDERDRRSASIRLTPQGRALVTHLLPAHLATTQRVLAPLSAQEQRTLEELAGRMLAGLEQGV [Source organism chain A]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [UniProt ID chain A-2]=Q9RV71 [UniProt boundaries chain A-2]=8-181 [UniProt coverage chain A-2]=96% [Name chain A-2]=Transcriptional regulator, MarR family [UniProt sequence chain A-2]=MSARMDNDTAALLERIRSDWARLNHGQGPDSDGLTPSAGPMLTLLLLERLHAALGREIERTYAASGLNAAGWDLLLTLYRSAPPEGLRPTELSALAAISGPSTSNRIVRLLEKGLIERREDERDRRSASIRLTPQGRALVTHLLPAHLATTQRVLAPLSAQEQRTLEELAGRMLAGLEQGV [Source organism chain A-2]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [ExpTech]=X-ray [Resolution]=2.58 [Source organism]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [Accession]=MF7000759 [Entry] [Entry number]=944 [Entry name]=Catechol 1,2-dioxygenase with catechol (Acinetobacter sp. ADP 1) [PDB ID]=1dlt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=P07773 [UniProt boundaries chain A]=3-311 [UniProt coverage chain A]=99% [Name chain A]=Catechol 1,2-dioxygenase [UniProt sequence chain A]=MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV [Source organism chain A]=Acinetobacter baylyi [UniProt ID chain B]=P07773 [UniProt boundaries chain B]=3-311 [UniProt coverage chain B]=99% [Name chain B]=Catechol 1,2-dioxygenase [UniProt sequence chain B]=MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV [Source organism chain B]=Acinetobacter baylyi [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Acinetobacter baylyi [Accession]=MF7000760 [Entry] [Entry number]=945 [Entry name]=Catechol 1,2-dioxygenase (Acinetobacter calcoaceticus) [PDB ID]=1dlm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=P07773 [UniProt boundaries chain A]=3-311 [UniProt coverage chain A]=99% [Name chain A]=Catechol 1,2-dioxygenase [UniProt sequence chain A]=MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV [Source organism chain A]=Acinetobacter baylyi [UniProt ID chain B]=P07773 [UniProt boundaries chain B]=3-311 [UniProt coverage chain B]=99% [Name chain B]=Catechol 1,2-dioxygenase [UniProt sequence chain B]=MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV [Source organism chain B]=Acinetobacter baylyi [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Acinetobacter baylyi [Accession]=MF7000761 [Entry] [Entry number]=946 [Entry name]=Catechol 1,2-dioxygenase with Hg (Acinetobacter sp. ADP1) [PDB ID]=1dlq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=P07773 [UniProt boundaries chain A]=3-311 [UniProt coverage chain A]=99% [Name chain A]=Catechol 1,2-dioxygenase [UniProt sequence chain A]=MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV [Source organism chain A]=Acinetobacter baylyi [UniProt ID chain B]=P07773 [UniProt boundaries chain B]=3-311 [UniProt coverage chain B]=99% [Name chain B]=Catechol 1,2-dioxygenase [UniProt sequence chain B]=MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV [Source organism chain B]=Acinetobacter baylyi [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Acinetobacter baylyi [Accession]=MF7000762 [Entry] [Entry number]=947 [Entry name]=Catechol 1,2-dioxygenase with 4-methylcatechol (Acinetobacter sp. ADP1) [PDB ID]=1dmh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=P07773 [UniProt boundaries chain A]=3-311 [UniProt coverage chain A]=99% [Name chain A]=Catechol 1,2-dioxygenase [UniProt sequence chain A]=MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV [Source organism chain A]=Acinetobacter baylyi [UniProt ID chain B]=P07773 [UniProt boundaries chain B]=3-311 [UniProt coverage chain B]=99% [Name chain B]=Catechol 1,2-dioxygenase [UniProt sequence chain B]=MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV [Source organism chain B]=Acinetobacter baylyi [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Acinetobacter baylyi [Accession]=MF7000763 [Entry] [Entry number]=948 [Entry name]=Catechol 1,2-dioxygenase (Pseudomonas arvilla C-1) [PDB ID]=2azq [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=Q51433 [UniProt boundaries chain A]=3-311 [UniProt coverage chain A]=99% [Name chain A]=catechol 1,2-dioxygenase [UniProt sequence chain A]=MTVKISHTADIQAFFNQVAGLDHAEGKPRFKQIILRVLQDTARLIEDLEITEDEFWHAVDYLNRLGGRNEAGLLAAGLGIEHFLDLLQDAKDAEAGLGGGTPRTIEGPLYVAGAPLAQGEVRMDDGTDPGVVMFLQGQVFDANGKPLAGATVDLWHANTQGTYSYFDSTQSEFNLRRRIITDAEGRYRARSIVPSGYGCDPQGPTQECLDLLGRHGQRPAHVHFFISAPGHRHLTTQINFAGDKYLWDDFAYATRDGLIGELRFVEDAAAARDRGVQGERFAELSFDFRLQGAQSPDAEERSHRPRALQEG [Source organism chain A]=Pseudomonas putida [UniProt ID chain A-2]=Q51433 [UniProt boundaries chain A-2]=3-311 [UniProt coverage chain A-2]=99% [Name chain A-2]=catechol 1,2-dioxygenase [UniProt sequence chain A-2]=MTVKISHTADIQAFFNQVAGLDHAEGKPRFKQIILRVLQDTARLIEDLEITEDEFWHAVDYLNRLGGRNEAGLLAAGLGIEHFLDLLQDAKDAEAGLGGGTPRTIEGPLYVAGAPLAQGEVRMDDGTDPGVVMFLQGQVFDANGKPLAGATVDLWHANTQGTYSYFDSTQSEFNLRRRIITDAEGRYRARSIVPSGYGCDPQGPTQECLDLLGRHGQRPAHVHFFISAPGHRHLTTQINFAGDKYLWDDFAYATRDGLIGELRFVEDAAAARDRGVQGERFAELSFDFRLQGAQSPDAEERSHRPRALQEG [Source organism chain A-2]=Pseudomonas putida [ExpTech]=X-ray [Resolution]=2.65 [Source organism]=Pseudomonas putida [Accession]=MF7000764 [Entry] [Entry number]=949 [Entry name]=Catechol 1,2 dioxygenase, wild type (Acinetobacter radioresistens) [PDB ID]=2xsr [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=Q9F103 [UniProt boundaries chain A]=2-306 [UniProt coverage chain A]=99% [Name chain A]=catechol 1,2-dioxygenase [UniProt sequence chain A]=MNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA [Source organism chain A]=Acinetobacter radioresistens [UniProt ID chain A-2]=Q9F103 [UniProt boundaries chain A-2]=2-306 [UniProt coverage chain A-2]=99% [Name chain A-2]=catechol 1,2-dioxygenase [UniProt sequence chain A-2]=MNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA [Source organism chain A-2]=Acinetobacter radioresistens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Acinetobacter radioresistens [Accession]=MF7000765 [Entry] [Entry number]=950 [Entry name]=Catechol 1,2 dioxygenase, mutant A72G (Acinetobacter radioresistens) [PDB ID]=2xsu [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=Q9F103 [UniProt boundaries chain A]=2-306 [UniProt coverage chain A]=99% [Name chain A]=catechol 1,2-dioxygenase [UniProt sequence chain A]=MNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA [Source organism chain A]=Acinetobacter radioresistens [UniProt ID chain A-2]=Q9F103 [UniProt boundaries chain A-2]=2-306 [UniProt coverage chain A-2]=99% [Name chain A-2]=catechol 1,2-dioxygenase [UniProt sequence chain A-2]=MNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA [Source organism chain A-2]=Acinetobacter radioresistens [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Acinetobacter radioresistens [Accession]=MF7000766 [Entry] [Entry number]=951 [Entry name]=Catechol 1,2 dioxygenase, mutant L69A (Acinetobacter radioresistens) [PDB ID]=2xsv [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=Q9F103 [UniProt boundaries chain A]=2-306 [UniProt coverage chain A]=99% [Name chain A]=catechol 1,2-dioxygenase [UniProt sequence chain A]=MNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA [Source organism chain A]=Acinetobacter radioresistens [UniProt ID chain A-2]=Q9F103 [UniProt boundaries chain A-2]=2-306 [UniProt coverage chain A-2]=99% [Name chain A-2]=catechol 1,2-dioxygenase [UniProt sequence chain A-2]=MNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA [Source organism chain A-2]=Acinetobacter radioresistens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Acinetobacter radioresistens [Accession]=MF7000767 [Entry] [Entry number]=952 [Entry name]=4-chlorocatechol dioxygenase with pyrogallol (Rhodococcus opacus 1CP) [PDB ID]=3o6r [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=O67987 [UniProt boundaries chain A]=2-257 [UniProt coverage chain A]=99% [Name chain A]=Chlorocatechol 1,2-dioxygenase [UniProt sequence chain A]=MANTRVIELFDEFTDLIRDFIVRHEITTPEYETIMQYMISVGEAGEWPLWLDAFFETTVDSVSYGKGNWTSSAIQGPFFKEGAPLLTGKPATLPMRADEPGDRMRFTGSVRDTSGTPITGAVIDVWHSTNDGNYSFFSPALPDQYLLRGRVVPAEDGSIEFHSIRPVPYEIPKAGPTGQLMNSYLGRHSWRPAHIHIRITADGYRPLITQLYFEGDPYLDSDSCSAVKSELVLPVNKIDIDGETWQLVDFNFILQHN [Source organism chain A]=Rhodococcus opacus [UniProt ID chain B]=O67987 [UniProt boundaries chain B]=2-257 [UniProt coverage chain B]=99% [Name chain B]=Chlorocatechol 1,2-dioxygenase [UniProt sequence chain B]=MANTRVIELFDEFTDLIRDFIVRHEITTPEYETIMQYMISVGEAGEWPLWLDAFFETTVDSVSYGKGNWTSSAIQGPFFKEGAPLLTGKPATLPMRADEPGDRMRFTGSVRDTSGTPITGAVIDVWHSTNDGNYSFFSPALPDQYLLRGRVVPAEDGSIEFHSIRPVPYEIPKAGPTGQLMNSYLGRHSWRPAHIHIRITADGYRPLITQLYFEGDPYLDSDSCSAVKSELVLPVNKIDIDGETWQLVDFNFILQHN [Source organism chain B]=Rhodococcus opacus [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Rhodococcus opacus [Accession]=MF7000768 [Entry] [Entry number]=953 [Entry name]=4-chlorocatechol dioxygenase with 3,5-dichlorocatechol (Rhodococcus opacus 1CP) [PDB ID]=3o32 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=O67987 [UniProt boundaries chain A]=2-257 [UniProt coverage chain A]=99% [Name chain A]=Chlorocatechol 1,2-dioxygenase [UniProt sequence chain A]=MANTRVIELFDEFTDLIRDFIVRHEITTPEYETIMQYMISVGEAGEWPLWLDAFFETTVDSVSYGKGNWTSSAIQGPFFKEGAPLLTGKPATLPMRADEPGDRMRFTGSVRDTSGTPITGAVIDVWHSTNDGNYSFFSPALPDQYLLRGRVVPAEDGSIEFHSIRPVPYEIPKAGPTGQLMNSYLGRHSWRPAHIHIRITADGYRPLITQLYFEGDPYLDSDSCSAVKSELVLPVNKIDIDGETWQLVDFNFILQHN [Source organism chain A]=Rhodococcus opacus [UniProt ID chain B]=O67987 [UniProt boundaries chain B]=3-257 [UniProt coverage chain B]=99% [Name chain B]=Chlorocatechol 1,2-dioxygenase [UniProt sequence chain B]=MANTRVIELFDEFTDLIRDFIVRHEITTPEYETIMQYMISVGEAGEWPLWLDAFFETTVDSVSYGKGNWTSSAIQGPFFKEGAPLLTGKPATLPMRADEPGDRMRFTGSVRDTSGTPITGAVIDVWHSTNDGNYSFFSPALPDQYLLRGRVVPAEDGSIEFHSIRPVPYEIPKAGPTGQLMNSYLGRHSWRPAHIHIRITADGYRPLITQLYFEGDPYLDSDSCSAVKSELVLPVNKIDIDGETWQLVDFNFILQHN [Source organism chain B]=Rhodococcus opacus [ExpTech]=X-ray [Resolution]=2.85 [Source organism]=Rhodococcus opacus [Accession]=MF7000769 [Entry] [Entry number]=954 [Entry name]=4-chlorocatechol dioxygenase with protocatechuate (Rhodococcus opacus 1CP) [PDB ID]=3o5u [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=O67987 [UniProt boundaries chain A]=2-257 [UniProt coverage chain A]=99% [Name chain A]=Chlorocatechol 1,2-dioxygenase [UniProt sequence chain A]=MANTRVIELFDEFTDLIRDFIVRHEITTPEYETIMQYMISVGEAGEWPLWLDAFFETTVDSVSYGKGNWTSSAIQGPFFKEGAPLLTGKPATLPMRADEPGDRMRFTGSVRDTSGTPITGAVIDVWHSTNDGNYSFFSPALPDQYLLRGRVVPAEDGSIEFHSIRPVPYEIPKAGPTGQLMNSYLGRHSWRPAHIHIRITADGYRPLITQLYFEGDPYLDSDSCSAVKSELVLPVNKIDIDGETWQLVDFNFILQHN [Source organism chain A]=Rhodococcus opacus [UniProt ID chain B]=O67987 [UniProt boundaries chain B]=2-257 [UniProt coverage chain B]=99% [Name chain B]=Chlorocatechol 1,2-dioxygenase [UniProt sequence chain B]=MANTRVIELFDEFTDLIRDFIVRHEITTPEYETIMQYMISVGEAGEWPLWLDAFFETTVDSVSYGKGNWTSSAIQGPFFKEGAPLLTGKPATLPMRADEPGDRMRFTGSVRDTSGTPITGAVIDVWHSTNDGNYSFFSPALPDQYLLRGRVVPAEDGSIEFHSIRPVPYEIPKAGPTGQLMNSYLGRHSWRPAHIHIRITADGYRPLITQLYFEGDPYLDSDSCSAVKSELVLPVNKIDIDGETWQLVDFNFILQHN [Source organism chain B]=Rhodococcus opacus [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Rhodococcus opacus [Accession]=MF7000770 [Entry] [Entry number]=955 [Entry name]=4-chlorocatechol dioxygenase with hydroxyquinol (Rhodococcus opacus 1CP) [PDB ID]=3o6j [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Dioxygenase [Evidence level]=Indirect evidence [Evidence text]=A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000760,MF7000761,MF7000762,MF7000763,MF7000764,MF7000765,MF7000766,MF7000767,MF7000768,MF7000769,MF7000770,MF7000771 [UniProt ID chain A]=O67987 [UniProt boundaries chain A]=2-257 [UniProt coverage chain A]=99% [Name chain A]=Chlorocatechol 1,2-dioxygenase [UniProt sequence chain A]=MANTRVIELFDEFTDLIRDFIVRHEITTPEYETIMQYMISVGEAGEWPLWLDAFFETTVDSVSYGKGNWTSSAIQGPFFKEGAPLLTGKPATLPMRADEPGDRMRFTGSVRDTSGTPITGAVIDVWHSTNDGNYSFFSPALPDQYLLRGRVVPAEDGSIEFHSIRPVPYEIPKAGPTGQLMNSYLGRHSWRPAHIHIRITADGYRPLITQLYFEGDPYLDSDSCSAVKSELVLPVNKIDIDGETWQLVDFNFILQHN [Source organism chain A]=Rhodococcus opacus [UniProt ID chain B]=O67987 [UniProt boundaries chain B]=2-257 [UniProt coverage chain B]=99% [Name chain B]=Chlorocatechol 1,2-dioxygenase [UniProt sequence chain B]=MANTRVIELFDEFTDLIRDFIVRHEITTPEYETIMQYMISVGEAGEWPLWLDAFFETTVDSVSYGKGNWTSSAIQGPFFKEGAPLLTGKPATLPMRADEPGDRMRFTGSVRDTSGTPITGAVIDVWHSTNDGNYSFFSPALPDQYLLRGRVVPAEDGSIEFHSIRPVPYEIPKAGPTGQLMNSYLGRHSWRPAHIHIRITADGYRPLITQLYFEGDPYLDSDSCSAVKSELVLPVNKIDIDGETWQLVDFNFILQHN [Source organism chain B]=Rhodococcus opacus [ExpTech]=X-ray [Resolution]=2.90 [Source organism]=Rhodococcus opacus [Accession]=MF7000771 [Entry] [Entry number]=956 [Entry name]=Selenomethionine variant of griffithsin [PDB ID]=2gux [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=1-121 [UniProt coverage chain A]=100% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain A-2]=P84801 [UniProt boundaries chain A-2]=1-121 [UniProt coverage chain A-2]=100% [Name chain A-2]=Griffithsin [UniProt sequence chain A-2]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A-2]=Griffithsia sp [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Griffithsia sp [Accession]=MF7000772 [Entry] [Entry number]=957 [Entry name]=Griffithsin [PDB ID]=2gty [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=1-121 [UniProt coverage chain A]=100% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=1-121 [UniProt coverage chain B]=100% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=1.30 [Source organism]=Griffithsia sp [Accession]=MF7000773 [Entry] [Entry number]=958 [Entry name]=Griffithsin with mannose at 0.94 A resolution [PDB ID]=2gud [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=1-121 [UniProt coverage chain A]=100% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=1-121 [UniProt coverage chain B]=100% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=0.94 [Source organism]=Griffithsia sp [Accession]=MF7000774 [Entry] [Entry number]=959 [Entry name]=Griffithsin with N-acetylglucosamine [PDB ID]=2gue [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=1-121 [UniProt coverage chain A]=100% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=1-121 [UniProt coverage chain B]=100% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=2.02 [Source organism]=Griffithsia sp [Accession]=MF7000775 [Entry] [Entry number]=960 [Entry name]=Griffithsin with 6alpha-mannobiose [PDB ID]=2hyq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=1-121 [UniProt coverage chain A]=100% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=1-121 [UniProt coverage chain B]=100% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Griffithsia sp [Accession]=MF7000776 [Entry] [Entry number]=961 [Entry name]=Griffithsin with maltose [PDB ID]=2hyr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=1-121 [UniProt coverage chain A]=100% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=1-121 [UniProt coverage chain B]=100% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=1.51 [Source organism]=Griffithsia sp [Accession]=MF7000777 [Entry] [Entry number]=962 [Entry name]=Griffithsin with N-acetylglucosamine [PDB ID]=2nu5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=1-121 [UniProt coverage chain A]=100% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=1-121 [UniProt coverage chain B]=100% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=1.56 [Source organism]=Griffithsia sp [Accession]=MF7000778 [Entry] [Entry number]=963 [Entry name]=Griffithsin with glucose [PDB ID]=2nuo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=1-121 [UniProt coverage chain A]=100% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=1-121 [UniProt coverage chain B]=100% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Griffithsia sp [Accession]=MF7000779 [Entry] [Entry number]=964 [Entry name]=Griffithsin (Y28A/Y68A/Y110A variant) [PDB ID]=7ria [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=2-121 [UniProt coverage chain A]=99% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=2-121 [UniProt coverage chain B]=99% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Griffithsia sp [Accession]=MF7000780 [Entry] [Entry number]=965 [Entry name]=Griffithsin, Y28W/Y68W/Y110W mutant [PDB ID]=7ric [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=2-121 [UniProt coverage chain A]=99% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain A-2]=P84801 [UniProt boundaries chain A-2]=2-121 [UniProt coverage chain A-2]=99% [Name chain A-2]=Griffithsin [UniProt sequence chain A-2]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A-2]=Griffithsia sp [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Griffithsia sp [Accession]=MF7000781 [Entry] [Entry number]=966 [Entry name]=Griffithsin, Y28W mutant [PDB ID]=7rkg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=2-121 [UniProt coverage chain A]=99% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=2-121 [UniProt coverage chain B]=99% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Griffithsia sp [Accession]=MF7000782 [Entry] [Entry number]=967 [Entry name]=Griffithsin, S10Y/S42Y/S88Y mutant [PDB ID]=7rki [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Homodimeric lectin [Sequence domain]=Jacalin-like lectin domain [Evidence level]=Indirect evidence [Evidence text]=Griffithsin forms an intimate, domain-swapped dimer, in which the first two β strands of one chain complete a beta prism consisting of three four-stranded sheets of the other chain. It is not clear whether a monomeric form does (or even could) exist. Griffithsin was shown to exist as a homodimer in solution by size-exclusion chromatography (PMID:16843894). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000772,MF7000773,MF7000774,MF7000775,MF7000776,MF7000777,MF7000778,MF7000779,MF7000780,MF7000781,MF7000782,MF7000783 [UniProt ID chain A]=P84801 [UniProt boundaries chain A]=2-121 [UniProt coverage chain A]=99% [Name chain A]=Griffithsin [UniProt sequence chain A]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain A]=Griffithsia sp [UniProt ID chain B]=P84801 [UniProt boundaries chain B]=2-121 [UniProt coverage chain B]=99% [Name chain B]=Griffithsin [UniProt sequence chain B]=SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY [Source organism chain B]=Griffithsia sp [ExpTech]=X-ray [Resolution]=2.09 [Source organism]=Griffithsia sp [Accession]=MF7000783 [Entry] [Entry number]=968 [Entry name]=CBS domain-containing protein (tm0935) (Thermotoga maritima) [PDB ID]=1o50 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=Q9X033 [UniProt boundaries chain A]=1-145 [UniProt coverage chain A]=100% [Name chain A]=CBS domain-containing protein [UniProt sequence chain A]=MKVKDVCKLISLKPTVVEEDTPIEEIVDRILEDPVTRTVYVARDNKLVGMIPVMHLLKVSGFHFFGFIPKEELIRSSMKRLIAKNASEIMLDPVYVHMDTPLEEALKLMIDNNIQEMPVVDEKGEIVGDLNSLEILLALWKGREK [Source organism chain A]=/ MSB8) [UniProt ID chain A-2]=Q9X033 [UniProt boundaries chain A-2]=1-145 [UniProt coverage chain A-2]=100% [Name chain A-2]=CBS domain-containing protein [UniProt sequence chain A-2]=MKVKDVCKLISLKPTVVEEDTPIEEIVDRILEDPVTRTVYVARDNKLVGMIPVMHLLKVSGFHFFGFIPKEELIRSSMKRLIAKNASEIMLDPVYVHMDTPLEEALKLMIDNNIQEMPVVDEKGEIVGDLNSLEILLALWKGREK [Source organism chain A-2]=/ MSB8) [ExpTech]=X-ray [Resolution]=1.87 [Source organism]=/ MSB8) [Accession]=MF7000784 [Entry] [Entry number]=969 [Entry name]=Yeast Bateman2 domain of Snf4 [PDB ID]=2nye [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=P12904 [UniProt boundaries chain A]=181-322 [UniProt coverage chain A]=44% [Name chain A]=5'-AMP-activated protein kinase subunit gamma [UniProt sequence chain A]=MKPTQDSQEKVSIEQQLAVESIRKFLNSKTSYDVLPVSYRLIVLDTSLLVKKSLNVLLQNSIVSAPLWDSKTSRFAGLLTTTDFINVIQYYFSNPDKFELVDKLQLDGLKDIERALGVDQLDTASIHPSRPLFEACLKMLESRSGRIPLIDQDEETHREIVVSVLTQYRILKFVALNCRETHFLKIPIGDLNIITQDNMKSCQMTTPVIDVIQMLTQGRVSSVPIIDENGYLINVYEAYDVLGLIKGGIYNDLSLSVGEALMRRSDDFEGVYTCTKNDKLSTIMDNIRKARVHRFFVVDDVGRLVGVLTLSDILKYILLGSN [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P12904 [UniProt boundaries chain B]=181-322 [UniProt coverage chain B]=44% [Name chain B]=5'-AMP-activated protein kinase subunit gamma [UniProt sequence chain B]=MKPTQDSQEKVSIEQQLAVESIRKFLNSKTSYDVLPVSYRLIVLDTSLLVKKSLNVLLQNSIVSAPLWDSKTSRFAGLLTTTDFINVIQYYFSNPDKFELVDKLQLDGLKDIERALGVDQLDTASIHPSRPLFEACLKMLESRSGRIPLIDQDEETHREIVVSVLTQYRILKFVALNCRETHFLKIPIGDLNIITQDNMKSCQMTTPVIDVIQMLTQGRVSSVPIIDENGYLINVYEAYDVLGLIKGGIYNDLSLSVGEALMRRSDDFEGVYTCTKNDKLSTIMDNIRKARVHRFFVVDDVGRLVGVLTLSDILKYILLGSN [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000785 [Entry] [Entry number]=970 [Entry name]=Yeast Bateman2 domain of Snf4 [PDB ID]=2nyc [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=P12904 [UniProt boundaries chain A]=181-320 [UniProt coverage chain A]=43% [Name chain A]=5'-AMP-activated protein kinase subunit gamma [UniProt sequence chain A]=MKPTQDSQEKVSIEQQLAVESIRKFLNSKTSYDVLPVSYRLIVLDTSLLVKKSLNVLLQNSIVSAPLWDSKTSRFAGLLTTTDFINVIQYYFSNPDKFELVDKLQLDGLKDIERALGVDQLDTASIHPSRPLFEACLKMLESRSGRIPLIDQDEETHREIVVSVLTQYRILKFVALNCRETHFLKIPIGDLNIITQDNMKSCQMTTPVIDVIQMLTQGRVSSVPIIDENGYLINVYEAYDVLGLIKGGIYNDLSLSVGEALMRRSDDFEGVYTCTKNDKLSTIMDNIRKARVHRFFVVDDVGRLVGVLTLSDILKYILLGSN [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=P12904 [UniProt boundaries chain A-2]=181-320 [UniProt coverage chain A-2]=43% [Name chain A-2]=5'-AMP-activated protein kinase subunit gamma [UniProt sequence chain A-2]=MKPTQDSQEKVSIEQQLAVESIRKFLNSKTSYDVLPVSYRLIVLDTSLLVKKSLNVLLQNSIVSAPLWDSKTSRFAGLLTTTDFINVIQYYFSNPDKFELVDKLQLDGLKDIERALGVDQLDTASIHPSRPLFEACLKMLESRSGRIPLIDQDEETHREIVVSVLTQYRILKFVALNCRETHFLKIPIGDLNIITQDNMKSCQMTTPVIDVIQMLTQGRVSSVPIIDENGYLINVYEAYDVLGLIKGGIYNDLSLSVGEALMRRSDDFEGVYTCTKNDKLSTIMDNIRKARVHRFFVVDDVGRLVGVLTLSDILKYILLGSN [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000786 [Entry] [Entry number]=971 [Entry name]=CBS domain pair from the regulatory gamma1 subunit of human AMPK with AMP [PDB ID]=2uv4 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=P54619 [UniProt boundaries chain A]=182-324 [UniProt coverage chain A]=43% [Name chain A]=5'-AMP-activated protein kinase subunit gamma-1 [UniProt sequence chain A]=METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P54619 [UniProt boundaries chain A-2]=182-324 [UniProt coverage chain A-2]=43% [Name chain A-2]=5'-AMP-activated protein kinase subunit gamma-1 [UniProt sequence chain A-2]=METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.33 [Source organism]=Homo sapiens [Accession]=MF7000787 [Entry] [Entry number]=972 [Entry name]=CBS domain pair from the regulatory gamma1 subunit of human AMPK with AMP [PDB ID]=2uv5 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=P54619 [UniProt boundaries chain A]=182-324 [UniProt coverage chain A]=43% [Name chain A]=5'-AMP-activated protein kinase subunit gamma-1 [UniProt sequence chain A]=METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P54619 [UniProt boundaries chain A-2]=182-324 [UniProt coverage chain A-2]=43% [Name chain A-2]=5'-AMP-activated protein kinase subunit gamma-1 [UniProt sequence chain A-2]=METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.69 [Source organism]=Homo sapiens [Accession]=MF7000788 [Entry] [Entry number]=973 [Entry name]=CBS domain pair from the regulatory gamma1 subunit of human AMPK with AMP [PDB ID]=2uv6 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=P54619 [UniProt boundaries chain A]=182-324 [UniProt coverage chain A]=43% [Name chain A]=5'-AMP-activated protein kinase subunit gamma-1 [UniProt sequence chain A]=METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P54619 [UniProt boundaries chain A-2]=182-324 [UniProt coverage chain A-2]=43% [Name chain A-2]=5'-AMP-activated protein kinase subunit gamma-1 [UniProt sequence chain A-2]=METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000789 [Entry] [Entry number]=974 [Entry name]=CBS domain pair from the regulatory gamma1 subunit of human AMPK with AMP [PDB ID]=2uv7 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=P54619 [UniProt boundaries chain A]=182-324 [UniProt coverage chain A]=43% [Name chain A]=5'-AMP-activated protein kinase subunit gamma-1 [UniProt sequence chain A]=METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P54619 [UniProt boundaries chain A-2]=182-324 [UniProt coverage chain A-2]=43% [Name chain A-2]=5'-AMP-activated protein kinase subunit gamma-1 [UniProt sequence chain A-2]=METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000790 [Entry] [Entry number]=975 [Entry name]=CBS domain protein PAE2072 (Pyrobaculum aerophilum) [PDB ID]=2rih [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=Q8ZVX8 [UniProt boundaries chain A]=2-132 [UniProt coverage chain A]=94% [Name chain A]=Conserved protein with 2 CBS domains [UniProt sequence chain A]=MIRTSELLKRPPVSLPETATIREVATELAKNRVGLAVLTARDNPKRPVAVVSERDILRAVAQRLDLDGPAMPIANSPITVLDTDPVHVAAEKMRRHNIRHVVVVNKNGELVGVLSIRDLCFERAILLELATAEVPATP [Source organism chain A]=104966 / NBRC 100827 / IM2) [UniProt ID chain B]=Q8ZVX8 [UniProt boundaries chain B]=2-131 [UniProt coverage chain B]=94% [Name chain B]=Conserved protein with 2 CBS domains [UniProt sequence chain B]=MIRTSELLKRPPVSLPETATIREVATELAKNRVGLAVLTARDNPKRPVAVVSERDILRAVAQRLDLDGPAMPIANSPITVLDTDPVHVAAEKMRRHNIRHVVVVNKNGELVGVLSIRDLCFERAILLELATAEVPATP [Source organism chain B]=104966 / NBRC 100827 / IM2) [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=104966 / NBRC 100827 / IM2) [Accession]=MF7000791 [Entry] [Entry number]=976 [Entry name]=CBS domain pair of protein MJ0100 with 5 -methylthioadenosine and S-adenosyl-L-methionine [PDB ID]=3kpc [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=Q57564 [UniProt boundaries chain A]=386-509 [UniProt coverage chain A]=24% [Name chain A]=L-aspartate semialdehyde sulfurtransferase [UniProt sequence chain A]=MIMKTIKEINEKIKKGEAVVVTAEEMIKIVEEEGAKRAADYVDVVTTGTFGAMCSSGVFINFGHSDPPIKMLRIYLNNVEAYGGLAAVDAYIGAAQPNEDPDVDIDYGGAHVIEDLVRGKEVELYAEGYTTDCYPRKEVNVRITLDDVNQAIMVNPRNCYQTYAAATNSREEKIYTYMGILLPEYNNVHYSGAGQLNPLQNDYNPETKSFNTIGIGTRIFLGGGIGYVIGEGTQHNPPFGTLMVKGDLKQMNPKFIRAATMPRYGSTLYVGIGIPIPVLNEKIAERCAIRDEDIEVPIYDYGFPRRDRPLIAKTNYKVLRSGKITLNVNIDGKDVEKTVKTGSVSSYKMAREVAETLKQWILDGKFLLTERVDTLGRAENKPMKSPITLVKDILSKPPITAHSNISIMEAAKILIKHNINHLPIVDEHGKLVGIITSWDIAKALAQNKKTIEEIMTRNVITAHEDEPVDHVAIKMSKYNISGVPVVDDYRRVVGIVTSEDISRLFGGKK [Source organism chain A]=10045 / NBRC 100440) [UniProt ID chain A-2]=Q57564 [UniProt boundaries chain A-2]=386-509 [UniProt coverage chain A-2]=24% [Name chain A-2]=L-aspartate semialdehyde sulfurtransferase [UniProt sequence chain A-2]=MIMKTIKEINEKIKKGEAVVVTAEEMIKIVEEEGAKRAADYVDVVTTGTFGAMCSSGVFINFGHSDPPIKMLRIYLNNVEAYGGLAAVDAYIGAAQPNEDPDVDIDYGGAHVIEDLVRGKEVELYAEGYTTDCYPRKEVNVRITLDDVNQAIMVNPRNCYQTYAAATNSREEKIYTYMGILLPEYNNVHYSGAGQLNPLQNDYNPETKSFNTIGIGTRIFLGGGIGYVIGEGTQHNPPFGTLMVKGDLKQMNPKFIRAATMPRYGSTLYVGIGIPIPVLNEKIAERCAIRDEDIEVPIYDYGFPRRDRPLIAKTNYKVLRSGKITLNVNIDGKDVEKTVKTGSVSSYKMAREVAETLKQWILDGKFLLTERVDTLGRAENKPMKSPITLVKDILSKPPITAHSNISIMEAAKILIKHNINHLPIVDEHGKLVGIITSWDIAKALAQNKKTIEEIMTRNVITAHEDEPVDHVAIKMSKYNISGVPVVDDYRRVVGIVTSEDISRLFGGKK [Source organism chain A-2]=10045 / NBRC 100440) [ExpTech]=X-ray [Resolution]=1.79 [Source organism]=10045 / NBRC 100440) [Accession]=MF7000792 [Entry] [Entry number]=977 [Entry name]=CBS domain of the bacterial CNNM/CorC family Mg2+ transporter [PDB ID]=7cfh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=CBS domain [Sequence domain]=CBS domain [Evidence level]=Direct evidence [Evidence text]=The crystallographic packing of the TM0935 structure implies that the dimer is the biologically relevant form (PMID:15326606). The MJ0729 protein with dimers formed from two 2 CBS (cystathionine β-synthase) domain containing monomers showed to be mutually folding. Thermal and chemical unfolding of MJ0729 in physiological pH occured with a two state mechanism (PMID:19267448). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000784,MF7000785,MF7000786,MF7000787,MF7000788,MF7000789,MF7000790,MF7000791,MF7000792,MF7000793 [UniProt ID chain A]=A0A109QFA5 [UniProt boundaries chain A]=186-350 [UniProt coverage chain A]=37% [Name chain A]=Hemolysin [UniProt sequence chain A]=MDRPPSRWLLLLALGTPALAQGEAASPENPWLWAVLVLLLALSAFFSASETAITTLYPWKLKELAESKNGPFRLLAEDITRFLTTILVGNNLVNIAATALVTELATQAFGSAGVGVATGAMTFLILFFGEITPKSLAVHHAEAIARLAAWPIYGLSVLFYPVGRFFSLVSGGLLRLLGLEPRGTPLVSEEELKLILAGAEESGAIQPQEEEMIHSILELEETPVREIMTPRVEMVAIEDEATLEDLLALYREHRYSRVPVYRESVDHIVGVAYAKDLLDYYCEEDLKGRTVASITHPPYFVPENMDAWSLLKELRRRKVHMAIVVDEFGGTAGLVTLEDVIEEIVGEIYDETDEPEDAAIRRLPDGSLSIQAQTPIDEVSEALGVELPEGEYDTLSGFLYALFGRIPSVGESVEWQGFRFVVESADQRRIERVRVERLVEHGEG [Source organism chain A]=Thermus parvatiensis [UniProt ID chain B]=A0A109QFA5 [UniProt boundaries chain B]=184-352 [UniProt coverage chain B]=38% [Name chain B]=Hemolysin [UniProt sequence chain B]=MDRPPSRWLLLLALGTPALAQGEAASPENPWLWAVLVLLLALSAFFSASETAITTLYPWKLKELAESKNGPFRLLAEDITRFLTTILVGNNLVNIAATALVTELATQAFGSAGVGVATGAMTFLILFFGEITPKSLAVHHAEAIARLAAWPIYGLSVLFYPVGRFFSLVSGGLLRLLGLEPRGTPLVSEEELKLILAGAEESGAIQPQEEEMIHSILELEETPVREIMTPRVEMVAIEDEATLEDLLALYREHRYSRVPVYRESVDHIVGVAYAKDLLDYYCEEDLKGRTVASITHPPYFVPENMDAWSLLKELRRRKVHMAIVVDEFGGTAGLVTLEDVIEEIVGEIYDETDEPEDAAIRRLPDGSLSIQAQTPIDEVSEALGVELPEGEYDTLSGFLYALFGRIPSVGESVEWQGFRFVVESADQRRIERVRVERLVEHGEG [Source organism chain B]=Thermus parvatiensis [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Thermus parvatiensis [Accession]=MF7000793 [Entry] [Entry number]=978 [Entry name]=CPXP adaptor protein [PDB ID]=3itf [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=P0AE85 [UniProt boundaries chain A]=40-150 [UniProt coverage chain A]=66% [Name chain A]=Periplasmic protein CpxP [UniProt sequence chain A]=MRIVTAAVMASTLAVSSLSHAAEVGSGDNWHPGEELTQRSTQSHMFDGISLTEHQRQQMRDLMQQARHEQPPVNVSELETMHRLVTAENFDENAVRAQAEKMANEQIARQVEMAKVRNQMYRLLTPEQQAVLNEKHQQRMEQLRDVTQWQKSSSLKLLSSSNSRSQ [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AE85 [UniProt boundaries chain B]=40-150 [UniProt coverage chain B]=66% [Name chain B]=Periplasmic protein CpxP [UniProt sequence chain B]=MRIVTAAVMASTLAVSSLSHAAEVGSGDNWHPGEELTQRSTQSHMFDGISLTEHQRQQMRDLMQQARHEQPPVNVSELETMHRLVTAENFDENAVRAQAEKMANEQIARQVEMAKVRNQMYRLLTPEQQAVLNEKHQQRMEQLRDVTQWQKSSSLKLLSSSNSRSQ [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.45 [Source organism]=Escherichia coli [Accession]=MF7000794 [Entry] [Entry number]=979 [Entry name]=Periplasmic stress response protein CpxP [PDB ID]=3qzc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=P0AE85 [UniProt boundaries chain A]=44-151 [UniProt coverage chain A]=65% [Name chain A]=Periplasmic protein CpxP [UniProt sequence chain A]=MRIVTAAVMASTLAVSSLSHAAEVGSGDNWHPGEELTQRSTQSHMFDGISLTEHQRQQMRDLMQQARHEQPPVNVSELETMHRLVTAENFDENAVRAQAEKMANEQIARQVEMAKVRNQMYRLLTPEQQAVLNEKHQQRMEQLRDVTQWQKSSSLKLLSSSNSRSQ [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P0AE85 [UniProt boundaries chain B]=40-151 [UniProt coverage chain B]=67% [Name chain B]=Periplasmic protein CpxP [UniProt sequence chain B]=MRIVTAAVMASTLAVSSLSHAAEVGSGDNWHPGEELTQRSTQSHMFDGISLTEHQRQQMRDLMQQARHEQPPVNVSELETMHRLVTAENFDENAVRAQAEKMANEQIARQVEMAKVRNQMYRLLTPEQQAVLNEKHQQRMEQLRDVTQWQKSSSLKLLSSSNSRSQ [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.85 [Source organism]=Escherichia coli [Accession]=MF7000795 [Entry] [Entry number]=980 [Entry name]=Chaperone Spy [PDB ID]=3o39 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=Q8XDZ4 [UniProt boundaries chain A]=52-147 [UniProt coverage chain A]=59% [Name chain A]=Periplasmic chaperone Spy [UniProt sequence chain A]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKAKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain A]=Escherichia coli O157:H7 [UniProt ID chain B]=Q8XDZ4 [UniProt boundaries chain B]=52-147 [UniProt coverage chain B]=59% [Name chain B]=Periplasmic chaperone Spy [UniProt sequence chain B]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKAKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain B]=Escherichia coli O157:H7 [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Escherichia coli O157:H7 [Accession]=MF7000796 [Entry] [Entry number]=981 [Entry name]=Chaperone Spy, mutant H96L [PDB ID]=5wo1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=P77754 [UniProt boundaries chain A]=52-146 [UniProt coverage chain A]=59% [Name chain A]=Periplasmic chaperone Spy [UniProt sequence chain A]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P77754 [UniProt boundaries chain B]=52-146 [UniProt coverage chain B]=59% [Name chain B]=Periplasmic chaperone Spy [UniProt sequence chain B]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.87 [Source organism]=Escherichia coli [Accession]=MF7000797 [Entry] [Entry number]=982 [Entry name]=Chaperone Spy with casein [PDB ID]=5wo2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=P77754 [UniProt boundaries chain A]=52-146 [UniProt coverage chain A]=59% [Name chain A]=Periplasmic chaperone Spy [UniProt sequence chain A]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P77754 [UniProt boundaries chain B]=52-147 [UniProt coverage chain B]=59% [Name chain B]=Periplasmic chaperone Spy [UniProt sequence chain B]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.77 [Source organism]=Escherichia coli [Accession]=MF7000798 [Entry] [Entry number]=983 [Entry name]=Chaperone Spy with Im7 [PDB ID]=5wo3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=P77754 [UniProt boundaries chain A]=52-146 [UniProt coverage chain A]=59% [Name chain A]=Periplasmic chaperone Spy [UniProt sequence chain A]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P77754 [UniProt boundaries chain B]=52-145 [UniProt coverage chain B]=58% [Name chain B]=Periplasmic chaperone Spy [UniProt sequence chain B]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.87 [Source organism]=Escherichia coli [Accession]=MF7000799 [Entry] [Entry number]=984 [Entry name]=Chaperone Spy [PDB ID]=6bie [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=P77754 [UniProt boundaries chain A]=52-147 [UniProt coverage chain A]=59% [Name chain A]=Periplasmic chaperone Spy [UniProt sequence chain A]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain A]=Escherichia coli [UniProt ID chain B-2]=P77754 [UniProt boundaries chain B-2]=52-147 [UniProt coverage chain B-2]=59% [Name chain B-2]=Periplasmic chaperone Spy [UniProt sequence chain B-2]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain B-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.77 [Source organism]=Escherichia coli [Accession]=MF7000800 [Entry] [Entry number]=985 [Entry name]=Chaperone Spy H96L:Im7 K20pI-Phe complex [PDB ID]=6owy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=P77754 [UniProt boundaries chain A]=52-145 [UniProt coverage chain A]=58% [Name chain A]=Periplasmic chaperone Spy [UniProt sequence chain A]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P77754 [UniProt boundaries chain B]=52-145 [UniProt coverage chain B]=58% [Name chain B]=Periplasmic chaperone Spy [UniProt sequence chain B]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.07 [Source organism]=Escherichia coli [Accession]=MF7000801 [Entry] [Entry number]=986 [Entry name]=Chaperone Spy H96L:Im7 L18pI-Phe complex [PDB ID]=6owx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=P77754 [UniProt boundaries chain A]=52-145 [UniProt coverage chain A]=58% [Name chain A]=Periplasmic chaperone Spy [UniProt sequence chain A]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P77754 [UniProt boundaries chain B]=52-145 [UniProt coverage chain B]=58% [Name chain B]=Periplasmic chaperone Spy [UniProt sequence chain B]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.06 [Source organism]=Escherichia coli [Accession]=MF7000802 [Entry] [Entry number]=987 [Entry name]=Chaperone Spy H96L:Im7 L19pI-Phe complex [PDB ID]=6owz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=LTXXQ motif family protein [Evidence level]=Indirect evidence [Evidence text]=Spy dimerizes through an antiparallel coiled-coiled interaction. There is an extensive interaction surface between the monomers, suggesting high dimeric stability (PMID:21317898). EcSpy exists as a dimer in solution (PMID:20799348). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000794,MF7000795,MF7000796,MF7000797,MF7000798,MF7000799,MF7000800,MF7000801,MF7000802,MF7000803 [UniProt ID chain A]=P77754 [UniProt boundaries chain A]=52-145 [UniProt coverage chain A]=58% [Name chain A]=Periplasmic chaperone Spy [UniProt sequence chain A]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P77754 [UniProt boundaries chain B]=53-145 [UniProt coverage chain B]=57% [Name chain B]=Periplasmic chaperone Spy [UniProt sequence chain B]=MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Escherichia coli [Accession]=MF7000803 [Entry] [Entry number]=988 [Entry name]=N-domain of the transcription factor AbrB [PDB ID]=1yfb [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=P08874 [UniProt boundaries chain A]=2-53 [UniProt coverage chain A]=54% [Name chain A]=Transition state regulatory protein AbrB [UniProt sequence chain A]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P08874 [UniProt boundaries chain B]=2-53 [UniProt coverage chain B]=54% [Name chain B]=Transition state regulatory protein AbrB [UniProt sequence chain B]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain B]=Bacillus subtilis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus subtilis [Accession]=MF7000804 [Entry] [Entry number]=989 [Entry name]=N-domain of the transcription factor AbrB [PDB ID]=1ysf [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=P08874 [UniProt boundaries chain A]=2-53 [UniProt coverage chain A]=54% [Name chain A]=Transition state regulatory protein AbrB [UniProt sequence chain A]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P08874 [UniProt boundaries chain B]=2-53 [UniProt coverage chain B]=54% [Name chain B]=Transition state regulatory protein AbrB [UniProt sequence chain B]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain B]=Bacillus subtilis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus subtilis [Accession]=MF7000805 [Entry] [Entry number]=990 [Entry name]=N-terminal DNA-recognition domain of AbrB (Bacillus subtilis) [PDB ID]=1z0r [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=P08874 [UniProt boundaries chain A]=3-55 [UniProt coverage chain A]=55% [Name chain A]=Transition state regulatory protein AbrB [UniProt sequence chain A]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P08874 [UniProt boundaries chain B]=3-55 [UniProt coverage chain B]=55% [Name chain B]=Transition state regulatory protein AbrB [UniProt sequence chain B]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain B]=Bacillus subtilis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus subtilis [Accession]=MF7000806 [Entry] [Entry number]=991 [Entry name]=N-terminal DNA-recognition domain of ABH (Bacillus subtilis) [PDB ID]=2fy9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=P39758 [UniProt boundaries chain A]=1-54 [UniProt coverage chain A]=58% [Name chain A]=Putative transition state regulator Abh [UniProt sequence chain A]=MKSIGVVRKVDELGRIVMPIELRRALDIAIKDSIEFFVDGDKIILKKYKPHGVCLMTGEITSENKEYGNGKITLSPEGAQLLLEEIQAALKE [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P39758 [UniProt boundaries chain B]=1-54 [UniProt coverage chain B]=58% [Name chain B]=Putative transition state regulator Abh [UniProt sequence chain B]=MKSIGVVRKVDELGRIVMPIELRRALDIAIKDSIEFFVDGDKIILKKYKPHGVCLMTGEITSENKEYGNGKITLSPEGAQLLLEEIQAALKE [Source organism chain B]=Bacillus subtilis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus subtilis [Accession]=MF7000807 [Entry] [Entry number]=992 [Entry name]=N-terminal DNA-recognition domain of AbrB (Bacillus subtilis) [PDB ID]=2ro4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=P08874 [UniProt boundaries chain A]=3-55 [UniProt coverage chain A]=55% [Name chain A]=Transition state regulatory protein AbrB [UniProt sequence chain A]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P08874 [UniProt boundaries chain B]=3-55 [UniProt coverage chain B]=55% [Name chain B]=Transition state regulatory protein AbrB [UniProt sequence chain B]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain B]=Bacillus subtilis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus subtilis [Accession]=MF7000808 [Entry] [Entry number]=993 [Entry name]=N-terminal DNA-recognition domain of SpoVT (Bacillus subtilis) [PDB ID]=2ro5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=P37554 [UniProt boundaries chain A]=1-55 [UniProt coverage chain A]=30% [Name chain A]=Stage V sporulation protein T [UniProt sequence chain A]=MKATGIVRRIDDLGRVVIPKEIRRTLRIREGDPLEIFVDRDGEVILKKYSPISELGDFAKEYADALYDSLGHSVLICDRDVYIAVSGSSKKDYLNKSISEMLERTMDQRSSVLESDAKSVQLVNGIDEDMNSYTVGPIVANGDPIGAVVIFSKDQTMGEVEHKAVETAAGFLARQMEQ [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P37554 [UniProt boundaries chain B]=1-55 [UniProt coverage chain B]=30% [Name chain B]=Stage V sporulation protein T [UniProt sequence chain B]=MKATGIVRRIDDLGRVVIPKEIRRTLRIREGDPLEIFVDRDGEVILKKYSPISELGDFAKEYADALYDSLGHSVLICDRDVYIAVSGSSKKDYLNKSISEMLERTMDQRSSVLESDAKSVQLVNGIDEDMNSYTVGPIVANGDPIGAVVIFSKDQTMGEVEHKAVETAAGFLARQMEQ [Source organism chain B]=Bacillus subtilis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus subtilis [Accession]=MF7000809 [Entry] [Entry number]=994 [Entry name]=N-terminal DNA-recognition domain of Abh (Bacillus subtilis) [PDB ID]=2ro3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=P39758 [UniProt boundaries chain A]=1-54 [UniProt coverage chain A]=58% [Name chain A]=Putative transition state regulator Abh [UniProt sequence chain A]=MKSIGVVRKVDELGRIVMPIELRRALDIAIKDSIEFFVDGDKIILKKYKPHGVCLMTGEITSENKEYGNGKITLSPEGAQLLLEEIQAALKE [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P39758 [UniProt boundaries chain B]=1-54 [UniProt coverage chain B]=58% [Name chain B]=Putative transition state regulator Abh [UniProt sequence chain B]=MKSIGVVRKVDELGRIVMPIELRRALDIAIKDSIEFFVDGDKIILKKYKPHGVCLMTGEITSENKEYGNGKITLSPEGAQLLLEEIQAALKE [Source organism chain B]=Bacillus subtilis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus subtilis [Accession]=MF7000810 [Entry] [Entry number]=995 [Entry name]=C68 from hybrid virus-plasmid pSSVx [PDB ID]=3o27 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Antitoxin MazE [Sequence domain]=Antidote-toxin recognition MazE [Evidence level]=Direct evidence [Evidence text]=The monomer does not have an independent hydrophobic core, thus dimerization is required for a stable fold. Dimerization takes place by the four β hairpin elements interacting with those of the other monomer (PMID:15939023). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000804,MF7000805,MF7000806,MF7000807,MF7000808,MF7000809,MF7000810,MF7000811,MF7000188,MF7000189 [UniProt ID chain A]=Q9P9J8 [UniProt boundaries chain A]=4-68 [UniProt coverage chain A]=95% [Name chain A]=SpoVT-AbrB domain-containing protein [UniProt sequence chain A]=MRPGIRKLVVLNPRAYKGGSGHTTFYLLIPKDIAEALDIKPDDTFILNMEQKDGDIVLSYKRVKELKI [Source organism chain A]=Sulfolobus islandicus [UniProt ID chain B]=Q9P9J8 [UniProt boundaries chain B]=4-68 [UniProt coverage chain B]=95% [Name chain B]=SpoVT-AbrB domain-containing protein [UniProt sequence chain B]=MRPGIRKLVVLNPRAYKGGSGHTTFYLLIPKDIAEALDIKPDDTFILNMEQKDGDIVLSYKRVKELKI [Source organism chain B]=Sulfolobus islandicus [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Sulfolobus islandicus [Accession]=MF7000811 [Entry] [Entry number]=996 [Entry name]=SarA (Staphylococcus Aureus) [PDB ID]=2frh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (SarA type) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The major component linking the two monomers are α1-helices. The dimerization surface is highly hydrophobic and conserved (PMID:16455801). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000812,MF7000813,MF7000251,MF7000252,MF7000253,MF7000254,MF7000814,MF7000815 [UniProt ID chain A]=Q7A1N5 [UniProt boundaries chain A]=2-124 [UniProt coverage chain A]=99% [Name chain A]=Transcriptional regulator SarA [UniProt sequence chain A]=MAITKINDCFELLSMVTYADKLKSLIKKEFSISFEEFAVLTYISENKEKEYYLKDIINHLNYKQPQVVKAVKILSQEDYFDKKRNEHDERTVLILVNAQQRKKIESLLSRVNKRITEANNEIEL [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=Q7A1N5 [UniProt boundaries chain B]=2-124 [UniProt coverage chain B]=99% [Name chain B]=Transcriptional regulator SarA [UniProt sequence chain B]=MAITKINDCFELLSMVTYADKLKSLIKKEFSISFEEFAVLTYISENKEKEYYLKDIINHLNYKQPQVVKAVKILSQEDYFDKKRNEHDERTVLILVNAQQRKKIESLLSRVNKRITEANNEIEL [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Staphylococcus aureus [Accession]=MF7000812 [Entry] [Entry number]=997 [Entry name]=SarA [PDB ID]=2fnp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (SarA type) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The major component linking the two monomers are α1-helices. The dimerization surface is highly hydrophobic and conserved (PMID:16455801). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000812,MF7000813,MF7000251,MF7000252,MF7000253,MF7000254,MF7000814,MF7000815 [UniProt ID chain A]=Q7A1N5 [UniProt boundaries chain A]=3-124 [UniProt coverage chain A]=98% [Name chain A]=Transcriptional regulator SarA [UniProt sequence chain A]=MAITKINDCFELLSMVTYADKLKSLIKKEFSISFEEFAVLTYISENKEKEYYLKDIINHLNYKQPQVVKAVKILSQEDYFDKKRNEHDERTVLILVNAQQRKKIESLLSRVNKRITEANNEIEL [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=Q7A1N5 [UniProt boundaries chain B]=3-124 [UniProt coverage chain B]=98% [Name chain B]=Transcriptional regulator SarA [UniProt sequence chain B]=MAITKINDCFELLSMVTYADKLKSLIKKEFSISFEEFAVLTYISENKEKEYYLKDIINHLNYKQPQVVKAVKILSQEDYFDKKRNEHDERTVLILVNAQQRKKIESLLSRVNKRITEANNEIEL [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Staphylococcus aureus [Accession]=MF7000813 [Entry] [Entry number]=998 [Entry name]=Rot (Staphylococcus aureus) [PDB ID]=4q77 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (SarA type) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The major component linking the two monomers are α1-helices. The dimerization surface is highly hydrophobic and conserved (PMID:16455801). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000812,MF7000813,MF7000251,MF7000252,MF7000253,MF7000254,MF7000814,MF7000815 [UniProt ID chain A]=Q6GFT9 [UniProt boundaries chain A]=37-166 [UniProt coverage chain A]=78% [Name chain A]=HTH-type transcriptional regulator rot [UniProt sequence chain A]=MHKLAHISFGIVGMFVNTCMVAKYVIINWEMYSMKKVNNDTVFGILQLETLLGDINSIFSEIESEYKMSREEILILLTLWQKGSMTLKEMDRFVEVKPYKRTRTYNNLVELEWIYKERPVDDERTVIIHFNEKLQQEKVELLNFISDAIASRATAMQNSLNAIIAV [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=Q6GFT9 [UniProt boundaries chain B]=37-166 [UniProt coverage chain B]=78% [Name chain B]=HTH-type transcriptional regulator rot [UniProt sequence chain B]=MHKLAHISFGIVGMFVNTCMVAKYVIINWEMYSMKKVNNDTVFGILQLETLLGDINSIFSEIESEYKMSREEILILLTLWQKGSMTLKEMDRFVEVKPYKRTRTYNNLVELEWIYKERPVDDERTVIIHFNEKLQQEKVELLNFISDAIASRATAMQNSLNAIIAV [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=1.77 [Source organism]=Staphylococcus aureus [Accession]=MF7000814 [Entry] [Entry number]=999 [Entry name]=AbfR homodimer [PDB ID]=5hli [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (SarA type) transcriptional regulator [Evidence level]=Indirect evidence [Evidence text]=The major component linking the two monomers are α1-helices. The dimerization surface is highly hydrophobic and conserved (PMID:16455801). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000812,MF7000813,MF7000251,MF7000252,MF7000253,MF7000254,MF7000814,MF7000815 [UniProt ID chain A]=Q5HKZ1 [UniProt boundaries chain A]=1-146 [UniProt coverage chain A]=100% [Name chain A]=Transcriptional regulator, MarR family [UniProt sequence chain A]=MKQEQMRLANQLCFSAYNVSRLFAQFYEKKLKQFGITYSQYLVLLTLWEENPQTLNSIGRHLDLSSNTLTPLLKRLEQSGWVKRERQQSDKRQLIITLTDNGQQQQEAVFEAISSCLPQEFDTTEYDETKYVFEELEQTLKHLIEK [Source organism chain A]=Staphylococcus epidermidis [UniProt ID chain B]=Q5HKZ1 [UniProt boundaries chain B]=1-145 [UniProt coverage chain B]=99% [Name chain B]=Transcriptional regulator, MarR family [UniProt sequence chain B]=MKQEQMRLANQLCFSAYNVSRLFAQFYEKKLKQFGITYSQYLVLLTLWEENPQTLNSIGRHLDLSSNTLTPLLKRLEQSGWVKRERQQSDKRQLIITLTDNGQQQQEAVFEAISSCLPQEFDTTEYDETKYVFEELEQTLKHLIEK [Source organism chain B]=Staphylococcus epidermidis [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Staphylococcus epidermidis [Accession]=MF7000815 [Entry] [Entry number]=1000 [Entry name]=Desulforedoxin (Desulfovibrio gigas) [PDB ID]=1dxg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Rubredoxin-like [Sequence domain]=Desulfoferrodoxin [Evidence level]=Direct evidence [Evidence text]=Large interaction surface between monomers. Extensive hydrogen bonding and hydrophobic contacts in the core of the molecule contribute to the stabilization of the dimeric form. The Dx dimeric structure does not dissociate completely, even under conditions of electrospray mass spectroscopy (PMID:7666420; F. Rusnak, personal communication). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000816,MF7000817,MF7000818,MF7000819,MF7000820 [UniProt ID chain A]=P00273 [UniProt boundaries chain A]=2-37 [UniProt coverage chain A]=97% [Name chain A]=Desulforedoxin [UniProt sequence chain A]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain A]=Megalodesulfovibrio gigas [UniProt ID chain B]=P00273 [UniProt boundaries chain B]=2-37 [UniProt coverage chain B]=97% [Name chain B]=Desulforedoxin [UniProt sequence chain B]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain B]=Megalodesulfovibrio gigas [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Megalodesulfovibrio gigas [Accession]=MF7000816 [Entry] [Entry number]=1001 [Entry name]=Cd-113 derivative of desulforedoxin [PDB ID]=2lk6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Rubredoxin-like [Sequence domain]=Desulfoferrodoxin [Evidence level]=Direct evidence [Evidence text]=Large interaction surface between monomers. Extensive hydrogen bonding and hydrophobic contacts in the core of the molecule contribute to the stabilization of the dimeric form. The Dx dimeric structure does not dissociate completely, even under conditions of electrospray mass spectroscopy (PMID:7666420; F. Rusnak, personal communication). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000816,MF7000817,MF7000818,MF7000819,MF7000820 [UniProt ID chain A]=P00273 [UniProt boundaries chain A]=2-37 [UniProt coverage chain A]=97% [Name chain A]=Desulforedoxin [UniProt sequence chain A]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain A]=Megalodesulfovibrio gigas [UniProt ID chain B]=P00273 [UniProt boundaries chain B]=2-37 [UniProt coverage chain B]=97% [Name chain B]=Desulforedoxin [UniProt sequence chain B]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain B]=Megalodesulfovibrio gigas [ExpTech]=NMR [Resolution]=N/A [Source organism]=Megalodesulfovibrio gigas [Accession]=MF7000817 [Entry] [Entry number]=1002 [Entry name]=Ga-substituted desulforedoxin [PDB ID]=1cfw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Rubredoxin-like [Sequence domain]=Desulfoferrodoxin [Evidence level]=Direct evidence [Evidence text]=Large interaction surface between monomers. Extensive hydrogen bonding and hydrophobic contacts in the core of the molecule contribute to the stabilization of the dimeric form. The Dx dimeric structure does not dissociate completely, even under conditions of electrospray mass spectroscopy (PMID:7666420; F. Rusnak, personal communication). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000816,MF7000817,MF7000818,MF7000819,MF7000820 [UniProt ID chain A]=P00273 [UniProt boundaries chain A]=2-37 [UniProt coverage chain A]=97% [Name chain A]=Desulforedoxin [UniProt sequence chain A]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain A]=Megalodesulfovibrio gigas [UniProt ID chain B]=P00273 [UniProt boundaries chain B]=2-37 [UniProt coverage chain B]=97% [Name chain B]=Desulforedoxin [UniProt sequence chain B]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain B]=Megalodesulfovibrio gigas [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Megalodesulfovibrio gigas [Accession]=MF7000818 [Entry] [Entry number]=1003 [Entry name]=Desulforedoxin with Cd [PDB ID]=1dcd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Rubredoxin-like [Sequence domain]=Desulfoferrodoxin [Evidence level]=Direct evidence [Evidence text]=Large interaction surface between monomers. Extensive hydrogen bonding and hydrophobic contacts in the core of the molecule contribute to the stabilization of the dimeric form. The Dx dimeric structure does not dissociate completely, even under conditions of electrospray mass spectroscopy (PMID:7666420; F. Rusnak, personal communication). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000816,MF7000817,MF7000818,MF7000819,MF7000820 [UniProt ID chain A]=P00273 [UniProt boundaries chain A]=2-37 [UniProt coverage chain A]=97% [Name chain A]=Desulforedoxin [UniProt sequence chain A]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain A]=Megalodesulfovibrio gigas [UniProt ID chain B]=P00273 [UniProt boundaries chain B]=2-37 [UniProt coverage chain B]=97% [Name chain B]=Desulforedoxin [UniProt sequence chain B]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain B]=Megalodesulfovibrio gigas [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Megalodesulfovibrio gigas [Accession]=MF7000819 [Entry] [Entry number]=1004 [Entry name]=Hg-substituted desulforedoxin [PDB ID]=1dhg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Rubredoxin-like [Sequence domain]=Desulfoferrodoxin [Evidence level]=Direct evidence [Evidence text]=Large interaction surface between monomers. Extensive hydrogen bonding and hydrophobic contacts in the core of the molecule contribute to the stabilization of the dimeric form. The Dx dimeric structure does not dissociate completely, even under conditions of electrospray mass spectroscopy (PMID:7666420; F. Rusnak, personal communication). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000816,MF7000817,MF7000818,MF7000819,MF7000820 [UniProt ID chain A]=P00273 [UniProt boundaries chain A]=2-37 [UniProt coverage chain A]=97% [Name chain A]=Desulforedoxin [UniProt sequence chain A]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain A]=Megalodesulfovibrio gigas [UniProt ID chain B]=P00273 [UniProt boundaries chain B]=2-37 [UniProt coverage chain B]=97% [Name chain B]=Desulforedoxin [UniProt sequence chain B]=MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ [Source organism chain B]=Megalodesulfovibrio gigas [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Megalodesulfovibrio gigas [Accession]=MF7000820 [Entry] [Entry number]=1005 [Entry name]=TM107 [PDB ID]=1ilv [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Survival protein SurE [Evidence level]=Direct evidence [Evidence text]=Two-state thermal unfolding (PMID:23409101). Domain-swapped dimer with extensive swap region and large dimer interface. Dimeric in solution (gel filtration, DLS). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000821,MF7000221,MF7000222,MF7000224,MF7000227,MF7000223,MF7000225,MF7000226 [UniProt ID chain A]=P96112 [UniProt boundaries chain A]=1-246 [UniProt coverage chain A]=99% [Name chain A]=5'-nucleotidase SurE [UniProt sequence chain A]=MRILVTNDDGIQSKGIIVLAELLSEEHEVFVVAPDKERSATGHSITIHVPLWMKKVFISERVVAYSTTGTPADCVKLAYNVVMDKRVDLIVSGVNRGPNMGMDILHSGTVSGAMEGAMMNIPSIAISSANYESPDFEGAARFLIDFLKEFDFSLLDPFTMLNINVPAGEIKGWRFTRQSRRRWNDYFEERVSPFGEKYYWMMGEVIEDDDRDDVDYKAVREGYVSITPIHPFLTNEQCLKKLREVYD [Source organism chain A]=/ MSB8) [UniProt ID chain A-2]=P96112 [UniProt boundaries chain A-2]=1-247 [UniProt coverage chain A-2]=100% [Name chain A-2]=5'-nucleotidase SurE [UniProt sequence chain A-2]=MRILVTNDDGIQSKGIIVLAELLSEEHEVFVVAPDKERSATGHSITIHVPLWMKKVFISERVVAYSTTGTPADCVKLAYNVVMDKRVDLIVSGVNRGPNMGMDILHSGTVSGAMEGAMMNIPSIAISSANYESPDFEGAARFLIDFLKEFDFSLLDPFTMLNINVPAGEIKGWRFTRQSRRRWNDYFEERVSPFGEKYYWMMGEVIEDDDRDDVDYKAVREGYVSITPIHPFLTNEQCLKKLREVYD [Source organism chain A-2]=/ MSB8) [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=/ MSB8) [Accession]=MF7000821 [Entry] [Entry number]=1006 [Entry name]=DcpS with m7GpppG [PDB ID]=1st0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Scavenger mRNA decapping enzyme (DcpS) [Evidence level]=Indirect evidence [Evidence text]=Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000822,MF7000823,MF7000824,MF7000825,MF7000826,MF7000827,MF7000828,MF7000829 [UniProt ID chain B]=Q96C86 [UniProt boundaries chain B]=40-336 [UniProt coverage chain B]=88% [Name chain B]=m7GpppX diphosphatase [UniProt sequence chain B]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain B]=Homo sapiens [UniProt ID chain A]=Q96C86 [UniProt boundaries chain A]=38-337 [UniProt coverage chain A]=89% [Name chain A]=m7GpppX diphosphatase [UniProt sequence chain A]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain A]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Homo sapiens [Accession]=MF7000822 [Entry] [Entry number]=1007 [Entry name]=DcpS with m7GpppA [PDB ID]=1st4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Scavenger mRNA decapping enzyme (DcpS) [Evidence level]=Indirect evidence [Evidence text]=Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000822,MF7000823,MF7000824,MF7000825,MF7000826,MF7000827,MF7000828,MF7000829 [UniProt ID chain B]=Q96C86 [UniProt boundaries chain B]=40-336 [UniProt coverage chain B]=88% [Name chain B]=m7GpppX diphosphatase [UniProt sequence chain B]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain B]=Homo sapiens [UniProt ID chain A]=Q96C86 [UniProt boundaries chain A]=38-337 [UniProt coverage chain A]=89% [Name chain A]=m7GpppX diphosphatase [UniProt sequence chain A]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain A]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.02 [Source organism]=Homo sapiens [Accession]=MF7000823 [Entry] [Entry number]=1008 [Entry name]=Human Dcps [PDB ID]=1xml [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Scavenger mRNA decapping enzyme (DcpS) [Evidence level]=Indirect evidence [Evidence text]=Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000822,MF7000823,MF7000824,MF7000825,MF7000826,MF7000827,MF7000828,MF7000829 [UniProt ID chain B]=Q96C86 [UniProt boundaries chain B]=40-336 [UniProt coverage chain B]=88% [Name chain B]=m7GpppX diphosphatase [UniProt sequence chain B]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain B]=Homo sapiens [UniProt ID chain A]=Q96C86 [UniProt boundaries chain A]=38-336 [UniProt coverage chain A]=88% [Name chain A]=m7GpppX diphosphatase [UniProt sequence chain A]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain A]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000824 [Entry] [Entry number]=1009 [Entry name]=Mouse mRNA decapping enzyme (DcpS) [PDB ID]=1vlr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Scavenger mRNA decapping enzyme (DcpS) [Evidence level]=Indirect evidence [Evidence text]=Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000822,MF7000823,MF7000824,MF7000825,MF7000826,MF7000827,MF7000828,MF7000829 [UniProt ID chain A]=Q9DAR7 [UniProt boundaries chain A]=38-337 [UniProt coverage chain A]=88% [Name chain A]=m7GpppX diphosphatase [UniProt sequence chain A]=MADTAPQLKRKREQEAEEAETPSTEEKEAGVGNGTSAPVRLPFSGFRVQKVLRESARDKIIFLHGKVNEDSGDTHGEDAVVILEKTPFQVEHVAQLLTGSPELKLQFSNDIYSTYNLFPPRHLSDIKTTVVYPATEKHLQKYMRQDLRLIRETGDDYRTITLPYLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILREGQEAILKRYQVTGDRLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAQVIENLECDPKHYQQRTLTFALRTDDPLLQLLQKAQQERN [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q9DAR7 [UniProt boundaries chain B]=39-337 [UniProt coverage chain B]=88% [Name chain B]=m7GpppX diphosphatase [UniProt sequence chain B]=MADTAPQLKRKREQEAEEAETPSTEEKEAGVGNGTSAPVRLPFSGFRVQKVLRESARDKIIFLHGKVNEDSGDTHGEDAVVILEKTPFQVEHVAQLLTGSPELKLQFSNDIYSTYNLFPPRHLSDIKTTVVYPATEKHLQKYMRQDLRLIRETGDDYRTITLPYLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILREGQEAILKRYQVTGDRLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAQVIENLECDPKHYQQRTLTFALRTDDPLLQLLQKAQQERN [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.83 [Source organism]=Mus musculus [Accession]=MF7000825 [Entry] [Entry number]=1010 [Entry name]=DcpS with inhibitor DG153249 [PDB ID]=3bla [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Scavenger mRNA decapping enzyme (DcpS) [Evidence level]=Indirect evidence [Evidence text]=Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000822,MF7000823,MF7000824,MF7000825,MF7000826,MF7000827,MF7000828,MF7000829 [UniProt ID chain A]=Q96C86 [UniProt boundaries chain A]=42-334 [UniProt coverage chain A]=86% [Name chain A]=m7GpppX diphosphatase [UniProt sequence chain A]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q96C86 [UniProt boundaries chain B]=40-336 [UniProt coverage chain B]=88% [Name chain B]=m7GpppX diphosphatase [UniProt sequence chain B]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Homo sapiens [Accession]=MF7000826 [Entry] [Entry number]=1011 [Entry name]=DcpS with inhibitor DG156844 [PDB ID]=3bl7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Scavenger mRNA decapping enzyme (DcpS) [Evidence level]=Indirect evidence [Evidence text]=Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000822,MF7000823,MF7000824,MF7000825,MF7000826,MF7000827,MF7000828,MF7000829 [UniProt ID chain A]=Q96C86 [UniProt boundaries chain A]=42-334 [UniProt coverage chain A]=86% [Name chain A]=m7GpppX diphosphatase [UniProt sequence chain A]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q96C86 [UniProt boundaries chain B]=40-336 [UniProt coverage chain B]=88% [Name chain B]=m7GpppX diphosphatase [UniProt sequence chain B]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.31 [Source organism]=Homo sapiens [Accession]=MF7000827 [Entry] [Entry number]=1012 [Entry name]=DcpS with inhibitor DG157493 [PDB ID]=3bl9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Scavenger mRNA decapping enzyme (DcpS) [Evidence level]=Indirect evidence [Evidence text]=Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000822,MF7000823,MF7000824,MF7000825,MF7000826,MF7000827,MF7000828,MF7000829 [UniProt ID chain A]=Q96C86 [UniProt boundaries chain A]=42-334 [UniProt coverage chain A]=86% [Name chain A]=m7GpppX diphosphatase [UniProt sequence chain A]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q96C86 [UniProt boundaries chain B]=40-336 [UniProt coverage chain B]=88% [Name chain B]=m7GpppX diphosphatase [UniProt sequence chain B]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Homo sapiens [Accession]=MF7000828 [Entry] [Entry number]=1013 [Entry name]=Human decapping scavenger enzyme (hDcpS) with m7G(5'S)ppSp(5'S)G mRNA 5' cap analog [PDB ID]=5osy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Scavenger mRNA decapping enzyme (DcpS) [Evidence level]=Indirect evidence [Evidence text]=Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000822,MF7000823,MF7000824,MF7000825,MF7000826,MF7000827,MF7000828,MF7000829 [UniProt ID chain A]=Q96C86 [UniProt boundaries chain A]=37-336 [UniProt coverage chain A]=89% [Name chain A]=m7GpppX diphosphatase [UniProt sequence chain A]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q96C86 [UniProt boundaries chain B]=40-336 [UniProt coverage chain B]=88% [Name chain B]=m7GpppX diphosphatase [UniProt sequence chain B]=MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.06 [Source organism]=Homo sapiens [Accession]=MF7000829 [Entry] [Entry number]=1014 [Entry name]=PerR-Zn (Bacillus subtilis) [PDB ID]=2fe3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and dimerization domain [Sequence domain]=Ferric uptake regulator family [Evidence level]=Indirect evidence [Evidence text]=The protein assembles into a biological dimer in which each monomer has two domains, the DNA-binding domain and the dimerization domain, as other ferric uptake regulators (PMID:29739988). Dimeric in solution according to its FPLC profile (PMID:16925555). The dimerization domain is a strong candidate for MSF due to large interface and beta sheet augmentation between the monomers. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000830,MF7000831,MF7000832,MF7000833,MF7000834,MF7000320,MF7000319 [UniProt ID chain A]=P71086 [UniProt boundaries chain A]=4-144 [UniProt coverage chain A]=97% [Name chain A]=Peroxide operon regulator [UniProt sequence chain A]=MAAHELKEALETLKETGVRITPQRHAILEYLVNSMAHPTADDIYKALEGKFPNMSVATVYNNLRVFRESGLVKELTYGDASSRFDFVTSDHYHAICENCGKIVDFHYPGLDEVEQLAAHVTGFKVSHHRLEIYGVCQECSKKENH [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P71086 [UniProt boundaries chain B]=3-145 [UniProt coverage chain B]=98% [Name chain B]=Peroxide operon regulator [UniProt sequence chain B]=MAAHELKEALETLKETGVRITPQRHAILEYLVNSMAHPTADDIYKALEGKFPNMSVATVYNNLRVFRESGLVKELTYGDASSRFDFVTSDHYHAICENCGKIVDFHYPGLDEVEQLAAHVTGFKVSHHRLEIYGVCQECSKKENH [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.75 [Source organism]=Bacillus subtilis [Accession]=MF7000830 [Entry] [Entry number]=1015 [Entry name]=PerR-Ox (Bacillus subtilis) [PDB ID]=2rgv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and dimerization domain [Sequence domain]=Ferric uptake regulator family [Evidence level]=Indirect evidence [Evidence text]=The protein assembles into a biological dimer in which each monomer has two domains, the DNA-binding domain and the dimerization domain, as other ferric uptake regulators (PMID:29739988). Dimeric in solution according to its FPLC profile (PMID:16925555). The dimerization domain is a strong candidate for MSF due to large interface and beta sheet augmentation between the monomers. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000830,MF7000831,MF7000832,MF7000833,MF7000834,MF7000320,MF7000319 [UniProt ID chain A]=P71086 [UniProt boundaries chain A]=4-144 [UniProt coverage chain A]=97% [Name chain A]=Peroxide operon regulator [UniProt sequence chain A]=MAAHELKEALETLKETGVRITPQRHAILEYLVNSMAHPTADDIYKALEGKFPNMSVATVYNNLRVFRESGLVKELTYGDASSRFDFVTSDHYHAICENCGKIVDFHYPGLDEVEQLAAHVTGFKVSHHRLEIYGVCQECSKKENH [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P71086 [UniProt boundaries chain B]=3-145 [UniProt coverage chain B]=98% [Name chain B]=Peroxide operon regulator [UniProt sequence chain B]=MAAHELKEALETLKETGVRITPQRHAILEYLVNSMAHPTADDIYKALEGKFPNMSVATVYNNLRVFRESGLVKELTYGDASSRFDFVTSDHYHAICENCGKIVDFHYPGLDEVEQLAAHVTGFKVSHHRLEIYGVCQECSKKENH [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Bacillus subtilis [Accession]=MF7000831 [Entry] [Entry number]=1016 [Entry name]=Nur, a Ni-specific Fur homologue [PDB ID]=3eyy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and dimerization domain [Sequence domain]=Ferric uptake regulator family [Evidence level]=Indirect evidence [Evidence text]=The protein assembles into a biological dimer in which each monomer has two domains, the DNA-binding domain and the dimerization domain, as other ferric uptake regulators (PMID:29739988). Dimeric in solution according to its FPLC profile (PMID:16925555). The dimerization domain is a strong candidate for MSF due to large interface and beta sheet augmentation between the monomers. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000830,MF7000831,MF7000832,MF7000833,MF7000834,MF7000320,MF7000319 [UniProt ID chain A]=Q9K4F8 [UniProt boundaries chain A]=3-135 [UniProt coverage chain A]=91% [Name chain A]=Iron uptake regulatory protein [UniProt sequence chain A]=MVSTDWKSDLRQRGYRLTPQRQLVLEAVDTLEHATPDDILGEVRKTASGINISTVYRTLELLEELGLVSHAHLGHGAPTYHLADRHHHIHLVCRDCTNVIEADLSVAADFTAKLREQFGFDTDMKHFAIFGRCESCSLKGSTTDS [Source organism chain A]=Streptomyces coelicolor [UniProt ID chain B]=Q9K4F8 [UniProt boundaries chain B]=3-135 [UniProt coverage chain B]=91% [Name chain B]=Iron uptake regulatory protein [UniProt sequence chain B]=MVSTDWKSDLRQRGYRLTPQRQLVLEAVDTLEHATPDDILGEVRKTASGINISTVYRTLELLEELGLVSHAHLGHGAPTYHLADRHHHIHLVCRDCTNVIEADLSVAADFTAKLREQFGFDTDMKHFAIFGRCESCSLKGSTTDS [Source organism chain B]=Streptomyces coelicolor [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Streptomyces coelicolor [Accession]=MF7000832 [Entry] [Entry number]=1017 [Entry name]=PerR-Zn-Mn [PDB ID]=3f8n [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and dimerization domain [Sequence domain]=Ferric uptake regulator family [Evidence level]=Indirect evidence [Evidence text]=The protein assembles into a biological dimer in which each monomer has two domains, the DNA-binding domain and the dimerization domain, as other ferric uptake regulators (PMID:29739988). Dimeric in solution according to its FPLC profile (PMID:16925555). The dimerization domain is a strong candidate for MSF due to large interface and beta sheet augmentation between the monomers. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000830,MF7000831,MF7000832,MF7000833,MF7000834,MF7000320,MF7000319 [UniProt ID chain A]=P71086 [UniProt boundaries chain A]=4-140 [UniProt coverage chain A]=94% [Name chain A]=Peroxide operon regulator [UniProt sequence chain A]=MAAHELKEALETLKETGVRITPQRHAILEYLVNSMAHPTADDIYKALEGKFPNMSVATVYNNLRVFRESGLVKELTYGDASSRFDFVTSDHYHAICENCGKIVDFHYPGLDEVEQLAAHVTGFKVSHHRLEIYGVCQECSKKENH [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P71086 [UniProt boundaries chain B]=4-139 [UniProt coverage chain B]=93% [Name chain B]=Peroxide operon regulator [UniProt sequence chain B]=MAAHELKEALETLKETGVRITPQRHAILEYLVNSMAHPTADDIYKALEGKFPNMSVATVYNNLRVFRESGLVKELTYGDASSRFDFVTSDHYHAICENCGKIVDFHYPGLDEVEQLAAHVTGFKVSHHRLEIYGVCQECSKKENH [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=3.15 [Source organism]=Bacillus subtilis [Accession]=MF7000833 [Entry] [Entry number]=1018 [Entry name]=Zn uptake regulator (Zur) [PDB ID]=3mwm [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and dimerization domain [Sequence domain]=Ferric uptake regulator family [Evidence level]=Indirect evidence [Evidence text]=The protein assembles into a biological dimer in which each monomer has two domains, the DNA-binding domain and the dimerization domain, as other ferric uptake regulators (PMID:29739988). Dimeric in solution according to its FPLC profile (PMID:16925555). The dimerization domain is a strong candidate for MSF due to large interface and beta sheet augmentation between the monomers. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000830,MF7000831,MF7000832,MF7000833,MF7000834,MF7000320,MF7000319 [UniProt ID chain A]=Q9L2H5 [UniProt boundaries chain A]=10-136 [UniProt coverage chain A]=91% [Name chain A]=Metal uptake regulation protein [UniProt sequence chain A]=MTTAGPPVKGRATRQRAAVSAALQEVEEFRSAQELHDMLKHKGDAVGLTTVYRTLQSLADAGEVDVLRTAEGESVYRRCSTGDHHHHLVCRACGKAVEVEGPAVEKWAEAIAAEHGYVNVAHTVEIFGTCADCAGASGG [Source organism chain A]=Streptomyces coelicolor [UniProt ID chain A-2]=Q9L2H5 [UniProt boundaries chain A-2]=11-135 [UniProt coverage chain A-2]=89% [Name chain A-2]=Metal uptake regulation protein [UniProt sequence chain A-2]=MTTAGPPVKGRATRQRAAVSAALQEVEEFRSAQELHDMLKHKGDAVGLTTVYRTLQSLADAGEVDVLRTAEGESVYRRCSTGDHHHHLVCRACGKAVEVEGPAVEKWAEAIAAEHGYVNVAHTVEIFGTCADCAGASGG [Source organism chain A-2]=Streptomyces coelicolor [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Streptomyces coelicolor [Accession]=MF7000834 [Entry] [Entry number]=1019 [Entry name]=MinE (Neisseria gonorrhoeae) [PDB ID]=2kxo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=MinE superfamily [Sequence domain]=Septum formation topological specificity factor MinE [Evidence level]=Direct evidence [Evidence text]=MinE is an example of IDP that undergoes disorder to order transition on self-assembly (Review: https://doi.org/10.3389/fphy.2019.00010). Tight dimer, there is beta sheet augmentation between the monomers. There is no evidence for monomeric state even at very low concentrations, only dimeric form could be detected (PMID:31772021). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000045,MF7000048,MF7000049,MF7000835,MF7000836,MF7000046,MF7000047 [UniProt ID chain A]=P58152 [UniProt boundaries chain A]=1-87 [UniProt coverage chain A]=100% [Name chain A]=Cell division topological specificity factor [UniProt sequence chain A]=MSLIELLFGRKQKTATVARDRLQIIIAQERAQEGQTPDYLPTLRKELMEVLSKYVNVSLDNIRISQEKQDGMDVLELNITLPEQKKV [Source organism chain A]=Neisseria gonorrhoeae [UniProt ID chain B]=P58152 [UniProt boundaries chain B]=1-87 [UniProt coverage chain B]=100% [Name chain B]=Cell division topological specificity factor [UniProt sequence chain B]=MSLIELLFGRKQKTATVARDRLQIIIAQERAQEGQTPDYLPTLRKELMEVLSKYVNVSLDNIRISQEKQDGMDVLELNITLPEQKKV [Source organism chain B]=Neisseria gonorrhoeae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Neisseria gonorrhoeae [Accession]=MF7000835 [Entry] [Entry number]=1020 [Entry name]=MinE, latent form (Neisseria gonorrheae) [PDB ID]=6u6p [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=MinE superfamily [Sequence domain]=Septum formation topological specificity factor MinE [Evidence level]=Direct evidence [Evidence text]=MinE is an example of IDP that undergoes disorder to order transition on self-assembly (Review: https://doi.org/10.3389/fphy.2019.00010). Tight dimer, there is beta sheet augmentation between the monomers. There is no evidence for monomeric state even at very low concentrations, only dimeric form could be detected (PMID:31772021). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000045,MF7000048,MF7000049,MF7000835,MF7000836,MF7000046,MF7000047 [UniProt ID chain A]=P58152 [UniProt boundaries chain A]=1-81 [UniProt coverage chain A]=93% [Name chain A]=Cell division topological specificity factor [UniProt sequence chain A]=MSLIELLFGRKQKTATVARDRLQIIIAQERAQEGQTPDYLPTLRKELMEVLSKYVNVSLDNIRISQEKQDGMDVLELNITLPEQKKV [Source organism chain A]=Neisseria gonorrhoeae [UniProt ID chain B]=P58152 [UniProt boundaries chain B]=1-81 [UniProt coverage chain B]=93% [Name chain B]=Cell division topological specificity factor [UniProt sequence chain B]=MSLIELLFGRKQKTATVARDRLQIIIAQERAQEGQTPDYLPTLRKELMEVLSKYVNVSLDNIRISQEKQDGMDVLELNITLPEQKKV [Source organism chain B]=Neisseria gonorrhoeae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Neisseria gonorrhoeae [Accession]=MF7000836 [Entry] [Entry number]=1021 [Entry name]=OHR (Pseudomonas aeruginosa) [PDB ID]=1n2f [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=OsmC-like protein [Evidence level]=Direct evidence [Evidence text]=Ohr is a tightly folded homodimer with a large buried hydrophobic surface area. The two monomers are tightly wrapped around each other in a head-to-tail orientation. Dimerization is dominated by helix–helix packing interactions of two long helices at the center of the hydrophobic core of the dimeric enzyme. Also, each β-sheet is composed of six strands, three from one monomer and three from the other (beta sheet augmentation). The hydrophobic core, as well as the surrounding β-sheets, are generated by combining elements of both monomers, therefore, it is clear that the two polypeptide chains have to fold together to form active Ohr, and that each monomer would individually be unstable. The two active sites are also located at the dimer interface (PMID:12485986). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000837,MF7000838,MF7000839,MF7000840,MF7000841,MF7000842,MF7000843 [UniProt ID chain A]=Q9HZZ3 [UniProt boundaries chain A]=1-142 [UniProt coverage chain A]=100% [Name chain A]=Organic hydroperoxide resistance protein [UniProt sequence chain A]=MQTIKALYTATATATGGRDGRAVSSDGVLDVKLSTPRELGGQGGAATNPEQLFAAGYSACFIGALKFVAGQRKQTLPADASITGKVGIGQIPGGFGLEVELHINLPGLEREAAEALVAAAHQVCPYSNATRGNIDVRLNVSV [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=Q9HZZ3 [UniProt boundaries chain B]=1-142 [UniProt coverage chain B]=100% [Name chain B]=Organic hydroperoxide resistance protein [UniProt sequence chain B]=MQTIKALYTATATATGGRDGRAVSSDGVLDVKLSTPRELGGQGGAATNPEQLFAAGYSACFIGALKFVAGQRKQTLPADASITGKVGIGQIPGGFGLEVELHINLPGLEREAAEALVAAAHQVCPYSNATRGNIDVRLNVSV [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.01 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000837 [Entry] [Entry number]=1022 [Entry name]=Hydroperoxide resistance protein (Deinococcus radiodurans) [PDB ID]=1usp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=OsmC-like protein [Evidence level]=Direct evidence [Evidence text]=Ohr is a tightly folded homodimer with a large buried hydrophobic surface area. The two monomers are tightly wrapped around each other in a head-to-tail orientation. Dimerization is dominated by helix–helix packing interactions of two long helices at the center of the hydrophobic core of the dimeric enzyme. Also, each β-sheet is composed of six strands, three from one monomer and three from the other (beta sheet augmentation). The hydrophobic core, as well as the surrounding β-sheets, are generated by combining elements of both monomers, therefore, it is clear that the two polypeptide chains have to fold together to form active Ohr, and that each monomer would individually be unstable. The two active sites are also located at the dimer interface (PMID:12485986). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000837,MF7000838,MF7000839,MF7000840,MF7000841,MF7000842,MF7000843 [UniProt ID chain A]=Q9RTA8 [UniProt boundaries chain A]=3-139 [UniProt coverage chain A]=98% [Name chain A]=Organic hydroperoxide resistance protein [UniProt sequence chain A]=MANVYTAEATATGGRAGTTRSSDDRLNLDLSVPAEMGGDGGPGTNPEQLFAAGYAACFQGALGVVSRRQKIDVPADSTITARVGLQKAGLAFALDVELEGHFPGLSREQAEGLMHAAHEVCPYSAATRNNVDVRLKVRE [Source organism chain A]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [UniProt ID chain B]=Q9RTA8 [UniProt boundaries chain B]=2-139 [UniProt coverage chain B]=99% [Name chain B]=Organic hydroperoxide resistance protein [UniProt sequence chain B]=MANVYTAEATATGGRAGTTRSSDDRLNLDLSVPAEMGGDGGPGTNPEQLFAAGYAACFQGALGVVSRRQKIDVPADSTITARVGLQKAGLAFALDVELEGHFPGLSREQAEGLMHAAHEVCPYSAATRNNVDVRLKVRE [Source organism chain B]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [ExpTech]=X-ray [Resolution]=1.9 [Source organism]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [Accession]=MF7000838 [Entry] [Entry number]=1023 [Entry name]=Osmotically inducible protein C (Thermus thermophilus) [PDB ID]=1ukk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=OsmC-like protein [Evidence level]=Direct evidence [Evidence text]=Ohr is a tightly folded homodimer with a large buried hydrophobic surface area. The two monomers are tightly wrapped around each other in a head-to-tail orientation. Dimerization is dominated by helix–helix packing interactions of two long helices at the center of the hydrophobic core of the dimeric enzyme. Also, each β-sheet is composed of six strands, three from one monomer and three from the other (beta sheet augmentation). The hydrophobic core, as well as the surrounding β-sheets, are generated by combining elements of both monomers, therefore, it is clear that the two polypeptide chains have to fold together to form active Ohr, and that each monomer would individually be unstable. The two active sites are also located at the dimer interface (PMID:12485986). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000837,MF7000838,MF7000839,MF7000840,MF7000841,MF7000842,MF7000843 [UniProt ID chain A]=P84124 [UniProt boundaries chain A]=2-142 [UniProt coverage chain A]=99% [Name chain A]=Osmotically inducible protein C [UniProt sequence chain A]=MPVRKAKAVWEGGLRQGKGVMELQSQAFQGPYSYPSRFEEGEGTNPEELIAAAHAGXFSMALAASLEREGFPPKRVSTEARVHLEVVDGKPTLTRIELLTEAEVPGISSEKFLEIAEAAKEGCPVSRALAGVKEVVLTARLV [Source organism chain A]=Thermus thermophilus [UniProt ID chain B]=P84124 [UniProt boundaries chain B]=2-142 [UniProt coverage chain B]=99% [Name chain B]=Osmotically inducible protein C [UniProt sequence chain B]=MPVRKAKAVWEGGLRQGKGVMELQSQAFQGPYSYPSRFEEGEGTNPEELIAAAHAGXFSMALAASLEREGFPPKRVSTEARVHLEVVDGKPTLTRIELLTEAEVPGISSEKFLEIAEAAKEGCPVSRALAGVKEVVLTARLV [Source organism chain B]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Thermus thermophilus [Accession]=MF7000839 [Entry] [Entry number]=1024 [Entry name]=Peroxide resistance protein (Xylella fastidiosa) [PDB ID]=1zb8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=OsmC-like protein [Evidence level]=Direct evidence [Evidence text]=Ohr is a tightly folded homodimer with a large buried hydrophobic surface area. The two monomers are tightly wrapped around each other in a head-to-tail orientation. Dimerization is dominated by helix–helix packing interactions of two long helices at the center of the hydrophobic core of the dimeric enzyme. Also, each β-sheet is composed of six strands, three from one monomer and three from the other (beta sheet augmentation). The hydrophobic core, as well as the surrounding β-sheets, are generated by combining elements of both monomers, therefore, it is clear that the two polypeptide chains have to fold together to form active Ohr, and that each monomer would individually be unstable. The two active sites are also located at the dimer interface (PMID:12485986). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000837,MF7000838,MF7000839,MF7000840,MF7000841,MF7000842,MF7000843 [UniProt ID chain A]=Q9PCF4 [UniProt boundaries chain A]=3-143 [UniProt coverage chain A]=98% [Name chain A]=Organic hydroperoxide resistance protein [UniProt sequence chain A]=MNSLEKVLYTAIVTATGGRDGSVVSSDNVLNVKLSVPQGLGGPGGSGTNPEQLFAAGYSACFIGALKFVANKEKVDLPAEPRVEGRVGIGEIPGGFGLVVELRIAVSGMERSMLQTLVDKAHRVCPYSNATRGNIDVVLILID [Source organism chain A]=Xylella fastidiosa [UniProt ID chain B]=Q9PCF4 [UniProt boundaries chain B]=3-143 [UniProt coverage chain B]=98% [Name chain B]=Organic hydroperoxide resistance protein [UniProt sequence chain B]=MNSLEKVLYTAIVTATGGRDGSVVSSDNVLNVKLSVPQGLGGPGGSGTNPEQLFAAGYSACFIGALKFVANKEKVDLPAEPRVEGRVGIGEIPGGFGLVVELRIAVSGMERSMLQTLVDKAHRVCPYSNATRGNIDVVLILID [Source organism chain B]=Xylella fastidiosa [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Xylella fastidiosa [Accession]=MF7000840 [Entry] [Entry number]=1025 [Entry name]=Peroxide resistance protein (Xylella fastidiosa) [PDB ID]=1zb9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=OsmC-like protein [Evidence level]=Direct evidence [Evidence text]=Ohr is a tightly folded homodimer with a large buried hydrophobic surface area. The two monomers are tightly wrapped around each other in a head-to-tail orientation. Dimerization is dominated by helix–helix packing interactions of two long helices at the center of the hydrophobic core of the dimeric enzyme. Also, each β-sheet is composed of six strands, three from one monomer and three from the other (beta sheet augmentation). The hydrophobic core, as well as the surrounding β-sheets, are generated by combining elements of both monomers, therefore, it is clear that the two polypeptide chains have to fold together to form active Ohr, and that each monomer would individually be unstable. The two active sites are also located at the dimer interface (PMID:12485986). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000837,MF7000838,MF7000839,MF7000840,MF7000841,MF7000842,MF7000843 [UniProt ID chain A]=Q9PCF4 [UniProt boundaries chain A]=2-143 [UniProt coverage chain A]=99% [Name chain A]=Organic hydroperoxide resistance protein [UniProt sequence chain A]=MNSLEKVLYTAIVTATGGRDGSVVSSDNVLNVKLSVPQGLGGPGGSGTNPEQLFAAGYSACFIGALKFVANKEKVDLPAEPRVEGRVGIGEIPGGFGLVVELRIAVSGMERSMLQTLVDKAHRVCPYSNATRGNIDVVLILID [Source organism chain A]=Xylella fastidiosa [UniProt ID chain B]=Q9PCF4 [UniProt boundaries chain B]=3-143 [UniProt coverage chain B]=98% [Name chain B]=Organic hydroperoxide resistance protein [UniProt sequence chain B]=MNSLEKVLYTAIVTATGGRDGSVVSSDNVLNVKLSVPQGLGGPGGSGTNPEQLFAAGYSACFIGALKFVANKEKVDLPAEPRVEGRVGIGEIPGGFGLVVELRIAVSGMERSMLQTLVDKAHRVCPYSNATRGNIDVVLILID [Source organism chain B]=Xylella fastidiosa [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Xylella fastidiosa [Accession]=MF7000841 [Entry] [Entry number]=1026 [Entry name]=Hydroperoxide resistance protein, OhrB (Bacillus subtilis) [PDB ID]=2bjo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=OsmC-like protein [Evidence level]=Direct evidence [Evidence text]=Ohr is a tightly folded homodimer with a large buried hydrophobic surface area. The two monomers are tightly wrapped around each other in a head-to-tail orientation. Dimerization is dominated by helix–helix packing interactions of two long helices at the center of the hydrophobic core of the dimeric enzyme. Also, each β-sheet is composed of six strands, three from one monomer and three from the other (beta sheet augmentation). The hydrophobic core, as well as the surrounding β-sheets, are generated by combining elements of both monomers, therefore, it is clear that the two polypeptide chains have to fold together to form active Ohr, and that each monomer would individually be unstable. The two active sites are also located at the dimer interface (PMID:12485986). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000837,MF7000838,MF7000839,MF7000840,MF7000841,MF7000842,MF7000843 [UniProt ID chain A]=P80242 [UniProt boundaries chain A]=2-136 [UniProt coverage chain A]=99% [Name chain A]=Organic hydroperoxide resistance protein OhrB [UniProt sequence chain A]=MALFTAKVTARGGRAGHITSDDGVLDFDIVMPNAKKEGQTGTNPEQLFAAGYAACFGGALEHVAKEQNIEIDSEIEGQVSLMKDESDGGFKIGVTLVVNTKDLDREKAQELVNAAHEFCPYSKATRGNVDVKLELK [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P80242 [UniProt boundaries chain B]=2-136 [UniProt coverage chain B]=99% [Name chain B]=Organic hydroperoxide resistance protein OhrB [UniProt sequence chain B]=MALFTAKVTARGGRAGHITSDDGVLDFDIVMPNAKKEGQTGTNPEQLFAAGYAACFGGALEHVAKEQNIEIDSEIEGQVSLMKDESDGGFKIGVTLVVNTKDLDREKAQELVNAAHEFCPYSKATRGNVDVKLELK [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Bacillus subtilis [Accession]=MF7000842 [Entry] [Entry number]=1027 [Entry name]=Hydroperoxide resistance protein (Burkholderia pseudomallei) [PDB ID]=6uhw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=OsmC-like protein [Evidence level]=Direct evidence [Evidence text]=Ohr is a tightly folded homodimer with a large buried hydrophobic surface area. The two monomers are tightly wrapped around each other in a head-to-tail orientation. Dimerization is dominated by helix–helix packing interactions of two long helices at the center of the hydrophobic core of the dimeric enzyme. Also, each β-sheet is composed of six strands, three from one monomer and three from the other (beta sheet augmentation). The hydrophobic core, as well as the surrounding β-sheets, are generated by combining elements of both monomers, therefore, it is clear that the two polypeptide chains have to fold together to form active Ohr, and that each monomer would individually be unstable. The two active sites are also located at the dimer interface (PMID:12485986). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000837,MF7000838,MF7000839,MF7000840,MF7000841,MF7000842,MF7000843 [UniProt ID chain A]=Q3JK82 [UniProt boundaries chain A]=1-139 [UniProt coverage chain A]=100% [Name chain A]=Organic hydroperoxide resistance protein [UniProt sequence chain A]=MNILYKTAATSTGGRDGRATSHDQKLDVKLSAPRELGGAGAEGTNPEQLFAAGYSACFLSAMKFVAGQNKQTLPADTTVTAEVGIGPNEEGGFALDVELRVALPGLDAAAAKTLVDRAHHVCPYSNATRNNVAVRLVVA [Source organism chain A]=Burkholderia pseudomallei [UniProt ID chain B]=Q3JK82 [UniProt boundaries chain B]=1-139 [UniProt coverage chain B]=100% [Name chain B]=Organic hydroperoxide resistance protein [UniProt sequence chain B]=MNILYKTAATSTGGRDGRATSHDQKLDVKLSAPRELGGAGAEGTNPEQLFAAGYSACFLSAMKFVAGQNKQTLPADTTVTAEVGIGPNEEGGFALDVELRVALPGLDAAAAKTLVDRAHHVCPYSNATRNNVAVRLVVA [Source organism chain B]=Burkholderia pseudomallei [ExpTech]=NMR [Resolution]=N/A [Source organism]=Burkholderia pseudomallei [Accession]=MF7000843 [Entry] [Entry number]=1028 [Entry name]=Bleomycin-binding protein (Streptoalloteichus hindustanus) [PDB ID]=1byl [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase superfamily [Evidence level]=Indirect evidence [Evidence text]=The bleomycin resistance protein forms a tight dimer with a large hydrophobic interface and domain-swapping involving the N-terminal end of both monomers. Only dimeric form could be detected in solution by several dedicated methods. The antibiotic binds to he dimer interface contacting both monomers (PMID:7516875). Temperature-induced equilibrium unfolding experiments on the Shble protein and its engineered variants suggested a two-state model of unfolding (although unfolding was largely irreversible with only 40% of the native folded signal regained during the refolding phase) and the strong stabilizing effect of bleomycin on the dimer based on largely increased thermostability of the protein in the presence of the antibiotic (PMID:15640151). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000844,MF7000845,MF7000846,MF7000847,MF7000848,MF7000849,MF7000850 [UniProt ID chain A]=P17493 [UniProt boundaries chain A]=1-121 [UniProt coverage chain A]=97% [Name chain A]=Bleomycin resistance protein [UniProt sequence chain A]=MAKLTSAVPVLTARDVAGAVEFWTDRLGFSRDFVEDDFAGVVRDDVTLFISAVQDQVVPDNTLAWVWVRGLDELYAEWSEVVSTNFRDASGPAMTEIGEQPWGREFALRDPAGNCVHFVAEEQD [Source organism chain A]=Streptoalloteichus hindustanus [UniProt ID chain A-2]=P17493 [UniProt boundaries chain A-2]=1-121 [UniProt coverage chain A-2]=97% [Name chain A-2]=Bleomycin resistance protein [UniProt sequence chain A-2]=MAKLTSAVPVLTARDVAGAVEFWTDRLGFSRDFVEDDFAGVVRDDVTLFISAVQDQVVPDNTLAWVWVRGLDELYAEWSEVVSTNFRDASGPAMTEIGEQPWGREFALRDPAGNCVHFVAEEQD [Source organism chain A-2]=Streptoalloteichus hindustanus [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Streptoalloteichus hindustanus [Accession]=MF7000844 [Entry] [Entry number]=1029 [Entry name]=Bleomycin-binding protein (Streptomyces verticillus) [PDB ID]=1qto [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase superfamily [Evidence level]=Indirect evidence [Evidence text]=The bleomycin resistance protein forms a tight dimer with a large hydrophobic interface and domain-swapping involving the N-terminal end of both monomers. Only dimeric form could be detected in solution by several dedicated methods. The antibiotic binds to he dimer interface contacting both monomers (PMID:7516875). Temperature-induced equilibrium unfolding experiments on the Shble protein and its engineered variants suggested a two-state model of unfolding (although unfolding was largely irreversible with only 40% of the native folded signal regained during the refolding phase) and the strong stabilizing effect of bleomycin on the dimer based on largely increased thermostability of the protein in the presence of the antibiotic (PMID:15640151). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000844,MF7000845,MF7000846,MF7000847,MF7000848,MF7000849,MF7000850 [UniProt ID chain A]=Q53793 [UniProt boundaries chain A]=1-122 [UniProt coverage chain A]=100% [Name chain A]=Bleomycin resistance protein [UniProt sequence chain A]=MVKFLGAVPVLTAVDVPANVSFWVDTLGFEKDFGDRDFAGVRRGDIRLHISRTEHQIVADNTSAWIEVTDPDALHEEWARAVSTDYADTSGPAMTPVGESPAGREFAVRDPAGNCVHFTAGE [Source organism chain A]=Streptomyces verticillus [UniProt ID chain A-2]=Q53793 [UniProt boundaries chain A-2]=1-122 [UniProt coverage chain A-2]=100% [Name chain A-2]=Bleomycin resistance protein [UniProt sequence chain A-2]=MVKFLGAVPVLTAVDVPANVSFWVDTLGFEKDFGDRDFAGVRRGDIRLHISRTEHQIVADNTSAWIEVTDPDALHEEWARAVSTDYADTSGPAMTPVGESPAGREFAVRDPAGNCVHFTAGE [Source organism chain A-2]=Streptomyces verticillus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Streptomyces verticillus [Accession]=MF7000845 [Entry] [Entry number]=1030 [Entry name]=Bleomycin-binding protein with metal-free bleomycin (Streptomyces verticillus) [PDB ID]=1jie [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase superfamily [Evidence level]=Indirect evidence [Evidence text]=The bleomycin resistance protein forms a tight dimer with a large hydrophobic interface and domain-swapping involving the N-terminal end of both monomers. Only dimeric form could be detected in solution by several dedicated methods. The antibiotic binds to he dimer interface contacting both monomers (PMID:7516875). Temperature-induced equilibrium unfolding experiments on the Shble protein and its engineered variants suggested a two-state model of unfolding (although unfolding was largely irreversible with only 40% of the native folded signal regained during the refolding phase) and the strong stabilizing effect of bleomycin on the dimer based on largely increased thermostability of the protein in the presence of the antibiotic (PMID:15640151). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000844,MF7000845,MF7000846,MF7000847,MF7000848,MF7000849,MF7000850 [UniProt ID chain A]=Q53793 [UniProt boundaries chain A]=1-122 [UniProt coverage chain A]=100% [Name chain A]=Bleomycin resistance protein [UniProt sequence chain A]=MVKFLGAVPVLTAVDVPANVSFWVDTLGFEKDFGDRDFAGVRRGDIRLHISRTEHQIVADNTSAWIEVTDPDALHEEWARAVSTDYADTSGPAMTPVGESPAGREFAVRDPAGNCVHFTAGE [Source organism chain A]=Streptomyces verticillus [UniProt ID chain B]=Q53793 [UniProt boundaries chain B]=1-122 [UniProt coverage chain B]=100% [Name chain B]=Bleomycin resistance protein [UniProt sequence chain B]=MVKFLGAVPVLTAVDVPANVSFWVDTLGFEKDFGDRDFAGVRRGDIRLHISRTEHQIVADNTSAWIEVTDPDALHEEWARAVSTDYADTSGPAMTPVGESPAGREFAVRDPAGNCVHFTAGE [Source organism chain B]=Streptomyces verticillus [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Streptomyces verticillus [Accession]=MF7000846 [Entry] [Entry number]=1031 [Entry name]=Bleomycin-binding protein with copper(II)-bleomycin (Treptomyces verticillus) [PDB ID]=1jif [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase superfamily [Evidence level]=Indirect evidence [Evidence text]=The bleomycin resistance protein forms a tight dimer with a large hydrophobic interface and domain-swapping involving the N-terminal end of both monomers. Only dimeric form could be detected in solution by several dedicated methods. The antibiotic binds to he dimer interface contacting both monomers (PMID:7516875). Temperature-induced equilibrium unfolding experiments on the Shble protein and its engineered variants suggested a two-state model of unfolding (although unfolding was largely irreversible with only 40% of the native folded signal regained during the refolding phase) and the strong stabilizing effect of bleomycin on the dimer based on largely increased thermostability of the protein in the presence of the antibiotic (PMID:15640151). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000844,MF7000845,MF7000846,MF7000847,MF7000848,MF7000849,MF7000850 [UniProt ID chain A]=Q53793 [UniProt boundaries chain A]=1-122 [UniProt coverage chain A]=100% [Name chain A]=Bleomycin resistance protein [UniProt sequence chain A]=MVKFLGAVPVLTAVDVPANVSFWVDTLGFEKDFGDRDFAGVRRGDIRLHISRTEHQIVADNTSAWIEVTDPDALHEEWARAVSTDYADTSGPAMTPVGESPAGREFAVRDPAGNCVHFTAGE [Source organism chain A]=Streptomyces verticillus [UniProt ID chain B]=Q53793 [UniProt boundaries chain B]=1-122 [UniProt coverage chain B]=100% [Name chain B]=Bleomycin resistance protein [UniProt sequence chain B]=MVKFLGAVPVLTAVDVPANVSFWVDTLGFEKDFGDRDFAGVRRGDIRLHISRTEHQIVADNTSAWIEVTDPDALHEEWARAVSTDYADTSGPAMTPVGESPAGREFAVRDPAGNCVHFTAGE [Source organism chain B]=Streptomyces verticillus [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Streptomyces verticillus [Accession]=MF7000847 [Entry] [Entry number]=1032 [Entry name]=Bleomycin-binding protein, mutant (Streptoalloteichus hindustanus) [PDB ID]=1xrk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase superfamily [Evidence level]=Indirect evidence [Evidence text]=The bleomycin resistance protein forms a tight dimer with a large hydrophobic interface and domain-swapping involving the N-terminal end of both monomers. Only dimeric form could be detected in solution by several dedicated methods. The antibiotic binds to he dimer interface contacting both monomers (PMID:7516875). Temperature-induced equilibrium unfolding experiments on the Shble protein and its engineered variants suggested a two-state model of unfolding (although unfolding was largely irreversible with only 40% of the native folded signal regained during the refolding phase) and the strong stabilizing effect of bleomycin on the dimer based on largely increased thermostability of the protein in the presence of the antibiotic (PMID:15640151). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000844,MF7000845,MF7000846,MF7000847,MF7000848,MF7000849,MF7000850 [UniProt ID chain A]=P17493 [UniProt boundaries chain A]=2-121 [UniProt coverage chain A]=96% [Name chain A]=Bleomycin resistance protein [UniProt sequence chain A]=MAKLTSAVPVLTARDVAGAVEFWTDRLGFSRDFVEDDFAGVVRDDVTLFISAVQDQVVPDNTLAWVWVRGLDELYAEWSEVVSTNFRDASGPAMTEIGEQPWGREFALRDPAGNCVHFVAEEQD [Source organism chain A]=Streptoalloteichus hindustanus [UniProt ID chain B]=P17493 [UniProt boundaries chain B]=2-122 [UniProt coverage chain B]=97% [Name chain B]=Bleomycin resistance protein [UniProt sequence chain B]=MAKLTSAVPVLTARDVAGAVEFWTDRLGFSRDFVEDDFAGVVRDDVTLFISAVQDQVVPDNTLAWVWVRGLDELYAEWSEVVSTNFRDASGPAMTEIGEQPWGREFALRDPAGNCVHFVAEEQD [Source organism chain B]=Streptoalloteichus hindustanus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Streptoalloteichus hindustanus [Accession]=MF7000848 [Entry] [Entry number]=1033 [Entry name]=Zorbamycin-binding protein (ZbmA) (Streptomyces flavoviridis) [PDB ID]=4iag [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase superfamily [Evidence level]=Indirect evidence [Evidence text]=The bleomycin resistance protein forms a tight dimer with a large hydrophobic interface and domain-swapping involving the N-terminal end of both monomers. Only dimeric form could be detected in solution by several dedicated methods. The antibiotic binds to he dimer interface contacting both monomers (PMID:7516875). Temperature-induced equilibrium unfolding experiments on the Shble protein and its engineered variants suggested a two-state model of unfolding (although unfolding was largely irreversible with only 40% of the native folded signal regained during the refolding phase) and the strong stabilizing effect of bleomycin on the dimer based on largely increased thermostability of the protein in the presence of the antibiotic (PMID:15640151). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000844,MF7000845,MF7000846,MF7000847,MF7000848,MF7000849,MF7000850 [UniProt ID chain A]=B9UIZ4 [UniProt boundaries chain A]=2-122 [UniProt coverage chain A]=91% [Name chain A]=Zbm binding protein [UniProt sequence chain A]=MAVLLSGVPVLAALDVSTTQKFWIEVLGFTEEFLTEDFGGVSRDGVELFICSVEDQVVPDNTQAWLRVRDIDALHAEWSARVSSDYADASHPAMTAIREVPWGREFGLRDPAGNLVHFSELSEAAETTRTVR [Source organism chain A]=Streptomyces pilosus [UniProt ID chain A-2]=B9UIZ4 [UniProt boundaries chain A-2]=2-122 [UniProt coverage chain A-2]=91% [Name chain A-2]=Zbm binding protein [UniProt sequence chain A-2]=MAVLLSGVPVLAALDVSTTQKFWIEVLGFTEEFLTEDFGGVSRDGVELFICSVEDQVVPDNTQAWLRVRDIDALHAEWSARVSSDYADASHPAMTAIREVPWGREFGLRDPAGNLVHFSELSEAAETTRTVR [Source organism chain A-2]=Streptomyces pilosus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Streptomyces pilosus [Accession]=MF7000849 [Entry] [Entry number]=1034 [Entry name]=Zorbamycin-binding protein (ZbmA) with zorbamycin (Streptomyces flavoviridis) [PDB ID]=5cj3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Glyoxalase superfamily [Evidence level]=Indirect evidence [Evidence text]=The bleomycin resistance protein forms a tight dimer with a large hydrophobic interface and domain-swapping involving the N-terminal end of both monomers. Only dimeric form could be detected in solution by several dedicated methods. The antibiotic binds to he dimer interface contacting both monomers (PMID:7516875). Temperature-induced equilibrium unfolding experiments on the Shble protein and its engineered variants suggested a two-state model of unfolding (although unfolding was largely irreversible with only 40% of the native folded signal regained during the refolding phase) and the strong stabilizing effect of bleomycin on the dimer based on largely increased thermostability of the protein in the presence of the antibiotic (PMID:15640151). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000844,MF7000845,MF7000846,MF7000847,MF7000848,MF7000849,MF7000850 [UniProt ID chain A]=B9UIZ4 [UniProt boundaries chain A]=1-123 [UniProt coverage chain A]=93% [Name chain A]=Zbm binding protein [UniProt sequence chain A]=MAVLLSGVPVLAALDVSTTQKFWIEVLGFTEEFLTEDFGGVSRDGVELFICSVEDQVVPDNTQAWLRVRDIDALHAEWSARVSSDYADASHPAMTAIREVPWGREFGLRDPAGNLVHFSELSEAAETTRTVR [Source organism chain A]=Streptomyces pilosus [UniProt ID chain B]=B9UIZ4 [UniProt boundaries chain B]=1-126 [UniProt coverage chain B]=95% [Name chain B]=Zbm binding protein [UniProt sequence chain B]=MAVLLSGVPVLAALDVSTTQKFWIEVLGFTEEFLTEDFGGVSRDGVELFICSVEDQVVPDNTQAWLRVRDIDALHAEWSARVSSDYADASHPAMTAIREVPWGREFGLRDPAGNLVHFSELSEAAETTRTVR [Source organism chain B]=Streptomyces pilosus [ExpTech]=X-ray [Resolution]=1.65 [Source organism]=Streptomyces pilosus [Accession]=MF7000850 [Entry] [Entry number]=1035 [Entry name]=RbcX (Anabaena CA) [PDB ID]=2peo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Chaperonin-like RbcX [Sequence domain]=Chaperonin-like RbcX [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. However, RbcX is a dimer in solution (PMID:17574029) and its biologically relevant form is the homodimer (a monomeric form with this fold is not known PMID:23295968, PMID:21821880). The structure is highly intertwined with the interface being extended and hydrophobic between the two four-helix-bundle cores and by the exchange of the C-terminal parts of the long a4 helices between the two subunits (PMID:21821880). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000851,MF7000852,MF7000853,MF7000854,MF7000855,MF7000321 [UniProt ID chain A]=Q44212 [UniProt boundaries chain A]=1-115 [UniProt coverage chain A]=85% [Name chain A]=RuBisCO chaperone RbcX [UniProt sequence chain A]=MNLKQIAKDTAKTLQSYLTYQALRTVLAQLGETNPPLALWLHNFSAGKVQDGEKYIEELFLEKPDLALRIMTVREHIAEEIAEFLPEMVVTGIQQANMEKRRQHLERMTQVSLSHPSPESEQQQFSDPDWDNLAS [Source organism chain A]=Anabaena sp [UniProt ID chain B]=Q44212 [UniProt boundaries chain B]=1-114 [UniProt coverage chain B]=84% [Name chain B]=RuBisCO chaperone RbcX [UniProt sequence chain B]=MNLKQIAKDTAKTLQSYLTYQALRTVLAQLGETNPPLALWLHNFSAGKVQDGEKYIEELFLEKPDLALRIMTVREHIAEEIAEFLPEMVVTGIQQANMEKRRQHLERMTQVSLSHPSPESEQQQFSDPDWDNLAS [Source organism chain B]=Anabaena sp [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Anabaena sp [Accession]=MF7000851 [Entry] [Entry number]=1036 [Entry name]=RbcX (Anabaena sp. CA = ATCC 33047) [PDB ID]=2peq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Chaperonin-like RbcX [Sequence domain]=Chaperonin-like RbcX [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. However, RbcX is a dimer in solution (PMID:17574029) and its biologically relevant form is the homodimer (a monomeric form with this fold is not known PMID:23295968, PMID:21821880). The structure is highly intertwined with the interface being extended and hydrophobic between the two four-helix-bundle cores and by the exchange of the C-terminal parts of the long a4 helices between the two subunits (PMID:21821880). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000851,MF7000852,MF7000853,MF7000854,MF7000855,MF7000321 [UniProt ID chain A]=Q44177 [UniProt boundaries chain A]=1-109 [UniProt coverage chain A]=81% [Name chain A]=RuBisCO chaperone RbcX [UniProt sequence chain A]=MEFKKVAKETAITLQSYLTYQAVRLISQQLSETNPGQAIWLGEFSKRHPIQESDLYLEAMMLENKELVLRILTVRENLAEGVLEFLPEMVLSQIKQSNGNHRRSLLERLTQVDSSSTDQTEPNPGESDTSEDSE [Source organism chain A]=quadruplicatum) [UniProt ID chain B]=Q44177 [UniProt boundaries chain B]=1-109 [UniProt coverage chain B]=81% [Name chain B]=RuBisCO chaperone RbcX [UniProt sequence chain B]=MEFKKVAKETAITLQSYLTYQAVRLISQQLSETNPGQAIWLGEFSKRHPIQESDLYLEAMMLENKELVLRILTVRENLAEGVLEFLPEMVLSQIKQSNGNHRRSLLERLTQVDSSSTDQTEPNPGESDTSEDSE [Source organism chain B]=quadruplicatum) [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=quadruplicatum) [Accession]=MF7000852 [Entry] [Entry number]=1037 [Entry name]=RbcX (Anabaena sp.) [PDB ID]=3hyb [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Chaperonin-like RbcX [Sequence domain]=Chaperonin-like RbcX [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. However, RbcX is a dimer in solution (PMID:17574029) and its biologically relevant form is the homodimer (a monomeric form with this fold is not known PMID:23295968, PMID:21821880). The structure is highly intertwined with the interface being extended and hydrophobic between the two four-helix-bundle cores and by the exchange of the C-terminal parts of the long a4 helices between the two subunits (PMID:21821880). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000851,MF7000852,MF7000853,MF7000854,MF7000855,MF7000321 [UniProt ID chain A]=Q44212 [UniProt boundaries chain A]=1-105 [UniProt coverage chain A]=77% [Name chain A]=RuBisCO chaperone RbcX [UniProt sequence chain A]=MNLKQIAKDTAKTLQSYLTYQALRTVLAQLGETNPPLALWLHNFSAGKVQDGEKYIEELFLEKPDLALRIMTVREHIAEEIAEFLPEMVVTGIQQANMEKRRQHLERMTQVSLSHPSPESEQQQFSDPDWDNLAS [Source organism chain A]=Anabaena sp [UniProt ID chain B]=Q44212 [UniProt boundaries chain B]=1-105 [UniProt coverage chain B]=77% [Name chain B]=RuBisCO chaperone RbcX [UniProt sequence chain B]=MNLKQIAKDTAKTLQSYLTYQALRTVLAQLGETNPPLALWLHNFSAGKVQDGEKYIEELFLEKPDLALRIMTVREHIAEEIAEFLPEMVVTGIQQANMEKRRQHLERMTQVSLSHPSPESEQQQFSDPDWDNLAS [Source organism chain B]=Anabaena sp [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Anabaena sp [Accession]=MF7000853 [Entry] [Entry number]=1038 [Entry name]=RbcX, mutant C103A (Thermosynechococcus elongatus) [PDB ID]=3q20 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Chaperonin-like RbcX [Sequence domain]=Chaperonin-like RbcX [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. However, RbcX is a dimer in solution (PMID:17574029) and its biologically relevant form is the homodimer (a monomeric form with this fold is not known PMID:23295968, PMID:21821880). The structure is highly intertwined with the interface being extended and hydrophobic between the two four-helix-bundle cores and by the exchange of the C-terminal parts of the long a4 helices between the two subunits (PMID:21821880). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000851,MF7000852,MF7000853,MF7000854,MF7000855,MF7000321 [UniProt ID chain A]=Q8DIS6 [UniProt boundaries chain A]=1-114 [UniProt coverage chain A]=90% [Name chain A]=RuBisCO chaperone RbcX [UniProt sequence chain A]=MDVKHIAKQTTKTLISYLTYQAVRTVIGQLAETDPPRSLWLHQFTSQESIQDGERYLEALFREQPDLGFRILTVREHLAEMVADYLPEMLRAGIQQANLQQRCQQLERMTQVSEANVENSNLETPE [Source organism chain A]=Thermosynechococcus vestitus [UniProt ID chain B]=Q8DIS6 [UniProt boundaries chain B]=2-107 [UniProt coverage chain B]=84% [Name chain B]=RuBisCO chaperone RbcX [UniProt sequence chain B]=MDVKHIAKQTTKTLISYLTYQAVRTVIGQLAETDPPRSLWLHQFTSQESIQDGERYLEALFREQPDLGFRILTVREHLAEMVADYLPEMLRAGIQQANLQQRCQQLERMTQVSEANVENSNLETPE [Source organism chain B]=Thermosynechococcus vestitus [ExpTech]=X-ray [Resolution]=1.71 [Source organism]=Thermosynechococcus vestitus [Accession]=MF7000854 [Entry] [Entry number]=1039 [Entry name]=AtRbcX2 (Arabidopsis thaliana) [PDB ID]=4gr6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Chaperonin-like RbcX [Sequence domain]=Chaperonin-like RbcX [Evidence level]=Indirect evidence [Evidence text]=There is no information on the stability/disoder of the monomeric forms. However, RbcX is a dimer in solution (PMID:17574029) and its biologically relevant form is the homodimer (a monomeric form with this fold is not known PMID:23295968, PMID:21821880). The structure is highly intertwined with the interface being extended and hydrophobic between the two four-helix-bundle cores and by the exchange of the C-terminal parts of the long a4 helices between the two subunits (PMID:21821880). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000851,MF7000852,MF7000853,MF7000854,MF7000855,MF7000321 [UniProt ID chain A]=Q8L9X2 [UniProt boundaries chain A]=88-191 [UniProt coverage chain A]=51% [Name chain A]=Chaperonin-like RbcX protein 2, chloroplastic [UniProt sequence chain A]=MVSAWFVVGSPVMDSSSSPCLCLDAHTTGTIRRKKILGKARNLELGSSFTGSRIVFRLSPKRVSRIANRKSKKLLIVNEDVAGNYDDTFGDVQKQIVNYFTYKAVRTVLHQLYEMNPPQYTWFYNHIITNRPTDGKRFLRALGKESQELAERVMITRLHLYGKWIKKCDHGKIYQEISDENLALMRERLMETVIWPSDDTNSR [Source organism chain A]=Arabidopsis thaliana [UniProt ID chain B]=Q8L9X2 [UniProt boundaries chain B]=88-192 [UniProt coverage chain B]=51% [Name chain B]=Chaperonin-like RbcX protein 2, chloroplastic [UniProt sequence chain B]=MVSAWFVVGSPVMDSSSSPCLCLDAHTTGTIRRKKILGKARNLELGSSFTGSRIVFRLSPKRVSRIANRKSKKLLIVNEDVAGNYDDTFGDVQKQIVNYFTYKAVRTVLHQLYEMNPPQYTWFYNHIITNRPTDGKRFLRALGKESQELAERVMITRLHLYGKWIKKCDHGKIYQEISDENLALMRERLMETVIWPSDDTNSR [Source organism chain B]=Arabidopsis thaliana [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Arabidopsis thaliana [Accession]=MF7000855 [Entry] [Entry number]=1040 [Entry name]=Beta-carbonic anhydrase isoform I (TvaCA1) (Trichomonas vaginalis protozoan) [PDB ID]=6y04 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Carbonic anhydrase [Evidence level]=Indirect evidence [Evidence text]=The native carbonic anhydrase is dimeric in solution, in agreement with being a tightly associated dimer with a large, hydrophobic buried surface area. The extended β-sheet core consisting of ten β–strands is equally contributed by the two monomers, and the N-terminal helix of each monomer extends around the other monomer. Based on the highly intertwined structure, the monomeric form is most probably not a stable, independently folding unit. The two active sites are also located in clefts at the dimeric interface, further suggesting that dimer is the functional form (PMID:32515610). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000278,MF7000279,MF7000856,MF7000857,MF7000858,MF7000859 [UniProt ID chain A]=A2ENQ8 [UniProt boundaries chain A]=1-182 [UniProt coverage chain A]=100% [Name chain A]=Carbonic anhydrase [UniProt sequence chain A]=MSQLELITSANQAFLEANPELTKLNKAPQRHIAIVTCMDTRLVNFAEDAIGVKRGEATVIKAAGNGIWTTGLSDIVVSLLVSIYELGVQEIFIMGHECCGMTHASTDSLGAQMLKSGIKPEDIEKFKSDLSKWVDDFKDPIDNIKNSVRCVRENPLIPKNIPIHGLLIHPDTGKVTTIINGY [Source organism chain A]=Trichomonas vaginalis [UniProt ID chain B]=A2ENQ8 [UniProt boundaries chain B]=1-182 [UniProt coverage chain B]=100% [Name chain B]=Carbonic anhydrase [UniProt sequence chain B]=MSQLELITSANQAFLEANPELTKLNKAPQRHIAIVTCMDTRLVNFAEDAIGVKRGEATVIKAAGNGIWTTGLSDIVVSLLVSIYELGVQEIFIMGHECCGMTHASTDSLGAQMLKSGIKPEDIEKFKSDLSKWVDDFKDPIDNIKNSVRCVRENPLIPKNIPIHGLLIHPDTGKVTTIINGY [Source organism chain B]=Trichomonas vaginalis [ExpTech]=X-ray [Resolution]=2.48 [Source organism]=Trichomonas vaginalis [Accession]=MF7000856 [Entry] [Entry number]=1041 [Entry name]=CafB, disulfide-bonded form (Aspergillus fumigatus) [PDB ID]=7cxx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Carbonic anhydrase [Evidence level]=Indirect evidence [Evidence text]=The native carbonic anhydrase is dimeric in solution, in agreement with being a tightly associated dimer with a large, hydrophobic buried surface area. The extended β-sheet core consisting of ten β–strands is equally contributed by the two monomers, and the N-terminal helix of each monomer extends around the other monomer. Based on the highly intertwined structure, the monomeric form is most probably not a stable, independently folding unit. The two active sites are also located in clefts at the dimeric interface, further suggesting that dimer is the functional form (PMID:32515610). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000278,MF7000279,MF7000856,MF7000857,MF7000858,MF7000859 [UniProt ID chain A]=A4DA32 [UniProt boundaries chain A]=9-224 [UniProt coverage chain A]=94% [Name chain A]=Carbonic anhydrase [UniProt sequence chain A]=MEPSDQKVDTVPQYLKQSHERIFENNRAWVATKMKDDPAFFEKLSAGQTPEYLYIGCSDSRVPANEIMGLEAGEVFVHRNIANLVPNTDLNVMSVINYAVRHLQVKHIVVCGHYHCGGVKAALTPSDLGLLNPWLRNVRDVYRLHEQELDGIQDATARYRRLVELNVIESCRNVIKTAAVQQSFHERQFPVVHGWIFDVETGLLRDLEIDFEETLRDIKKIYNLAPGS [Source organism chain A]=Af293) [UniProt ID chain B]=A4DA32 [UniProt boundaries chain B]=21-221 [UniProt coverage chain B]=88% [Name chain B]=Carbonic anhydrase [UniProt sequence chain B]=MEPSDQKVDTVPQYLKQSHERIFENNRAWVATKMKDDPAFFEKLSAGQTPEYLYIGCSDSRVPANEIMGLEAGEVFVHRNIANLVPNTDLNVMSVINYAVRHLQVKHIVVCGHYHCGGVKAALTPSDLGLLNPWLRNVRDVYRLHEQELDGIQDATARYRRLVELNVIESCRNVIKTAAVQQSFHERQFPVVHGWIFDVETGLLRDLEIDFEETLRDIKKIYNLAPGS [Source organism chain B]=Af293) [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Af293) [Accession]=MF7000857 [Entry] [Entry number]=1042 [Entry name]=CafB, C116 flipped form (Aspergillus fumigatus) [PDB ID]=7cxw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Carbonic anhydrase [Evidence level]=Indirect evidence [Evidence text]=The native carbonic anhydrase is dimeric in solution, in agreement with being a tightly associated dimer with a large, hydrophobic buried surface area. The extended β-sheet core consisting of ten β–strands is equally contributed by the two monomers, and the N-terminal helix of each monomer extends around the other monomer. Based on the highly intertwined structure, the monomeric form is most probably not a stable, independently folding unit. The two active sites are also located in clefts at the dimeric interface, further suggesting that dimer is the functional form (PMID:32515610). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000278,MF7000279,MF7000856,MF7000857,MF7000858,MF7000859 [UniProt ID chain A]=A4DA32 [UniProt boundaries chain A]=10-225 [UniProt coverage chain A]=94% [Name chain A]=Carbonic anhydrase [UniProt sequence chain A]=MEPSDQKVDTVPQYLKQSHERIFENNRAWVATKMKDDPAFFEKLSAGQTPEYLYIGCSDSRVPANEIMGLEAGEVFVHRNIANLVPNTDLNVMSVINYAVRHLQVKHIVVCGHYHCGGVKAALTPSDLGLLNPWLRNVRDVYRLHEQELDGIQDATARYRRLVELNVIESCRNVIKTAAVQQSFHERQFPVVHGWIFDVETGLLRDLEIDFEETLRDIKKIYNLAPGS [Source organism chain A]=Af293) [UniProt ID chain B]=A4DA32 [UniProt boundaries chain B]=10-225 [UniProt coverage chain B]=94% [Name chain B]=Carbonic anhydrase [UniProt sequence chain B]=MEPSDQKVDTVPQYLKQSHERIFENNRAWVATKMKDDPAFFEKLSAGQTPEYLYIGCSDSRVPANEIMGLEAGEVFVHRNIANLVPNTDLNVMSVINYAVRHLQVKHIVVCGHYHCGGVKAALTPSDLGLLNPWLRNVRDVYRLHEQELDGIQDATARYRRLVELNVIESCRNVIKTAAVQQSFHERQFPVVHGWIFDVETGLLRDLEIDFEETLRDIKKIYNLAPGS [Source organism chain B]=Af293) [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Af293) [Accession]=MF7000858 [Entry] [Entry number]=1043 [Entry name]=CafB, Zn-bound form (Aspergillus fumigatus) [PDB ID]=7cxy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Carbonic anhydrase [Evidence level]=Indirect evidence [Evidence text]=The native carbonic anhydrase is dimeric in solution, in agreement with being a tightly associated dimer with a large, hydrophobic buried surface area. The extended β-sheet core consisting of ten β–strands is equally contributed by the two monomers, and the N-terminal helix of each monomer extends around the other monomer. Based on the highly intertwined structure, the monomeric form is most probably not a stable, independently folding unit. The two active sites are also located in clefts at the dimeric interface, further suggesting that dimer is the functional form (PMID:32515610). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000278,MF7000279,MF7000856,MF7000857,MF7000858,MF7000859 [UniProt ID chain A]=A4DA32 [UniProt boundaries chain A]=9-222 [UniProt coverage chain A]=93% [Name chain A]=Carbonic anhydrase [UniProt sequence chain A]=MEPSDQKVDTVPQYLKQSHERIFENNRAWVATKMKDDPAFFEKLSAGQTPEYLYIGCSDSRVPANEIMGLEAGEVFVHRNIANLVPNTDLNVMSVINYAVRHLQVKHIVVCGHYHCGGVKAALTPSDLGLLNPWLRNVRDVYRLHEQELDGIQDATARYRRLVELNVIESCRNVIKTAAVQQSFHERQFPVVHGWIFDVETGLLRDLEIDFEETLRDIKKIYNLAPGS [Source organism chain A]=Af293) [UniProt ID chain B]=A4DA32 [UniProt boundaries chain B]=16-222 [UniProt coverage chain B]=90% [Name chain B]=Carbonic anhydrase [UniProt sequence chain B]=MEPSDQKVDTVPQYLKQSHERIFENNRAWVATKMKDDPAFFEKLSAGQTPEYLYIGCSDSRVPANEIMGLEAGEVFVHRNIANLVPNTDLNVMSVINYAVRHLQVKHIVVCGHYHCGGVKAALTPSDLGLLNPWLRNVRDVYRLHEQELDGIQDATARYRRLVELNVIESCRNVIKTAAVQQSFHERQFPVVHGWIFDVETGLLRDLEIDFEETLRDIKKIYNLAPGS [Source organism chain B]=Af293) [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Af293) [Accession]=MF7000859 [Entry] [Entry number]=1044 [Entry name]=CcdB (Escherichia coli) [PDB ID]=3vub [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Toxin CcdB [Sequence domain]=CcdB protein [Evidence level]=Direct evidence [Evidence text]=The CcdB dimer forms via β-sheet extension, the hydrophobic core crosses the dimer interface. In solution, CcdBVfi is a dimer that shows two-state unfolding to unfolded monomers (PMID:19959472). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000860,MF7000861,MF7000862,MF7000863,MF7000864,MF7000865 [UniProt ID chain A]=P62554 [UniProt boundaries chain A]=1-101 [UniProt coverage chain A]=100% [Name chain A]=Toxin CcdB [UniProt sequence chain A]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P62554 [UniProt boundaries chain A-2]=1-101 [UniProt coverage chain A-2]=100% [Name chain A-2]=Toxin CcdB [UniProt sequence chain A-2]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Escherichia coli [Accession]=MF7000860 [Entry] [Entry number]=1045 [Entry name]=CcdB (Escherichia coli) [PDB ID]=4vub [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Toxin CcdB [Sequence domain]=CcdB protein [Evidence level]=Direct evidence [Evidence text]=The CcdB dimer forms via β-sheet extension, the hydrophobic core crosses the dimer interface. In solution, CcdBVfi is a dimer that shows two-state unfolding to unfolded monomers (PMID:19959472). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000860,MF7000861,MF7000862,MF7000863,MF7000864,MF7000865 [UniProt ID chain A]=P62554 [UniProt boundaries chain A]=1-101 [UniProt coverage chain A]=100% [Name chain A]=Toxin CcdB [UniProt sequence chain A]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P62554 [UniProt boundaries chain A-2]=1-101 [UniProt coverage chain A-2]=100% [Name chain A-2]=Toxin CcdB [UniProt sequence chain A-2]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.45 [Source organism]=Escherichia coli [Accession]=MF7000861 [Entry] [Entry number]=1046 [Entry name]=CcdBVfi-FormII (Aliivibrio fischeri) [PDB ID]=3jrz [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Toxin CcdB [Sequence domain]=CcdB protein [Evidence level]=Direct evidence [Evidence text]=The CcdB dimer forms via β-sheet extension, the hydrophobic core crosses the dimer interface. In solution, CcdBVfi is a dimer that shows two-state unfolding to unfolded monomers (PMID:19959472). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000860,MF7000861,MF7000862,MF7000863,MF7000864,MF7000865 [UniProt ID chain A]=Q84B82 [UniProt boundaries chain A]=2-105 [UniProt coverage chain A]=99% [Name chain A]=Toxin CcdB [UniProt sequence chain A]=MSQFTLYKNKDKSSAKTYPYFVDVQSDLLDNLNTRLVIPLTPIELLDKKAPSHLCPTIHIDEGDFIMLTQQMTSVPVKILSEPVNELSTFRNEIIAAIDFLITGI [Source organism chain A]=Aliivibrio fischeri [UniProt ID chain A-2]=Q84B82 [UniProt boundaries chain A-2]=2-105 [UniProt coverage chain A-2]=99% [Name chain A-2]=Toxin CcdB [UniProt sequence chain A-2]=MSQFTLYKNKDKSSAKTYPYFVDVQSDLLDNLNTRLVIPLTPIELLDKKAPSHLCPTIHIDEGDFIMLTQQMTSVPVKILSEPVNELSTFRNEIIAAIDFLITGI [Source organism chain A-2]=Aliivibrio fischeri [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Aliivibrio fischeri [Accession]=MF7000862 [Entry] [Entry number]=1047 [Entry name]=CcdB, mutant V46L (Escherichia coli) [PDB ID]=7epj [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Toxin CcdB [Sequence domain]=CcdB protein [Evidence level]=Direct evidence [Evidence text]=The CcdB dimer forms via β-sheet extension, the hydrophobic core crosses the dimer interface. In solution, CcdBVfi is a dimer that shows two-state unfolding to unfolded monomers (PMID:19959472). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000860,MF7000861,MF7000862,MF7000863,MF7000864,MF7000865 [UniProt ID chain A]=P62554 [UniProt boundaries chain A]=1-101 [UniProt coverage chain A]=100% [Name chain A]=Toxin CcdB [UniProt sequence chain A]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P62554 [UniProt boundaries chain A-2]=1-101 [UniProt coverage chain A-2]=100% [Name chain A-2]=Toxin CcdB [UniProt sequence chain A-2]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=Escherichia coli [Accession]=MF7000863 [Entry] [Entry number]=1048 [Entry name]=CcdB, mutant S12G (Escherichia coli) [PDB ID]=7epg [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Toxin CcdB [Sequence domain]=CcdB protein [Evidence level]=Direct evidence [Evidence text]=The CcdB dimer forms via β-sheet extension, the hydrophobic core crosses the dimer interface. In solution, CcdBVfi is a dimer that shows two-state unfolding to unfolded monomers (PMID:19959472). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000860,MF7000861,MF7000862,MF7000863,MF7000864,MF7000865 [UniProt ID chain A]=P62554 [UniProt boundaries chain A]=1-100 [UniProt coverage chain A]=99% [Name chain A]=Toxin CcdB [UniProt sequence chain A]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P62554 [UniProt boundaries chain A-2]=1-100 [UniProt coverage chain A-2]=99% [Name chain A-2]=Toxin CcdB [UniProt sequence chain A-2]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.63 [Source organism]=Escherichia coli [Accession]=MF7000864 [Entry] [Entry number]=1049 [Entry name]=CcdB, mutant S60E (Escherichia coli) [PDB ID]=7epi [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Bacterial toxin-antitoxin systems [Subclass]=Toxin CcdB [Sequence domain]=CcdB protein [Evidence level]=Direct evidence [Evidence text]=The CcdB dimer forms via β-sheet extension, the hydrophobic core crosses the dimer interface. In solution, CcdBVfi is a dimer that shows two-state unfolding to unfolded monomers (PMID:19959472). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000860,MF7000861,MF7000862,MF7000863,MF7000864,MF7000865 [UniProt ID chain A]=P62554 [UniProt boundaries chain A]=1-101 [UniProt coverage chain A]=100% [Name chain A]=Toxin CcdB [UniProt sequence chain A]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P62554 [UniProt boundaries chain A-2]=1-101 [UniProt coverage chain A-2]=100% [Name chain A-2]=Toxin CcdB [UniProt sequence chain A-2]=MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=1.93 [Source organism]=Escherichia coli [Accession]=MF7000865 [Entry] [Entry number]=1050 [Entry name]=Erv2p [PDB ID]=1jr8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=ERV/ALR sulfhydryl oxidase domain [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000866,MF7000270,MF7000867,MF7000868,MF7000869,MF7000870 [UniProt ID chain A]=Q12284 [UniProt boundaries chain A]=74-178 [UniProt coverage chain A]=53% [Name chain A]=FAD-linked sulfhydryl oxidase ERV2 [UniProt sequence chain A]=MKQIVKRSHAIRIVAALGIIGLWMFFSSNELSIATPGLIKAKSGIDEVQGAAAEKNDARLKEIEKQTIMPLMGDDKVKKEVGRASWKYFHTLLARFPDEPTPEEREKLHTFIGLYAELYPCGECSYHFVKLIEKYPVQTSSRTAAAMWGCHIHNKVNEYLKKDIYDCATILEDYDCGCSDSDGKRVSLEKEAKQHG [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=Q12284 [UniProt boundaries chain B]=75-179 [UniProt coverage chain B]=53% [Name chain B]=FAD-linked sulfhydryl oxidase ERV2 [UniProt sequence chain B]=MKQIVKRSHAIRIVAALGIIGLWMFFSSNELSIATPGLIKAKSGIDEVQGAAAEKNDARLKEIEKQTIMPLMGDDKVKKEVGRASWKYFHTLLARFPDEPTPEEREKLHTFIGLYAELYPCGECSYHFVKLIEKYPVQTSSRTAAAMWGCHIHNKVNEYLKKDIYDCATILEDYDCGCSDSDGKRVSLEKEAKQHG [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000866 [Entry] [Entry number]=1051 [Entry name]=Human FAD-linked augmenter of liver regeneration (ALR) [PDB ID]=3o55 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=ERV/ALR sulfhydryl oxidase domain [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000866,MF7000270,MF7000867,MF7000868,MF7000869,MF7000870 [UniProt ID chain A]=P55789 [UniProt boundaries chain A]=91-205 [UniProt coverage chain A]=56% [Name chain A]=FAD-linked sulfhydryl oxidase ALR [UniProt sequence chain A]=MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P55789 [UniProt boundaries chain A-2]=91-205 [UniProt coverage chain A-2]=56% [Name chain A-2]=FAD-linked sulfhydryl oxidase ALR [UniProt sequence chain A-2]=MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Homo sapiens [Accession]=MF7000867 [Entry] [Entry number]=1052 [Entry name]=Human ALR, mutant C142S [PDB ID]=3u2l [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=ERV/ALR sulfhydryl oxidase domain [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000866,MF7000270,MF7000867,MF7000868,MF7000869,MF7000870 [UniProt ID chain A]=P55789 [UniProt boundaries chain A]=91-205 [UniProt coverage chain A]=56% [Name chain A]=FAD-linked sulfhydryl oxidase ALR [UniProt sequence chain A]=MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P55789 [UniProt boundaries chain A-2]=91-205 [UniProt coverage chain A-2]=56% [Name chain A-2]=FAD-linked sulfhydryl oxidase ALR [UniProt sequence chain A-2]=MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=Homo sapiens [Accession]=MF7000868 [Entry] [Entry number]=1053 [Entry name]=Human ALR, mutant C142/145S [PDB ID]=3u2m [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=ERV/ALR sulfhydryl oxidase domain [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000866,MF7000270,MF7000867,MF7000868,MF7000869,MF7000870 [UniProt ID chain A]=P55789 [UniProt boundaries chain A]=91-205 [UniProt coverage chain A]=56% [Name chain A]=FAD-linked sulfhydryl oxidase ALR [UniProt sequence chain A]=MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P55789 [UniProt boundaries chain A-2]=91-205 [UniProt coverage chain A-2]=56% [Name chain A-2]=FAD-linked sulfhydryl oxidase ALR [UniProt sequence chain A-2]=MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Homo sapiens [Accession]=MF7000869 [Entry] [Entry number]=1054 [Entry name]=Human ALR, selenium substituted [PDB ID]=3u5s [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=ERV/ALR sulfhydryl oxidase domain [Evidence level]=No contradicting information [Evidence text]=There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000866,MF7000270,MF7000867,MF7000868,MF7000869,MF7000870 [UniProt ID chain A]=P55789 [UniProt boundaries chain A]=82-205 [UniProt coverage chain A]=60% [Name chain A]=FAD-linked sulfhydryl oxidase ALR [UniProt sequence chain A]=MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=P55789 [UniProt boundaries chain A-2]=82-205 [UniProt coverage chain A-2]=60% [Name chain A-2]=FAD-linked sulfhydryl oxidase ALR [UniProt sequence chain A-2]=MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Homo sapiens [Accession]=MF7000870 [Entry] [Entry number]=1055 [Entry name]=Rv3272, mutant D175A (Mycobacterium tuberculosis) [PDB ID]=5yiy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=CoA-transferase family III [Evidence level]=Indirect evidence [Evidence text]=The structure of CaiB reveals a spectacular fold where two monomers are interlaced to form an interlocked dimer with large interface (PMID:15518548). The folding path of CaiB and other proteins of this fold must be quite complex because the dimer cannot be formed by the individually folded monomers, partial unfolding would have to take place to break the CaiB dimer, thus it is most probably very stable (PMID:15518548). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000131,MF7000132,MF7000133,MF7000134,MF7000135,MF7000871 [UniProt ID chain A]=P96877 [UniProt boundaries chain A]=5-394 [UniProt coverage chain A]=98% [Name chain A]=Probable fatty acyl-CoA transferase Rv3272 [UniProt sequence chain A]=MPTSNPAKPLDGFRVLDFTQNVAGPLAGQVLVDLGAEVIKVEAPGGEAARQITSVLPGRPPLATYFLPNNRGKKSVTVDLTTEQAKQQMLRLADTADVVLEAFRPGTMEKLGLGPDDLRSRNPNLIYARLTAYGGNGPHGSRPGIDLVVAAEAGMTTGMPTPEGKPQIIPFQLVDNASGHVLAQAVLAALLHRERNGVADVVQVAMYDVAVGLQANQLMMHLNRAASDQPKPEPAPKAKRRKGVGFATQPSDAFRTADGYIVISAYVPKHWQKLCYLIGRPDLVEDQRFAEQRSRSINYAELTAELELALASKTATEWVQLLQANGLMACLAHTWKQVVDTPLFAENDLTLEVGRGADTITVIRTPARYASFRAVVTDPPPTAGEHNAVFLARP [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P96877 [UniProt boundaries chain B]=5-393 [UniProt coverage chain B]=98% [Name chain B]=Probable fatty acyl-CoA transferase Rv3272 [UniProt sequence chain B]=MPTSNPAKPLDGFRVLDFTQNVAGPLAGQVLVDLGAEVIKVEAPGGEAARQITSVLPGRPPLATYFLPNNRGKKSVTVDLTTEQAKQQMLRLADTADVVLEAFRPGTMEKLGLGPDDLRSRNPNLIYARLTAYGGNGPHGSRPGIDLVVAAEAGMTTGMPTPEGKPQIIPFQLVDNASGHVLAQAVLAALLHRERNGVADVVQVAMYDVAVGLQANQLMMHLNRAASDQPKPEPAPKAKRRKGVGFATQPSDAFRTADGYIVISAYVPKHWQKLCYLIGRPDLVEDQRFAEQRSRSINYAELTAELELALASKTATEWVQLLQANGLMACLAHTWKQVVDTPLFAENDLTLEVGRGADTITVIRTPARYASFRAVVTDPPPTAGEHNAVFLARP [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000871 [Entry] [Entry number]=1056 [Entry name]=TRIM E3 ubiquitin ligase WT [PDB ID]=7xyy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=SPRY domain and RING-type zinc-finger [Sequence domain]=SPRY domain and RING-type zinc-finger [Evidence level]=Direct evidence [Evidence text]=Multidomain antiparallel dimer, where the dimerization subdomain is a long coiled-coil (PMID:37770719). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000872,MF7000873,MF7000874,MF7000875 [UniProt ID chain A]=Q1XH17 [UniProt boundaries chain A]=85-470 [UniProt coverage chain A]=80% [Name chain A]=Tripartite motif-containing protein 72 [UniProt sequence chain A]=MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q1XH17 [UniProt boundaries chain B]=85-470 [UniProt coverage chain B]=80% [Name chain B]=Tripartite motif-containing protein 72 [UniProt sequence chain B]=MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=7.10 [Source organism]=Mus musculus [Accession]=MF7000872 [Entry] [Entry number]=1057 [Entry name]=TRIM E3 ubiquitin ligase [PDB ID]=7xz0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=SPRY domain and RING-type zinc-finger [Sequence domain]=SPRY domain and RING-type zinc-finger [Evidence level]=Direct evidence [Evidence text]=Multidomain antiparallel dimer, where the dimerization subdomain is a long coiled-coil (PMID:37770719). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000872,MF7000873,MF7000874,MF7000875 [UniProt ID chain A]=Q1XH17 [UniProt boundaries chain A]=85-470 [UniProt coverage chain A]=80% [Name chain A]=Tripartite motif-containing protein 72 [UniProt sequence chain A]=MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q1XH17 [UniProt boundaries chain B]=85-470 [UniProt coverage chain B]=80% [Name chain B]=Tripartite motif-containing protein 72 [UniProt sequence chain B]=MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=3.28 [Source organism]=Mus musculus [Accession]=MF7000873 [Entry] [Entry number]=1058 [Entry name]=TRIM E3 ubiquitin ligase [PDB ID]=7xv2 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=SPRY domain and RING-type zinc-finger [Sequence domain]=SPRY domain and RING-type zinc-finger [Evidence level]=Direct evidence [Evidence text]=Multidomain antiparallel dimer, where the dimerization subdomain is a long coiled-coil (PMID:37770719). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000872,MF7000873,MF7000874,MF7000875 [UniProt ID chain A]=Q1XH17 [UniProt boundaries chain A]=85-470 [UniProt coverage chain A]=80% [Name chain A]=Tripartite motif-containing protein 72 [UniProt sequence chain A]=MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=Q1XH17 [UniProt boundaries chain A-2]=85-470 [UniProt coverage chain A-2]=80% [Name chain A-2]=Tripartite motif-containing protein 72 [UniProt sequence chain A-2]=MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=2.75 [Source organism]=Mus musculus [Accession]=MF7000874 [Entry] [Entry number]=1059 [Entry name]=TRIM E3 ubiquitin ligase [PDB ID]=7xz1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=SPRY domain and RING-type zinc-finger [Sequence domain]=SPRY domain and RING-type zinc-finger [Evidence level]=Direct evidence [Evidence text]=Multidomain antiparallel dimer, where the dimerization subdomain is a long coiled-coil (PMID:37770719). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000872,MF7000873,MF7000874,MF7000875 [UniProt ID chain A]=Q1XH17 [UniProt boundaries chain A]=85-470 [UniProt coverage chain A]=80% [Name chain A]=Tripartite motif-containing protein 72 [UniProt sequence chain A]=MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q1XH17 [UniProt boundaries chain B]=85-470 [UniProt coverage chain B]=80% [Name chain B]=Tripartite motif-containing protein 72 [UniProt sequence chain B]=MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=5.20 [Source organism]=Mus musculus [Accession]=MF7000875 [Entry] [Entry number]=1060 [Entry name]=BTB domain of PLZF [PDB ID]=1buo [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=BTB/POZ domain [Evidence level]=Indirect evidence [Evidence text]=The dimer is highly stable, it is the only form observed in solution by different methods, and it shows a single coupled two-state transition during unfolding (PMID:9341182). Nac1 most likely functions as an obligate homodimer (PMID:19407373). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000876,MF7000877,MF7000878,MF7000879,MF7000880 [UniProt ID chain A]=Q05516 [UniProt boundaries chain A]=6-126 [UniProt coverage chain A]=17% [Name chain A]=Zinc finger and BTB domain-containing protein 16 [UniProt sequence chain A]=MDLTKMGMIQLQNPSHPTGLLCKANQMRLAGTLCDVVIMVDSQEFHAHRTVLACTSKMFEILFHRNSQHYTLDFLSPKTFQQILEYAYTATLQAKAEDLDDLLYAAEILEIEYLEEQCLKMLETIQASDDNDTEATMADGGAEEEEDRKARYLKNIFISKHSSEESGYASVAGQSLPGPMVDQSPSVSTSFGLSAMSPTKAAVDSLMTIGQSLLQGTLQPPAGPEEPTLAGGGRHPGVAEVKTEMMQVDEVPSQDSPGAAESSISGGMGDKVEERGKEGPGTPTRSSVITSARELHYGREESAEQVPPPAEAGQAPTGRPEHPAPPPEKHLGIYSVLPNHKADAVLSMPSSVTSGLHVQPALAVSMDFSTYGGLLPQGFIQRELFSKLGELAVGMKSESRTIGEQCSVCGVELPDNEAVEQHRKLHSGMKTYGCELCGKRFLDSLRLRMHLLAHSAGAKAFVCDQCGAQFSKEDALETHRQTHTGTDMAVFCLLCGKRFQAQSALQQHMEVHAGVRSYICSECNRTFPSHTALKRHLRSHTGDHPYECEFCGSCFRDESTLKSHKRIHTGEKPYECNGCGKKFSLKHQLETHYRVHTGEKPFECKLCHQRSRDYSAMIKHLRTHNGASPYQCTICTEYCPSLSSMQKHMKGHKPEEIPPDWRIEKTYLYLCYV [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q05516 [UniProt boundaries chain A-2]=6-126 [UniProt coverage chain A-2]=17% [Name chain A-2]=Zinc finger and BTB domain-containing protein 16 [UniProt sequence chain A-2]=MDLTKMGMIQLQNPSHPTGLLCKANQMRLAGTLCDVVIMVDSQEFHAHRTVLACTSKMFEILFHRNSQHYTLDFLSPKTFQQILEYAYTATLQAKAEDLDDLLYAAEILEIEYLEEQCLKMLETIQASDDNDTEATMADGGAEEEEDRKARYLKNIFISKHSSEESGYASVAGQSLPGPMVDQSPSVSTSFGLSAMSPTKAAVDSLMTIGQSLLQGTLQPPAGPEEPTLAGGGRHPGVAEVKTEMMQVDEVPSQDSPGAAESSISGGMGDKVEERGKEGPGTPTRSSVITSARELHYGREESAEQVPPPAEAGQAPTGRPEHPAPPPEKHLGIYSVLPNHKADAVLSMPSSVTSGLHVQPALAVSMDFSTYGGLLPQGFIQRELFSKLGELAVGMKSESRTIGEQCSVCGVELPDNEAVEQHRKLHSGMKTYGCELCGKRFLDSLRLRMHLLAHSAGAKAFVCDQCGAQFSKEDALETHRQTHTGTDMAVFCLLCGKRFQAQSALQQHMEVHAGVRSYICSECNRTFPSHTALKRHLRSHTGDHPYECEFCGSCFRDESTLKSHKRIHTGEKPYECNGCGKKFSLKHQLETHYRVHTGEKPFECKLCHQRSRDYSAMIKHLRTHNGASPYQCTICTEYCPSLSSMQKHMKGHKPEEIPPDWRIEKTYLYLCYV [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Homo sapiens [Accession]=MF7000876 [Entry] [Entry number]=1061 [Entry name]=Human Nac1 POZ Domain [PDB ID]=3ga1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=BTB/POZ domain [Evidence level]=Indirect evidence [Evidence text]=The dimer is highly stable, it is the only form observed in solution by different methods, and it shows a single coupled two-state transition during unfolding (PMID:9341182). Nac1 most likely functions as an obligate homodimer (PMID:19407373). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000876,MF7000877,MF7000878,MF7000879,MF7000880 [UniProt ID chain A]=Q96RE7 [UniProt boundaries chain A]=3-115 [UniProt coverage chain A]=21% [Name chain A]=Nucleus accumbens-associated protein 1 [UniProt sequence chain A]=MAQTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNNSRSAVVELPAAVQPQSFQQILSFCYTGRLSMNVGDQFLLMYTAGFLQIQEIMEKGTEFFLKVSSPSCDSQGLHAEEAPSSEPQSPVAQTSGWPACSTPLPLVSRVKTEQQESDSVQCMPVAKRLWDSGQKEAGGGGNGSRKMAKFSTPDLAANRPHQPPPPQQAPVVAAAQPAVAAGAGQPAGGVAAAGGVVSGPSTSERTSPGTSSAYTSDSPGSYHNEEDEEEDGGEEGMDEQYRQICNMYTMYSMMNVGQTAEKVEALPEQVAPESRNRIRVRQDLASLPAELINQIGNRCHPKLYDEGDPSEKLELVTGTNVYITRAQLMNCHVSAGTRHKVLLRRLLASFFDRNTLANSCGTGIRSSTNDPRRKPLDSRVLHAVKYYCQNFAPNFKESEMNAIAADMCTNARRVVRKSWMPKVKVLKAEDDAYTTFISETGKIEPDMMGVEHGFETASHEGEAGPSAEALQ [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q96RE7 [UniProt boundaries chain B]=2-123 [UniProt coverage chain B]=23% [Name chain B]=Nucleus accumbens-associated protein 1 [UniProt sequence chain B]=MAQTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNNSRSAVVELPAAVQPQSFQQILSFCYTGRLSMNVGDQFLLMYTAGFLQIQEIMEKGTEFFLKVSSPSCDSQGLHAEEAPSSEPQSPVAQTSGWPACSTPLPLVSRVKTEQQESDSVQCMPVAKRLWDSGQKEAGGGGNGSRKMAKFSTPDLAANRPHQPPPPQQAPVVAAAQPAVAAGAGQPAGGVAAAGGVVSGPSTSERTSPGTSSAYTSDSPGSYHNEEDEEEDGGEEGMDEQYRQICNMYTMYSMMNVGQTAEKVEALPEQVAPESRNRIRVRQDLASLPAELINQIGNRCHPKLYDEGDPSEKLELVTGTNVYITRAQLMNCHVSAGTRHKVLLRRLLASFFDRNTLANSCGTGIRSSTNDPRRKPLDSRVLHAVKYYCQNFAPNFKESEMNAIAADMCTNARRVVRKSWMPKVKVLKAEDDAYTTFISETGKIEPDMMGVEHGFETASHEGEAGPSAEALQ [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Homo sapiens [Accession]=MF7000877 [Entry] [Entry number]=1062 [Entry name]=BTB domain (Drosophila CP190) [PDB ID]=4u77 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=BTB/POZ domain [Evidence level]=Indirect evidence [Evidence text]=The dimer is highly stable, it is the only form observed in solution by different methods, and it shows a single coupled two-state transition during unfolding (PMID:9341182). Nac1 most likely functions as an obligate homodimer (PMID:19407373). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000876,MF7000877,MF7000878,MF7000879,MF7000880 [UniProt ID chain A]=Q24478 [UniProt boundaries chain A]=2-122 [UniProt coverage chain A]=11% [Name chain A]=Centrosome-associated zinc finger protein Cp190 [UniProt sequence chain A]=MGEVKSVKVDNWGVFFLQKLQNFFNKTDYCDLTLQFRDNSQLKVHRLVLSACTDYFNVLEQTCEIVDDALIMPNEFQADVVVPIVNFMYTGTLEFELKMYGKLLRTAKEMNMTVLLKLLEAHRRTMENVNRQQRPPSPKGIRRRTVGQPSSGLPQQRVLGPSPQSRNVATPIAQRANTQRGSTGNTMSRTSGGSNRSPYGDSSNVKQEPTSPFEQLRKGYNNNKRPAQTSLLSPPSKKPSLEEVKEFAEQQRMRKQIAAEYGDNDPEYDGGMLYDDVHAGDDDDDDMPPQPSTSKQQSPQGTQTQLEHGSTTIILKQDSPSQTPTIIVKDSSNAKLNHTKIIAEVLRQYPHIVKGHKNIKLKIMPNTPAAPTEKSAPATVKPPANQSSATTSPHKKLHVSFKADKSTPLITAQQKAASSQQKSGTSQTTGNQGTGANPPANTAAAQKRRIDSKTMHALIAQGAENTTGPWLCLRCGVNGRPISIPSYRGFRRHLINTHKETIDPALCEHCGWRSVNNRELHFHMYMEHQTKSLLYTFAECALCNQSYRTKGELEAHINEVHTDDNKQQCIYCNKVFEQELQLYRHMKSYHKEQALEDGIIDETDEEFLGSQDEEEEAEGDEEQEPEQTGKVRILSDISLPATSAITVQQAQQEQLQEEDVEQVQQEVKFVGADGNEVELTDEQRKEILSQLNQQQAGATAGGVVMVLSEPEAEHVKQETDEKSLAGTEEEYDDSQIYSELGAADSVESAKKNIADESKESIDNLEWAENLIAESEEQSNKEPKSDKPRDDISEKLKELTGDWTEDENDDDVDDKPATAELASELANKDPEPTVHEEEDDIDLALQSLHKGPEEATEEKASEESVTSADDAVDAVPNINSQPEKMDVDSEAADEKASKAEVQIKKEAELENDQEEFIKEDSPIPHSDSVAELREAVTASEGEDDVHLEADNIRKELLDELIAEAEKPDQEKDIVQSEENATTEALDRSVTDEDDLVPPTQVSTEQMEIDEPAAEKAAENNEDTRTADEKEAVEDKPNQTQDVTTAEKPTLESAKAGDEATSGEAASVDKVKSLISEWGDDDEDEDENGVSAAAKEEL [Source organism chain A]=Drosophila melanogaster [UniProt ID chain A-2]=Q24478 [UniProt boundaries chain A-2]=2-122 [UniProt coverage chain A-2]=11% [Name chain A-2]=Centrosome-associated zinc finger protein Cp190 [UniProt sequence chain A-2]=MGEVKSVKVDNWGVFFLQKLQNFFNKTDYCDLTLQFRDNSQLKVHRLVLSACTDYFNVLEQTCEIVDDALIMPNEFQADVVVPIVNFMYTGTLEFELKMYGKLLRTAKEMNMTVLLKLLEAHRRTMENVNRQQRPPSPKGIRRRTVGQPSSGLPQQRVLGPSPQSRNVATPIAQRANTQRGSTGNTMSRTSGGSNRSPYGDSSNVKQEPTSPFEQLRKGYNNNKRPAQTSLLSPPSKKPSLEEVKEFAEQQRMRKQIAAEYGDNDPEYDGGMLYDDVHAGDDDDDDMPPQPSTSKQQSPQGTQTQLEHGSTTIILKQDSPSQTPTIIVKDSSNAKLNHTKIIAEVLRQYPHIVKGHKNIKLKIMPNTPAAPTEKSAPATVKPPANQSSATTSPHKKLHVSFKADKSTPLITAQQKAASSQQKSGTSQTTGNQGTGANPPANTAAAQKRRIDSKTMHALIAQGAENTTGPWLCLRCGVNGRPISIPSYRGFRRHLINTHKETIDPALCEHCGWRSVNNRELHFHMYMEHQTKSLLYTFAECALCNQSYRTKGELEAHINEVHTDDNKQQCIYCNKVFEQELQLYRHMKSYHKEQALEDGIIDETDEEFLGSQDEEEEAEGDEEQEPEQTGKVRILSDISLPATSAITVQQAQQEQLQEEDVEQVQQEVKFVGADGNEVELTDEQRKEILSQLNQQQAGATAGGVVMVLSEPEAEHVKQETDEKSLAGTEEEYDDSQIYSELGAADSVESAKKNIADESKESIDNLEWAENLIAESEEQSNKEPKSDKPRDDISEKLKELTGDWTEDENDDDVDDKPATAELASELANKDPEPTVHEEEDDIDLALQSLHKGPEEATEEKASEESVTSADDAVDAVPNINSQPEKMDVDSEAADEKASKAEVQIKKEAELENDQEEFIKEDSPIPHSDSVAELREAVTASEGEDDVHLEADNIRKELLDELIAEAEKPDQEKDIVQSEENATTEALDRSVTDEDDLVPPTQVSTEQMEIDEPAAEKAAENNEDTRTADEKEAVEDKPNQTQDVTTAEKPTLESAKAGDEATSGEAASVDKVKSLISEWGDDDEDEDENGVSAAAKEEL [Source organism chain A-2]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=2.03 [Source organism]=Drosophila melanogaster [Accession]=MF7000878 [Entry] [Entry number]=1063 [Entry name]=BTB domain (Drosophila melanogaster CP190) [PDB ID]=5eup [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=BTB/POZ domain [Evidence level]=Indirect evidence [Evidence text]=The dimer is highly stable, it is the only form observed in solution by different methods, and it shows a single coupled two-state transition during unfolding (PMID:9341182). Nac1 most likely functions as an obligate homodimer (PMID:19407373). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000876,MF7000877,MF7000878,MF7000879,MF7000880 [UniProt ID chain A]=Q24478 [UniProt boundaries chain A]=2-121 [UniProt coverage chain A]=10% [Name chain A]=Centrosome-associated zinc finger protein Cp190 [UniProt sequence chain A]=MGEVKSVKVDNWGVFFLQKLQNFFNKTDYCDLTLQFRDNSQLKVHRLVLSACTDYFNVLEQTCEIVDDALIMPNEFQADVVVPIVNFMYTGTLEFELKMYGKLLRTAKEMNMTVLLKLLEAHRRTMENVNRQQRPPSPKGIRRRTVGQPSSGLPQQRVLGPSPQSRNVATPIAQRANTQRGSTGNTMSRTSGGSNRSPYGDSSNVKQEPTSPFEQLRKGYNNNKRPAQTSLLSPPSKKPSLEEVKEFAEQQRMRKQIAAEYGDNDPEYDGGMLYDDVHAGDDDDDDMPPQPSTSKQQSPQGTQTQLEHGSTTIILKQDSPSQTPTIIVKDSSNAKLNHTKIIAEVLRQYPHIVKGHKNIKLKIMPNTPAAPTEKSAPATVKPPANQSSATTSPHKKLHVSFKADKSTPLITAQQKAASSQQKSGTSQTTGNQGTGANPPANTAAAQKRRIDSKTMHALIAQGAENTTGPWLCLRCGVNGRPISIPSYRGFRRHLINTHKETIDPALCEHCGWRSVNNRELHFHMYMEHQTKSLLYTFAECALCNQSYRTKGELEAHINEVHTDDNKQQCIYCNKVFEQELQLYRHMKSYHKEQALEDGIIDETDEEFLGSQDEEEEAEGDEEQEPEQTGKVRILSDISLPATSAITVQQAQQEQLQEEDVEQVQQEVKFVGADGNEVELTDEQRKEILSQLNQQQAGATAGGVVMVLSEPEAEHVKQETDEKSLAGTEEEYDDSQIYSELGAADSVESAKKNIADESKESIDNLEWAENLIAESEEQSNKEPKSDKPRDDISEKLKELTGDWTEDENDDDVDDKPATAELASELANKDPEPTVHEEEDDIDLALQSLHKGPEEATEEKASEESVTSADDAVDAVPNINSQPEKMDVDSEAADEKASKAEVQIKKEAELENDQEEFIKEDSPIPHSDSVAELREAVTASEGEDDVHLEADNIRKELLDELIAEAEKPDQEKDIVQSEENATTEALDRSVTDEDDLVPPTQVSTEQMEIDEPAAEKAAENNEDTRTADEKEAVEDKPNQTQDVTTAEKPTLESAKAGDEATSGEAASVDKVKSLISEWGDDDEDEDENGVSAAAKEEL [Source organism chain A]=Drosophila melanogaster [UniProt ID chain A-2]=Q24478 [UniProt boundaries chain A-2]=2-121 [UniProt coverage chain A-2]=10% [Name chain A-2]=Centrosome-associated zinc finger protein Cp190 [UniProt sequence chain A-2]=MGEVKSVKVDNWGVFFLQKLQNFFNKTDYCDLTLQFRDNSQLKVHRLVLSACTDYFNVLEQTCEIVDDALIMPNEFQADVVVPIVNFMYTGTLEFELKMYGKLLRTAKEMNMTVLLKLLEAHRRTMENVNRQQRPPSPKGIRRRTVGQPSSGLPQQRVLGPSPQSRNVATPIAQRANTQRGSTGNTMSRTSGGSNRSPYGDSSNVKQEPTSPFEQLRKGYNNNKRPAQTSLLSPPSKKPSLEEVKEFAEQQRMRKQIAAEYGDNDPEYDGGMLYDDVHAGDDDDDDMPPQPSTSKQQSPQGTQTQLEHGSTTIILKQDSPSQTPTIIVKDSSNAKLNHTKIIAEVLRQYPHIVKGHKNIKLKIMPNTPAAPTEKSAPATVKPPANQSSATTSPHKKLHVSFKADKSTPLITAQQKAASSQQKSGTSQTTGNQGTGANPPANTAAAQKRRIDSKTMHALIAQGAENTTGPWLCLRCGVNGRPISIPSYRGFRRHLINTHKETIDPALCEHCGWRSVNNRELHFHMYMEHQTKSLLYTFAECALCNQSYRTKGELEAHINEVHTDDNKQQCIYCNKVFEQELQLYRHMKSYHKEQALEDGIIDETDEEFLGSQDEEEEAEGDEEQEPEQTGKVRILSDISLPATSAITVQQAQQEQLQEEDVEQVQQEVKFVGADGNEVELTDEQRKEILSQLNQQQAGATAGGVVMVLSEPEAEHVKQETDEKSLAGTEEEYDDSQIYSELGAADSVESAKKNIADESKESIDNLEWAENLIAESEEQSNKEPKSDKPRDDISEKLKELTGDWTEDENDDDVDDKPATAELASELANKDPEPTVHEEEDDIDLALQSLHKGPEEATEEKASEESVTSADDAVDAVPNINSQPEKMDVDSEAADEKASKAEVQIKKEAELENDQEEFIKEDSPIPHSDSVAELREAVTASEGEDDVHLEADNIRKELLDELIAEAEKPDQEKDIVQSEENATTEALDRSVTDEDDLVPPTQVSTEQMEIDEPAAEKAAENNEDTRTADEKEAVEDKPNQTQDVTTAEKPTLESAKAGDEATSGEAASVDKVKSLISEWGDDDEDEDENGVSAAAKEEL [Source organism chain A-2]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Drosophila melanogaster [Accession]=MF7000879 [Entry] [Entry number]=1064 [Entry name]=BTB domain of human NS1-BP [PDB ID]=6n34 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=BTB/POZ domain [Evidence level]=Indirect evidence [Evidence text]=The dimer is highly stable, it is the only form observed in solution by different methods, and it shows a single coupled two-state transition during unfolding (PMID:9341182). Nac1 most likely functions as an obligate homodimer (PMID:19407373). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000876,MF7000877,MF7000878,MF7000879,MF7000880 [UniProt ID chain A]=Q9Y6Y0 [UniProt boundaries chain A]=6-129 [UniProt coverage chain A]=19% [Name chain A]=Influenza virus NS1A-binding protein [UniProt sequence chain A]=MIPNGYLMFEDENFIESSVAKLNALRKSGQFCDVRLQVCGHEMLAHRAVLACCSPYLFEIFNSDSDPHGISHVKFDDLNPEAVEVLLNYAYTAQLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDSLEELMEEVQTLYYSADHKLLDGNLLDGQAEVFGSDDDHIQFVQKKPPRENGHKQISSSSTGCLSSPNATVQSPKHEWKIVASEKTSNNTYLCLAVLDGIFCVIFLHGRNSPQSSPTSTPKLSKSLSFEMQQDELIEKPMSPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPMRTPRARFQMAVLMGQLYVVGGSNGHSDDLSCGEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVGGSDPYGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVCELGGYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSPYTKIFQF [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9Y6Y0 [UniProt boundaries chain B]=4-128 [UniProt coverage chain B]=19% [Name chain B]=Influenza virus NS1A-binding protein [UniProt sequence chain B]=MIPNGYLMFEDENFIESSVAKLNALRKSGQFCDVRLQVCGHEMLAHRAVLACCSPYLFEIFNSDSDPHGISHVKFDDLNPEAVEVLLNYAYTAQLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDSLEELMEEVQTLYYSADHKLLDGNLLDGQAEVFGSDDDHIQFVQKKPPRENGHKQISSSSTGCLSSPNATVQSPKHEWKIVASEKTSNNTYLCLAVLDGIFCVIFLHGRNSPQSSPTSTPKLSKSLSFEMQQDELIEKPMSPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPMRTPRARFQMAVLMGQLYVVGGSNGHSDDLSCGEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVGGSDPYGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVCELGGYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSPYTKIFQF [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=Homo sapiens [Accession]=MF7000880 [Entry] [Entry number]=1065 [Entry name]=Rv1264N, the regulatory domain of the mycobacterial adenylyl cylcase Rv1264, at pH 5.3 [PDB ID]=2ev3 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Adenylate cyclase regulatory domain [Evidence level]=Indirect evidence [Evidence text]=The N-terminal helical dimerization domain of the pH-sensitive adenylate cyclase Rv1264 (Rv1264N), similary to the full-length Rv1264 protein, is dimeric in solution based on gel-filtration experiments. The hydrophobic core of the helical bundle is made up by both monomers. Therefore, the dimer is unlikely to dissociate, it is very stable, which is also essential for its enzymatic function (PMID:17482646). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000881,MF7000882,MF7000883,MF7000884 [UniProt ID chain A]=P9WMU9 [UniProt boundaries chain A]=12-195 [UniProt coverage chain A]=46% [Name chain A]=pH-sensitive adenylate cyclase Rv1264 [UniProt sequence chain A]=MTDHVREADDANIDDLLGDLGGTARAERAKLVEWLLEQGITPDEIRATNPPLLLATRHLVGDDGTYVSAREISENYGVDLELLQRVQRAVGLARVDDPDAVVHMRADGEAAARAQRFVELGLNPDQVVLVVRVLAEGLSHAAEAMRYTALEAIMRPGATELDIAKGSQALVSQIVPLLGPMIQDMLFMQLRHMMETEAVNAGERAAGKPLPGARQVTVAFADLVGFTQLGEVVSAEELGHLAGRLAGLARDLTAPPVWFIKTIGDAVMLVCPDPAPLLDTVLKLVEVVDTDNNFPRLRAGVASGMAVSRAGDWFGSPVNVASRVTGVARPGAVLVADSVREALGDAPEADGFQWSFAGPRRLRGIRGDVRLFRVRRGATRTGSGGAAQDDDLAGSSP [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WMU9 [UniProt boundaries chain B]=11-195 [UniProt coverage chain B]=46% [Name chain B]=pH-sensitive adenylate cyclase Rv1264 [UniProt sequence chain B]=MTDHVREADDANIDDLLGDLGGTARAERAKLVEWLLEQGITPDEIRATNPPLLLATRHLVGDDGTYVSAREISENYGVDLELLQRVQRAVGLARVDDPDAVVHMRADGEAAARAQRFVELGLNPDQVVLVVRVLAEGLSHAAEAMRYTALEAIMRPGATELDIAKGSQALVSQIVPLLGPMIQDMLFMQLRHMMETEAVNAGERAAGKPLPGARQVTVAFADLVGFTQLGEVVSAEELGHLAGRLAGLARDLTAPPVWFIKTIGDAVMLVCPDPAPLLDTVLKLVEVVDTDNNFPRLRAGVASGMAVSRAGDWFGSPVNVASRVTGVARPGAVLVADSVREALGDAPEADGFQWSFAGPRRLRGIRGDVRLFRVRRGATRTGSGGAAQDDDLAGSSP [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.68 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000881 [Entry] [Entry number]=1066 [Entry name]=Rv1264N, the regulatory domain of the mycobacterial adenylyl cylcase Rv1264, at pH 6.0 [PDB ID]=2ev1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Adenylate cyclase regulatory domain [Evidence level]=Indirect evidence [Evidence text]=The N-terminal helical dimerization domain of the pH-sensitive adenylate cyclase Rv1264 (Rv1264N), similary to the full-length Rv1264 protein, is dimeric in solution based on gel-filtration experiments. The hydrophobic core of the helical bundle is made up by both monomers. Therefore, the dimer is unlikely to dissociate, it is very stable, which is also essential for its enzymatic function (PMID:17482646). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000881,MF7000882,MF7000883,MF7000884 [UniProt ID chain A]=P9WMU9 [UniProt boundaries chain A]=11-195 [UniProt coverage chain A]=46% [Name chain A]=pH-sensitive adenylate cyclase Rv1264 [UniProt sequence chain A]=MTDHVREADDANIDDLLGDLGGTARAERAKLVEWLLEQGITPDEIRATNPPLLLATRHLVGDDGTYVSAREISENYGVDLELLQRVQRAVGLARVDDPDAVVHMRADGEAAARAQRFVELGLNPDQVVLVVRVLAEGLSHAAEAMRYTALEAIMRPGATELDIAKGSQALVSQIVPLLGPMIQDMLFMQLRHMMETEAVNAGERAAGKPLPGARQVTVAFADLVGFTQLGEVVSAEELGHLAGRLAGLARDLTAPPVWFIKTIGDAVMLVCPDPAPLLDTVLKLVEVVDTDNNFPRLRAGVASGMAVSRAGDWFGSPVNVASRVTGVARPGAVLVADSVREALGDAPEADGFQWSFAGPRRLRGIRGDVRLFRVRRGATRTGSGGAAQDDDLAGSSP [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WMU9 [UniProt boundaries chain B]=13-193 [UniProt coverage chain B]=45% [Name chain B]=pH-sensitive adenylate cyclase Rv1264 [UniProt sequence chain B]=MTDHVREADDANIDDLLGDLGGTARAERAKLVEWLLEQGITPDEIRATNPPLLLATRHLVGDDGTYVSAREISENYGVDLELLQRVQRAVGLARVDDPDAVVHMRADGEAAARAQRFVELGLNPDQVVLVVRVLAEGLSHAAEAMRYTALEAIMRPGATELDIAKGSQALVSQIVPLLGPMIQDMLFMQLRHMMETEAVNAGERAAGKPLPGARQVTVAFADLVGFTQLGEVVSAEELGHLAGRLAGLARDLTAPPVWFIKTIGDAVMLVCPDPAPLLDTVLKLVEVVDTDNNFPRLRAGVASGMAVSRAGDWFGSPVNVASRVTGVARPGAVLVADSVREALGDAPEADGFQWSFAGPRRLRGIRGDVRLFRVRRGATRTGSGGAAQDDDLAGSSP [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000882 [Entry] [Entry number]=1067 [Entry name]=Rv1264N, the regulatory domain of the mycobacterial adenylyl cylcase Rv1264, at pH 8.5 [PDB ID]=2ev2 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Adenylate cyclase regulatory domain [Evidence level]=Indirect evidence [Evidence text]=The N-terminal helical dimerization domain of the pH-sensitive adenylate cyclase Rv1264 (Rv1264N), similary to the full-length Rv1264 protein, is dimeric in solution based on gel-filtration experiments. The hydrophobic core of the helical bundle is made up by both monomers. Therefore, the dimer is unlikely to dissociate, it is very stable, which is also essential for its enzymatic function (PMID:17482646). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000881,MF7000882,MF7000883,MF7000884 [UniProt ID chain A]=P9WMU9 [UniProt boundaries chain A]=11-196 [UniProt coverage chain A]=46% [Name chain A]=pH-sensitive adenylate cyclase Rv1264 [UniProt sequence chain A]=MTDHVREADDANIDDLLGDLGGTARAERAKLVEWLLEQGITPDEIRATNPPLLLATRHLVGDDGTYVSAREISENYGVDLELLQRVQRAVGLARVDDPDAVVHMRADGEAAARAQRFVELGLNPDQVVLVVRVLAEGLSHAAEAMRYTALEAIMRPGATELDIAKGSQALVSQIVPLLGPMIQDMLFMQLRHMMETEAVNAGERAAGKPLPGARQVTVAFADLVGFTQLGEVVSAEELGHLAGRLAGLARDLTAPPVWFIKTIGDAVMLVCPDPAPLLDTVLKLVEVVDTDNNFPRLRAGVASGMAVSRAGDWFGSPVNVASRVTGVARPGAVLVADSVREALGDAPEADGFQWSFAGPRRLRGIRGDVRLFRVRRGATRTGSGGAAQDDDLAGSSP [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WMU9 [UniProt boundaries chain B]=12-194 [UniProt coverage chain B]=46% [Name chain B]=pH-sensitive adenylate cyclase Rv1264 [UniProt sequence chain B]=MTDHVREADDANIDDLLGDLGGTARAERAKLVEWLLEQGITPDEIRATNPPLLLATRHLVGDDGTYVSAREISENYGVDLELLQRVQRAVGLARVDDPDAVVHMRADGEAAARAQRFVELGLNPDQVVLVVRVLAEGLSHAAEAMRYTALEAIMRPGATELDIAKGSQALVSQIVPLLGPMIQDMLFMQLRHMMETEAVNAGERAAGKPLPGARQVTVAFADLVGFTQLGEVVSAEELGHLAGRLAGLARDLTAPPVWFIKTIGDAVMLVCPDPAPLLDTVLKLVEVVDTDNNFPRLRAGVASGMAVSRAGDWFGSPVNVASRVTGVARPGAVLVADSVREALGDAPEADGFQWSFAGPRRLRGIRGDVRLFRVRRGATRTGSGGAAQDDDLAGSSP [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000883 [Entry] [Entry number]=1068 [Entry name]=Rv1264N, the regulatory domain of the mycobacterial adenylyl cylcase Rv1264, with a salt precipitant [PDB ID]=2ev4 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Adenylate cyclase regulatory domain [Evidence level]=Indirect evidence [Evidence text]=The N-terminal helical dimerization domain of the pH-sensitive adenylate cyclase Rv1264 (Rv1264N), similary to the full-length Rv1264 protein, is dimeric in solution based on gel-filtration experiments. The hydrophobic core of the helical bundle is made up by both monomers. Therefore, the dimer is unlikely to dissociate, it is very stable, which is also essential for its enzymatic function (PMID:17482646). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000881,MF7000882,MF7000883,MF7000884 [UniProt ID chain A]=P9WMU9 [UniProt boundaries chain A]=11-196 [UniProt coverage chain A]=46% [Name chain A]=pH-sensitive adenylate cyclase Rv1264 [UniProt sequence chain A]=MTDHVREADDANIDDLLGDLGGTARAERAKLVEWLLEQGITPDEIRATNPPLLLATRHLVGDDGTYVSAREISENYGVDLELLQRVQRAVGLARVDDPDAVVHMRADGEAAARAQRFVELGLNPDQVVLVVRVLAEGLSHAAEAMRYTALEAIMRPGATELDIAKGSQALVSQIVPLLGPMIQDMLFMQLRHMMETEAVNAGERAAGKPLPGARQVTVAFADLVGFTQLGEVVSAEELGHLAGRLAGLARDLTAPPVWFIKTIGDAVMLVCPDPAPLLDTVLKLVEVVDTDNNFPRLRAGVASGMAVSRAGDWFGSPVNVASRVTGVARPGAVLVADSVREALGDAPEADGFQWSFAGPRRLRGIRGDVRLFRVRRGATRTGSGGAAQDDDLAGSSP [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WMU9 [UniProt boundaries chain B]=12-194 [UniProt coverage chain B]=46% [Name chain B]=pH-sensitive adenylate cyclase Rv1264 [UniProt sequence chain B]=MTDHVREADDANIDDLLGDLGGTARAERAKLVEWLLEQGITPDEIRATNPPLLLATRHLVGDDGTYVSAREISENYGVDLELLQRVQRAVGLARVDDPDAVVHMRADGEAAARAQRFVELGLNPDQVVLVVRVLAEGLSHAAEAMRYTALEAIMRPGATELDIAKGSQALVSQIVPLLGPMIQDMLFMQLRHMMETEAVNAGERAAGKPLPGARQVTVAFADLVGFTQLGEVVSAEELGHLAGRLAGLARDLTAPPVWFIKTIGDAVMLVCPDPAPLLDTVLKLVEVVDTDNNFPRLRAGVASGMAVSRAGDWFGSPVNVASRVTGVARPGAVLVADSVREALGDAPEADGFQWSFAGPRRLRGIRGDVRLFRVRRGATRTGSGGAAQDDDLAGSSP [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.28 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000884 [Entry] [Entry number]=1069 [Entry name]=Human vascular endothelial growth factor-B [PDB ID]=2c7w [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=PDGF/VEGF-like [Sequence domain]=Cystine-knot cytokine/PDGF/VEGF-like [Evidence level]=Direct evidence [Evidence text]=Cystine-knot motif growth factors show two-state unfolding from dimers to unfolded monomers (PMID:34689403). The hydrophobic core is formed by both monomers, there is a large, hydrophobic interafce and the homodimer is covalently linked by two interchain disulfide bonds (PMID:16616187). There is a cystine-knot motif, positioned symmetrically, at the opposite end of each monomer (PMID:11069911). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000053,MF7000054,MF7000055,MF7000885,MF7000886 [UniProt ID chain A]=P49765 [UniProt boundaries chain A]=34-129 [UniProt coverage chain A]=46% [Name chain A]=Vascular endothelial growth factor B [UniProt sequence chain A]=MSPLLRRLLLAALLQLAPAQAPVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHSQCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAPSTTSALTPGPAAAAADAAASSVAKGGA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P49765 [UniProt boundaries chain B]=34-129 [UniProt coverage chain B]=46% [Name chain B]=Vascular endothelial growth factor B [UniProt sequence chain B]=MSPLLRRLLLAALLQLAPAQAPVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHSQCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAPSTTSALTPGPAAAAADAAASSVAKGGA [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.48 [Source organism]=Homo sapiens [Accession]=MF7000885 [Entry] [Entry number]=1070 [Entry name]=Vascular endothelial growth factor D [PDB ID]=2xv7 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Cystine-knot cytokines [Subclass]=PDGF/VEGF-like [Sequence domain]=Cystine-knot cytokine/PDGF/VEGF-like [Evidence level]=Direct evidence [Evidence text]=Cystine-knot motif growth factors show two-state unfolding from dimers to unfolded monomers (PMID:34689403). The hydrophobic core is formed by both monomers, there is a large, hydrophobic interafce and the homodimer is covalently linked by two interchain disulfide bonds (PMID:16616187). There is a cystine-knot motif, positioned symmetrically, at the opposite end of each monomer (PMID:11069911). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000053,MF7000054,MF7000055,MF7000885,MF7000886 [UniProt ID chain A]=O43915 [UniProt boundaries chain A]=92-194 [UniProt coverage chain A]=29% [Name chain A]=Vascular endothelial growth factor D [UniProt sequence chain A]=MYREWVVVNVFMMLYVQLVQGSSNEHGPVKRSSQSTLERSEQQIRAASSLEELLRITHSEDWKLWRCRLRLKSFTSMDSRSASHRSTRFAATFYDIETLKVIDEEWQRTQCSPRETCVEVASELGKSTNTFFKPPCVNVFRCGGCCNEESLICMNTSTSYISKQLFEISVPLTSVPELVPVKVANHTGCKCLPTAPRHPYSIIRRSIQIPEEDRCSHSKKLCPIDMLWDSNKCKCVLQEENPLAGTEDHSHLQEPALCGPHMMFDEDRCECVCKTPCPKDLIQHPKNCSCFECKESLETCCQKHKLFHPDTCSCEDRCPFHTRPCASGKTACAKHCRFPKEKRAAQGPHSRKNP [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=O43915 [UniProt boundaries chain A-2]=92-194 [UniProt coverage chain A-2]=29% [Name chain A-2]=Vascular endothelial growth factor D [UniProt sequence chain A-2]=MYREWVVVNVFMMLYVQLVQGSSNEHGPVKRSSQSTLERSEQQIRAASSLEELLRITHSEDWKLWRCRLRLKSFTSMDSRSASHRSTRFAATFYDIETLKVIDEEWQRTQCSPRETCVEVASELGKSTNTFFKPPCVNVFRCGGCCNEESLICMNTSTSYISKQLFEISVPLTSVPELVPVKVANHTGCKCLPTAPRHPYSIIRRSIQIPEEDRCSHSKKLCPIDMLWDSNKCKCVLQEENPLAGTEDHSHLQEPALCGPHMMFDEDRCECVCKTPCPKDLIQHPKNCSCFECKESLETCCQKHKLFHPDTCSCEDRCPFHTRPCASGKTACAKHCRFPKEKRAAQGPHSRKNP [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.90 [Source organism]=Homo sapiens [Accession]=MF7000886 [Entry] [Entry number]=1071 [Entry name]=RNA-binding domain of non-structural protein 1 (Influenza A virus) [PDB ID]=1ns1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Non-structural proteins [Sequence domain]=Influenza non-structural protein (NS1) [Evidence level]=No contradicting information [Evidence text]=NS1(1-73) forms a symmetric dimer corresponding to a novel six-helical motif in solution that has an extensive hydrophobic interface due to helix packing interactions (PMID:9360601). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000887,MF7000888,MF7000889,MF7000890,MF7000891 [UniProt ID chain A]=P03495 [UniProt boundaries chain A]=1-73 [UniProt coverage chain A]=30% [Name chain A]=Non-structural protein 1 [UniProt sequence chain A]=MDSNTVSSFQVDCFLWHVRKQVVDQELGDAPFLDRLRRDQKSLRGRGSTLGLNIEAATHVGKQIVEKILKEESDEALKMTMASTPASRYITDMTIEELSRDWFMLMPKQKVEGPLCIRIDQAIMDKNIMLKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSFPGHTIEDVKNAIGVLIGGLEWNDNTVRVSKTLQRFAWGSSNENGRPPLTPKQKRKMARTARSKVRRDKMAD [Source organism chain A]=Influenza A virus [UniProt ID chain B]=P03495 [UniProt boundaries chain B]=1-73 [UniProt coverage chain B]=30% [Name chain B]=Non-structural protein 1 [UniProt sequence chain B]=MDSNTVSSFQVDCFLWHVRKQVVDQELGDAPFLDRLRRDQKSLRGRGSTLGLNIEAATHVGKQIVEKILKEESDEALKMTMASTPASRYITDMTIEELSRDWFMLMPKQKVEGPLCIRIDQAIMDKNIMLKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSFPGHTIEDVKNAIGVLIGGLEWNDNTVRVSKTLQRFAWGSSNENGRPPLTPKQKRKMARTARSKVRRDKMAD [Source organism chain B]=Influenza A virus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Influenza A virus [Accession]=MF7000887 [Entry] [Entry number]=1072 [Entry name]=N-terminal fragment of NS1 protein (Influenza A virus) [PDB ID]=1ail [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Non-structural proteins [Sequence domain]=Influenza non-structural protein (NS1) [Evidence level]=No contradicting information [Evidence text]=NS1(1-73) forms a symmetric dimer corresponding to a novel six-helical motif in solution that has an extensive hydrophobic interface due to helix packing interactions (PMID:9360601). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000887,MF7000888,MF7000889,MF7000890,MF7000891 [UniProt ID chain A]=P03495 [UniProt boundaries chain A]=1-70 [UniProt coverage chain A]=29% [Name chain A]=Non-structural protein 1 [UniProt sequence chain A]=MDSNTVSSFQVDCFLWHVRKQVVDQELGDAPFLDRLRRDQKSLRGRGSTLGLNIEAATHVGKQIVEKILKEESDEALKMTMASTPASRYITDMTIEELSRDWFMLMPKQKVEGPLCIRIDQAIMDKNIMLKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSFPGHTIEDVKNAIGVLIGGLEWNDNTVRVSKTLQRFAWGSSNENGRPPLTPKQKRKMARTARSKVRRDKMAD [Source organism chain A]=Influenza A virus [UniProt ID chain A-2]=P03495 [UniProt boundaries chain A-2]=1-70 [UniProt coverage chain A-2]=29% [Name chain A-2]=Non-structural protein 1 [UniProt sequence chain A-2]=MDSNTVSSFQVDCFLWHVRKQVVDQELGDAPFLDRLRRDQKSLRGRGSTLGLNIEAATHVGKQIVEKILKEESDEALKMTMASTPASRYITDMTIEELSRDWFMLMPKQKVEGPLCIRIDQAIMDKNIMLKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSFPGHTIEDVKNAIGVLIGGLEWNDNTVRVSKTLQRFAWGSSNENGRPPLTPKQKRKMARTARSKVRRDKMAD [Source organism chain A-2]=Influenza A virus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Influenza A virus [Accession]=MF7000888 [Entry] [Entry number]=1073 [Entry name]=H17 Bat Influenza NS1 RNA-binding domain [PDB ID]=5bxz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Non-structural proteins [Sequence domain]=Influenza non-structural protein (NS1) [Evidence level]=No contradicting information [Evidence text]=NS1(1-73) forms a symmetric dimer corresponding to a novel six-helical motif in solution that has an extensive hydrophobic interface due to helix packing interactions (PMID:9360601). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000887,MF7000888,MF7000889,MF7000890,MF7000891 [UniProt ID chain A]=H6QM79 [UniProt boundaries chain A]=3-71 [UniProt coverage chain A]=31% [Name chain A]=Non-structural protein 1 [UniProt sequence chain A]=MEPNPTTIAFQVDCYLWHLKKTLSMMGEVDAPFEDRLRREQKALKGRSMTLGIDIQSATQEGYYKIKSITEESMPSYGILPNAGQNEPKYITEMTQEETIRNWVMIQPKQKVISGRILISMDQAVTNKVLTIKANFTVCFGKLERLVLARAFTEEGTVVGEINPLSFVTGHTGEDVKTAYELFRSGFEWNDNTIDESQILQRLARGVINENRRLPQDGSTE [Source organism chain A]=bat/Guatemala/153/2009 [UniProt ID chain B]=H6QM79 [UniProt boundaries chain B]=2-71 [UniProt coverage chain B]=31% [Name chain B]=Non-structural protein 1 [UniProt sequence chain B]=MEPNPTTIAFQVDCYLWHLKKTLSMMGEVDAPFEDRLRREQKALKGRSMTLGIDIQSATQEGYYKIKSITEESMPSYGILPNAGQNEPKYITEMTQEETIRNWVMIQPKQKVISGRILISMDQAVTNKVLTIKANFTVCFGKLERLVLARAFTEEGTVVGEINPLSFVTGHTGEDVKTAYELFRSGFEWNDNTIDESQILQRLARGVINENRRLPQDGSTE [Source organism chain B]=bat/Guatemala/153/2009 [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=bat/Guatemala/153/2009 [Accession]=MF7000889 [Entry] [Entry number]=1074 [Entry name]=H18 Bat Influenza NS1 RNA-binding domain [PDB ID]=5by1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Non-structural proteins [Sequence domain]=Influenza non-structural protein (NS1) [Evidence level]=No contradicting information [Evidence text]=NS1(1-73) forms a symmetric dimer corresponding to a novel six-helical motif in solution that has an extensive hydrophobic interface due to helix packing interactions (PMID:9360601). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000887,MF7000888,MF7000889,MF7000890,MF7000891 [UniProt ID chain A]=U5N1D7 [UniProt boundaries chain A]=1-71 [UniProt coverage chain A]=32% [Name chain A]=Non-structural protein 1 [UniProt sequence chain A]=MESTPTTIAFQVDCYLWHLKKMLSLMGEVDAPFEDRLRREQKALKGRSMTLGIDIQAATKAGYYKIKSITEDAMPYYGILPNAGQSEPKYITEMTVEETNRNWIMIQPKQKVIGGRILISMDQAITDKVITIKANFTVCFGKVERLVLARAFTPEGAVVGEINPLSFVTGHTGEDVKTAYELFRSGFEWNDNAIEESQILQGFLGRIADAERRLQENEPAE [Source organism chain A]=Influenza A virus [UniProt ID chain B]=U5N1D7 [UniProt boundaries chain B]=4-74 [UniProt coverage chain B]=32% [Name chain B]=Non-structural protein 1 [UniProt sequence chain B]=MESTPTTIAFQVDCYLWHLKKMLSLMGEVDAPFEDRLRREQKALKGRSMTLGIDIQAATKAGYYKIKSITEDAMPYYGILPNAGQSEPKYITEMTVEETNRNWIMIQPKQKVIGGRILISMDQAITDKVITIKANFTVCFGKVERLVLARAFTPEGAVVGEINPLSFVTGHTGEDVKTAYELFRSGFEWNDNAIEESQILQGFLGRIADAERRLQENEPAE [Source organism chain B]=Influenza A virus [ExpTech]=X-ray [Resolution]=1.75 [Source organism]=Influenza A virus [Accession]=MF7000890 [Entry] [Entry number]=1075 [Entry name]=NS1 (H17N10) RNA-binding domain [PDB ID]=5h5n [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Non-structural proteins [Sequence domain]=Influenza non-structural protein (NS1) [Evidence level]=No contradicting information [Evidence text]=NS1(1-73) forms a symmetric dimer corresponding to a novel six-helical motif in solution that has an extensive hydrophobic interface due to helix packing interactions (PMID:9360601). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000887,MF7000888,MF7000889,MF7000890,MF7000891 [UniProt ID chain A]=H6QM99 [UniProt boundaries chain A]=2-72 [UniProt coverage chain A]=32% [Name chain A]=Non-structural protein 1 [UniProt sequence chain A]=MEPNPTTIAFQVDCYLWHLKKTLSMMGEVDAPFEDRLRREQKALKGRSMTLGIDIQSATQEGYYKIKSITEESMPSYGILPNAGQNEPKYITEMTQEETTRNWVMIQPKQKIISGRILISMDQAVTNKVLTIKANFTVCFGKLERLVLARAFTEEGTVVGEINPLSFVTGHTGEDVKAAYELFRSGFEWNDNTIDESQILQRLARGVINENRRLPQDGPTE [Source organism chain A]=bat/Guatemala/060/2010 [UniProt ID chain B]=H6QM99 [UniProt boundaries chain B]=2-72 [UniProt coverage chain B]=32% [Name chain B]=Non-structural protein 1 [UniProt sequence chain B]=MEPNPTTIAFQVDCYLWHLKKTLSMMGEVDAPFEDRLRREQKALKGRSMTLGIDIQSATQEGYYKIKSITEESMPSYGILPNAGQNEPKYITEMTQEETTRNWVMIQPKQKIISGRILISMDQAVTNKVLTIKANFTVCFGKLERLVLARAFTEEGTVVGEINPLSFVTGHTGEDVKAAYELFRSGFEWNDNTIDESQILQRLARGVINENRRLPQDGPTE [Source organism chain B]=bat/Guatemala/060/2010 [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=bat/Guatemala/060/2010 [Accession]=MF7000891 [Entry] [Entry number]=1076 [Entry name]=Triose-phosphate isomerase (Leishmania mexicana) [PDB ID]=1amk [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Triosephosphate isomerase [Evidence level]=Direct evidence [Evidence text]=Two-state unfolding behavior was proved experimentally for sveral members of the family. Isolated monomers are not stable at all. (PMID:15037083, PMID:10785370, PMID:26206330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000892,MF7000893,MF7000894,MF7000895,MF7000896 [UniProt ID chain A]=P48499 [UniProt boundaries chain A]=2-251 [UniProt coverage chain A]=99% [Name chain A]=Triosephosphate isomerase [UniProt sequence chain A]=MSAKPQPIAAANWKCNGTTASIEKLVQVFNEHTISHDVQCVVAPTFVHIPLVQAKLRNPKYVISAENAIAKSGAFTGEVSMPILKDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPEFRDIIDATR [Source organism chain A]=Leishmania mexicana [UniProt ID chain A-2]=P48499 [UniProt boundaries chain A-2]=2-251 [UniProt coverage chain A-2]=99% [Name chain A-2]=Triosephosphate isomerase [UniProt sequence chain A-2]=MSAKPQPIAAANWKCNGTTASIEKLVQVFNEHTISHDVQCVVAPTFVHIPLVQAKLRNPKYVISAENAIAKSGAFTGEVSMPILKDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPEFRDIIDATR [Source organism chain A-2]=Leishmania mexicana [ExpTech]=X-ray [Resolution]=1.83 [Source organism]=Leishmania mexicana [Accession]=MF7000892 [Entry] [Entry number]=1077 [Entry name]=Rabbit muscle triosephosphate isomerase [PDB ID]=1r2t [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Triosephosphate isomerase [Evidence level]=Direct evidence [Evidence text]=Two-state unfolding behavior was proved experimentally for sveral members of the family. Isolated monomers are not stable at all. (PMID:15037083, PMID:10785370, PMID:26206330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000892,MF7000893,MF7000894,MF7000895,MF7000896 [UniProt ID chain A]=P00939 [UniProt boundaries chain A]=4-249 [UniProt coverage chain A]=98% [Name chain A]=Triosephosphate isomerase [UniProt sequence chain A]=MAPSRKFFVGGNWKMNGRKKNLGELITTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ [Source organism chain A]=Oryctolagus cuniculus [UniProt ID chain B]=P00939 [UniProt boundaries chain B]=3-249 [UniProt coverage chain B]=99% [Name chain B]=Triosephosphate isomerase [UniProt sequence chain B]=MAPSRKFFVGGNWKMNGRKKNLGELITTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ [Source organism chain B]=Oryctolagus cuniculus [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Oryctolagus cuniculus [Accession]=MF7000893 [Entry] [Entry number]=1078 [Entry name]=Triosephosphate Isomerase (Clostridium perfringens) [PDB ID]=4y8f [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Triosephosphate isomerase [Evidence level]=Direct evidence [Evidence text]=Two-state unfolding behavior was proved experimentally for sveral members of the family. Isolated monomers are not stable at all. (PMID:15037083, PMID:10785370, PMID:26206330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000892,MF7000893,MF7000894,MF7000895,MF7000896 [UniProt ID chain A]=Q8XKU1 [UniProt boundaries chain A]=1-248 [UniProt coverage chain A]=100% [Name chain A]=Triosephosphate isomerase [UniProt sequence chain A]=MRTPIIAGNWKMHYTIDEAVKLVEELKPLVKDAKCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKAAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQANETIAAIRAMVAEMFGQEVADKVRIQYGGSVKPNTIAEQMAKSDIDGALVGGASLVAADFAQIVNY [Source organism chain A]=Clostridium perfringens [UniProt ID chain A-2]=Q8XKU1 [UniProt boundaries chain A-2]=1-248 [UniProt coverage chain A-2]=100% [Name chain A-2]=Triosephosphate isomerase [UniProt sequence chain A-2]=MRTPIIAGNWKMHYTIDEAVKLVEELKPLVKDAKCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKAAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQANETIAAIRAMVAEMFGQEVADKVRIQYGGSVKPNTIAEQMAKSDIDGALVGGASLVAADFAQIVNY [Source organism chain A-2]=Clostridium perfringens [ExpTech]=X-ray [Resolution]=1.54 [Source organism]=Clostridium perfringens [Accession]=MF7000894 [Entry] [Entry number]=1079 [Entry name]=Triosephosphate Isomerase (Deinococcus radiodurans) [PDB ID]=4y90 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Triosephosphate isomerase [Evidence level]=Direct evidence [Evidence text]=Two-state unfolding behavior was proved experimentally for sveral members of the family. Isolated monomers are not stable at all. (PMID:15037083, PMID:10785370, PMID:26206330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000892,MF7000893,MF7000894,MF7000895,MF7000896 [UniProt ID chain A]=Q9RUP5 [UniProt boundaries chain A]=1-244 [UniProt coverage chain A]=100% [Name chain A]=Triosephosphate isomerase [UniProt sequence chain A]=MQTLLALNWKMNKTPTEARSWAEELTTKYAPAEGVDLAVLAPALDLSALAANLPAGIAFGGQDVSAHESGAYTGEISAAMLKDAGASCVVVGHSERREYHDESDAXVAAKARQAQANGLLPIVCVGENLDVRERGEHVPQTLAQLRGSLEGVGADVVVAYEPVWAIGTGKTATADDAEELAAAIRGALREQYGARAEGIRVLYGGSVKPENIAEICGKPNVNGALVGGASLKVPDVLGMLDALR [Source organism chain A]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [UniProt ID chain B]=Q9RUP5 [UniProt boundaries chain B]=1-244 [UniProt coverage chain B]=100% [Name chain B]=Triosephosphate isomerase [UniProt sequence chain B]=MQTLLALNWKMNKTPTEARSWAEELTTKYAPAEGVDLAVLAPALDLSALAANLPAGIAFGGQDVSAHESGAYTGEISAAMLKDAGASCVVVGHSERREYHDESDAXVAAKARQAQANGLLPIVCVGENLDVRERGEHVPQTLAQLRGSLEGVGADVVVAYEPVWAIGTGKTATADDAEELAAAIRGALREQYGARAEGIRVLYGGSVKPENIAEICGKPNVNGALVGGASLKVPDVLGMLDALR [Source organism chain B]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) [Accession]=MF7000895 [Entry] [Entry number]=1080 [Entry name]=Triosephosphate Isomerase (Streptomyces coelicolor) [PDB ID]=4y9a [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Triosephosphate isomerase [Evidence level]=Direct evidence [Evidence text]=Two-state unfolding behavior was proved experimentally for sveral members of the family. Isolated monomers are not stable at all. (PMID:15037083, PMID:10785370, PMID:26206330). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000892,MF7000893,MF7000894,MF7000895,MF7000896 [UniProt ID chain A]=Q9Z520 [UniProt boundaries chain A]=4-257 [UniProt coverage chain A]=98% [Name chain A]=Triosephosphate isomerase [UniProt sequence chain A]=MTTRTPLMAGNWKMNLNHLEAIAHVQKLAFALADKDYDAVEVAVLAPFTDLRSVQTLVDGDKLKIKYGAQDISAHDGGAYTGEISGPMLAKLKCTYVAVGHSERRQYHAETDEIVNAKVKAAYKHGLTPILCVGEELDVREAGNHVEHTLAQVEGGLKDLAAEQAESVVIAYEPVWAIGTGKVCGADDAQEVCAAIRGKLAELYSQELADKVRIQYGGSVKSGNVAEIMAKPDIDGALVGGASLDSDEFVKIVRFRDQ [Source organism chain A]=Streptomyces coelicolor [UniProt ID chain B]=Q9Z520 [UniProt boundaries chain B]=3-257 [UniProt coverage chain B]=98% [Name chain B]=Triosephosphate isomerase [UniProt sequence chain B]=MTTRTPLMAGNWKMNLNHLEAIAHVQKLAFALADKDYDAVEVAVLAPFTDLRSVQTLVDGDKLKIKYGAQDISAHDGGAYTGEISGPMLAKLKCTYVAVGHSERRQYHAETDEIVNAKVKAAYKHGLTPILCVGEELDVREAGNHVEHTLAQVEGGLKDLAAEQAESVVIAYEPVWAIGTGKVCGADDAQEVCAAIRGKLAELYSQELADKVRIQYGGSVKSGNVAEIMAKPDIDGALVGGASLDSDEFVKIVRFRDQ [Source organism chain B]=Streptomyces coelicolor [ExpTech]=X-ray [Resolution]=2.29 [Source organism]=Streptomyces coelicolor [Accession]=MF7000896 [Entry] [Entry number]=1081 [Entry name]=Giant reed (Arundodonax) lectin (ADL) with N-Acetyl glucosamine [PDB ID]=6stn [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Chitin recognition protein [Evidence level]=Indirect evidence [Evidence text]=Within the chitin recognition protein homodimers, two disulfide bridges connect the monomers. SDS PAGE, DLS and MS confirmed that the protein is a dimer in solution. In accordance with the large stability of the dimer, there is a large interaction surface, moreover, the lectin binding site is on the dimer interface, which strongly suggests that the dimeric form is obligate, i.e. required for function (PMID:34192315). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000897,MF7000898,MF7000899,MF7000900 [UniProt ID chain A]=A0A0A9P802 [UniProt boundaries chain A]=38-207 [UniProt coverage chain A]=72% [Name chain A]=Chitin-binding type-1 domain-containing protein [UniProt sequence chain A]=MAMFLAARSRAAKLHGAMRALALGALITLAGVIVAKGAEECGKQGGGALCPNNVCCSMWGYCGLGPDYCGTGCQSGACCPGKRCGKQANGETCPNNLCCSKDGYCGFGAEYCGNGCQSGPCRADRKCGTLAGGQLCPDNLCCSQWGYCGLGVEFCSDGCQSGACISMRCGRQASGAKCTNNYCCGGSGYCGLGSDYCGAGCQSGPCTSGVGAAALPMGELFNETATPVETIALVA [Source organism chain A]=Arundo donax [UniProt ID chain B]=A0A0A9P802 [UniProt boundaries chain B]=38-207 [UniProt coverage chain B]=72% [Name chain B]=Chitin-binding type-1 domain-containing protein [UniProt sequence chain B]=MAMFLAARSRAAKLHGAMRALALGALITLAGVIVAKGAEECGKQGGGALCPNNVCCSMWGYCGLGPDYCGTGCQSGACCPGKRCGKQANGETCPNNLCCSKDGYCGFGAEYCGNGCQSGPCRADRKCGTLAGGQLCPDNLCCSQWGYCGLGVEFCSDGCQSGACISMRCGRQASGAKCTNNYCCGGSGYCGLGSDYCGAGCQSGPCTSGVGAAALPMGELFNETATPVETIALVA [Source organism chain B]=Arundo donax [ExpTech]=X-ray [Resolution]=1.75 [Source organism]=Arundo donax [Accession]=MF7000897 [Entry] [Entry number]=1082 [Entry name]=Giant reed (Arundodonax) lectin (ADL) [PDB ID]=6stm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Chitin recognition protein [Evidence level]=Indirect evidence [Evidence text]=Within the chitin recognition protein homodimers, two disulfide bridges connect the monomers. SDS PAGE, DLS and MS confirmed that the protein is a dimer in solution. In accordance with the large stability of the dimer, there is a large interaction surface, moreover, the lectin binding site is on the dimer interface, which strongly suggests that the dimeric form is obligate, i.e. required for function (PMID:34192315). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000897,MF7000898,MF7000899,MF7000900 [UniProt ID chain A]=A0A0A9P802 [UniProt boundaries chain A]=38-207 [UniProt coverage chain A]=72% [Name chain A]=Chitin-binding type-1 domain-containing protein [UniProt sequence chain A]=MAMFLAARSRAAKLHGAMRALALGALITLAGVIVAKGAEECGKQGGGALCPNNVCCSMWGYCGLGPDYCGTGCQSGACCPGKRCGKQANGETCPNNLCCSKDGYCGFGAEYCGNGCQSGPCRADRKCGTLAGGQLCPDNLCCSQWGYCGLGVEFCSDGCQSGACISMRCGRQASGAKCTNNYCCGGSGYCGLGSDYCGAGCQSGPCTSGVGAAALPMGELFNETATPVETIALVA [Source organism chain A]=Arundo donax [UniProt ID chain B]=A0A0A9P802 [UniProt boundaries chain B]=38-207 [UniProt coverage chain B]=72% [Name chain B]=Chitin-binding type-1 domain-containing protein [UniProt sequence chain B]=MAMFLAARSRAAKLHGAMRALALGALITLAGVIVAKGAEECGKQGGGALCPNNVCCSMWGYCGLGPDYCGTGCQSGACCPGKRCGKQANGETCPNNLCCSKDGYCGFGAEYCGNGCQSGPCRADRKCGTLAGGQLCPDNLCCSQWGYCGLGVEFCSDGCQSGACISMRCGRQASGAKCTNNYCCGGSGYCGLGSDYCGAGCQSGPCTSGVGAAALPMGELFNETATPVETIALVA [Source organism chain B]=Arundo donax [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Arundo donax [Accession]=MF7000898 [Entry] [Entry number]=1083 [Entry name]=Giant reed (Arundodonax) lectin (ADL) with N-Acetyl lactosamine [PDB ID]=6sto [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Chitin recognition protein [Evidence level]=Indirect evidence [Evidence text]=Within the chitin recognition protein homodimers, two disulfide bridges connect the monomers. SDS PAGE, DLS and MS confirmed that the protein is a dimer in solution. In accordance with the large stability of the dimer, there is a large interaction surface, moreover, the lectin binding site is on the dimer interface, which strongly suggests that the dimeric form is obligate, i.e. required for function (PMID:34192315). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000897,MF7000898,MF7000899,MF7000900 [UniProt ID chain A]=A0A0A9P802 [UniProt boundaries chain A]=38-207 [UniProt coverage chain A]=72% [Name chain A]=Chitin-binding type-1 domain-containing protein [UniProt sequence chain A]=MAMFLAARSRAAKLHGAMRALALGALITLAGVIVAKGAEECGKQGGGALCPNNVCCSMWGYCGLGPDYCGTGCQSGACCPGKRCGKQANGETCPNNLCCSKDGYCGFGAEYCGNGCQSGPCRADRKCGTLAGGQLCPDNLCCSQWGYCGLGVEFCSDGCQSGACISMRCGRQASGAKCTNNYCCGGSGYCGLGSDYCGAGCQSGPCTSGVGAAALPMGELFNETATPVETIALVA [Source organism chain A]=Arundo donax [UniProt ID chain B]=A0A0A9P802 [UniProt boundaries chain B]=38-207 [UniProt coverage chain B]=72% [Name chain B]=Chitin-binding type-1 domain-containing protein [UniProt sequence chain B]=MAMFLAARSRAAKLHGAMRALALGALITLAGVIVAKGAEECGKQGGGALCPNNVCCSMWGYCGLGPDYCGTGCQSGACCPGKRCGKQANGETCPNNLCCSKDGYCGFGAEYCGNGCQSGPCRADRKCGTLAGGQLCPDNLCCSQWGYCGLGVEFCSDGCQSGACISMRCGRQASGAKCTNNYCCGGSGYCGLGSDYCGAGCQSGPCTSGVGAAALPMGELFNETATPVETIALVA [Source organism chain B]=Arundo donax [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Arundo donax [Accession]=MF7000899 [Entry] [Entry number]=1084 [Entry name]=Giant reed (Arundodonax) lectin (ADL) with sialic acid [PDB ID]=6stp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Chitin recognition protein [Evidence level]=Indirect evidence [Evidence text]=Within the chitin recognition protein homodimers, two disulfide bridges connect the monomers. SDS PAGE, DLS and MS confirmed that the protein is a dimer in solution. In accordance with the large stability of the dimer, there is a large interaction surface, moreover, the lectin binding site is on the dimer interface, which strongly suggests that the dimeric form is obligate, i.e. required for function (PMID:34192315). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000897,MF7000898,MF7000899,MF7000900 [UniProt ID chain A]=A0A0A9P802 [UniProt boundaries chain A]=38-207 [UniProt coverage chain A]=72% [Name chain A]=Chitin-binding type-1 domain-containing protein [UniProt sequence chain A]=MAMFLAARSRAAKLHGAMRALALGALITLAGVIVAKGAEECGKQGGGALCPNNVCCSMWGYCGLGPDYCGTGCQSGACCPGKRCGKQANGETCPNNLCCSKDGYCGFGAEYCGNGCQSGPCRADRKCGTLAGGQLCPDNLCCSQWGYCGLGVEFCSDGCQSGACISMRCGRQASGAKCTNNYCCGGSGYCGLGSDYCGAGCQSGPCTSGVGAAALPMGELFNETATPVETIALVA [Source organism chain A]=Arundo donax [UniProt ID chain B]=A0A0A9P802 [UniProt boundaries chain B]=38-207 [UniProt coverage chain B]=72% [Name chain B]=Chitin-binding type-1 domain-containing protein [UniProt sequence chain B]=MAMFLAARSRAAKLHGAMRALALGALITLAGVIVAKGAEECGKQGGGALCPNNVCCSMWGYCGLGPDYCGTGCQSGACCPGKRCGKQANGETCPNNLCCSKDGYCGFGAEYCGNGCQSGPCRADRKCGTLAGGQLCPDNLCCSQWGYCGLGVEFCSDGCQSGACISMRCGRQASGAKCTNNYCCGGSGYCGLGSDYCGAGCQSGPCTSGVGAAALPMGELFNETATPVETIALVA [Source organism chain B]=Arundo donax [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Arundo donax [Accession]=MF7000900 [Entry] [Entry number]=1085 [Entry name]=IreB homodimer [PDB ID]=5us5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=IreB regulatory phosphoprotein [Evidence level]=Indirect evidence [Evidence text]=Each IreB protomer contains a disordered N-terminus and 4 α-helices, with the α4 helix being partially domain-swapped within the dimer. The domain-swapped topology of IreB implies that monomeric IreB is not a stably folded protein. SEC revealed that IreB is predominantly in a dimeric form in solution, which was further confirmed by AUC even at low micromolar concentrations (PMID:28551334). The crystal structure of the related protein CcpS also shows a disordered N-terminus. Authors suggest that the homodimeric structure is obligate, because it is essential for function (PMID:37120581). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000901,MF7000902,MF7000903,MF7000904 [UniProt ID chain A]=Q836B3 [UniProt boundaries chain A]=1-89 [UniProt coverage chain A]=100% [Name chain A]=UPF0297 protein EF_1202 [UniProt sequence chain A]=MGFTDETVRFDFDDNRKKAISETLETVYRALEEKGYNPINQIVGYLLSGDPAYIPRYQDARNLIRRHERDEIMEELTKYYLANHGIDIK [Source organism chain A]=Enterococcus faecalis [UniProt ID chain B]=Q836B3 [UniProt boundaries chain B]=1-89 [UniProt coverage chain B]=100% [Name chain B]=UPF0297 protein EF_1202 [UniProt sequence chain B]=MGFTDETVRFDFDDNRKKAISETLETVYRALEEKGYNPINQIVGYLLSGDPAYIPRYQDARNLIRRHERDEIMEELTKYYLANHGIDIK [Source organism chain B]=Enterococcus faecalis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Enterococcus faecalis [Accession]=MF7000901 [Entry] [Entry number]=1086 [Entry name]=ReoM (Listeria monocytogenes) [PDB ID]=6tif [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=IreB regulatory phosphoprotein [Evidence level]=Indirect evidence [Evidence text]=Each IreB protomer contains a disordered N-terminus and 4 α-helices, with the α4 helix being partially domain-swapped within the dimer. The domain-swapped topology of IreB implies that monomeric IreB is not a stably folded protein. SEC revealed that IreB is predominantly in a dimeric form in solution, which was further confirmed by AUC even at low micromolar concentrations (PMID:28551334). The crystal structure of the related protein CcpS also shows a disordered N-terminus. Authors suggest that the homodimeric structure is obligate, because it is essential for function (PMID:37120581). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000901,MF7000902,MF7000903,MF7000904 [UniProt ID chain B]=P60357 [UniProt boundaries chain B]=2-88 [UniProt coverage chain B]=96% [Name chain B]=UPF0297 protein lmo1503 [UniProt sequence chain B]=MDSKDQTMFYNFGDDSIEEDVKKLMKQVYVALEEKGYNPVNQIVGYLLSGDPAYIPRHKDARSMIRRLERDEIIEELVKAYLKNNEIGEK [Source organism chain B]=Listeria monocytogenes serovar 1/2a [UniProt ID chain A]=P60357 [UniProt boundaries chain A]=5-88 [UniProt coverage chain A]=93% [Name chain A]=UPF0297 protein lmo1503 [UniProt sequence chain A]=MDSKDQTMFYNFGDDSIEEDVKKLMKQVYVALEEKGYNPVNQIVGYLLSGDPAYIPRHKDARSMIRRLERDEIIEELVKAYLKNNEIGEK [Source organism chain A]=Listeria monocytogenes serovar 1/2a [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Listeria monocytogenes serovar 1/2a [Accession]=MF7000902 [Entry] [Entry number]=1087 [Entry name]=CcpS mutant [PDB ID]=7y86 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=IreB regulatory phosphoprotein [Evidence level]=Indirect evidence [Evidence text]=Each IreB protomer contains a disordered N-terminus and 4 α-helices, with the α4 helix being partially domain-swapped within the dimer. The domain-swapped topology of IreB implies that monomeric IreB is not a stably folded protein. SEC revealed that IreB is predominantly in a dimeric form in solution, which was further confirmed by AUC even at low micromolar concentrations (PMID:28551334). The crystal structure of the related protein CcpS also shows a disordered N-terminus. Authors suggest that the homodimeric structure is obligate, because it is essential for function (PMID:37120581). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000901,MF7000902,MF7000903,MF7000904 [UniProt ID chain A]=A0A0K2E3A3 [UniProt boundaries chain A]=8-88 [UniProt coverage chain A]=92% [Name chain A]=UPF0297 protein A7J08_00425 [UniProt sequence chain A]=MGFTEETVRFRLDDTDKQEISKTLTSVYRSLEEKGYNPINQIIGYVLSGDPAYIPRYNDARNQIRKHERDEIIEELVRYYLKGNGIDL [Source organism chain A]=Streptococcus suis [UniProt ID chain B]=A0A0K2E3A3 [UniProt boundaries chain B]=8-88 [UniProt coverage chain B]=92% [Name chain B]=UPF0297 protein A7J08_00425 [UniProt sequence chain B]=MGFTEETVRFRLDDTDKQEISKTLTSVYRSLEEKGYNPINQIIGYVLSGDPAYIPRYNDARNQIRKHERDEIIEELVRYYLKGNGIDL [Source organism chain B]=Streptococcus suis [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Streptococcus suis [Accession]=MF7000903 [Entry] [Entry number]=1088 [Entry name]=CcpS [PDB ID]=7y8z [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=IreB regulatory phosphoprotein [Evidence level]=Indirect evidence [Evidence text]=Each IreB protomer contains a disordered N-terminus and 4 α-helices, with the α4 helix being partially domain-swapped within the dimer. The domain-swapped topology of IreB implies that monomeric IreB is not a stably folded protein. SEC revealed that IreB is predominantly in a dimeric form in solution, which was further confirmed by AUC even at low micromolar concentrations (PMID:28551334). The crystal structure of the related protein CcpS also shows a disordered N-terminus. Authors suggest that the homodimeric structure is obligate, because it is essential for function (PMID:37120581). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000901,MF7000902,MF7000903,MF7000904 [UniProt ID chain A]=A0A0K2E3A3 [UniProt boundaries chain A]=18-88 [UniProt coverage chain A]=80% [Name chain A]=UPF0297 protein A7J08_00425 [UniProt sequence chain A]=MGFTEETVRFRLDDTDKQEISKTLTSVYRSLEEKGYNPINQIIGYVLSGDPAYIPRYNDARNQIRKHERDEIIEELVRYYLKGNGIDL [Source organism chain A]=Streptococcus suis [UniProt ID chain B]=A0A0K2E3A3 [UniProt boundaries chain B]=7-88 [UniProt coverage chain B]=93% [Name chain B]=UPF0297 protein A7J08_00425 [UniProt sequence chain B]=MGFTEETVRFRLDDTDKQEISKTLTSVYRSLEEKGYNPINQIIGYVLSGDPAYIPRYNDARNQIRKHERDEIIEELVRYYLKGNGIDL [Source organism chain B]=Streptococcus suis [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Streptococcus suis [Accession]=MF7000904 [Entry] [Entry number]=1089 [Entry name]=BAR-PH domain of human APPL1 [PDB ID]=2elb [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=APPL BAR domain [Sequence domain]=APPL BAR domain [Evidence level]=Direct evidence [Evidence text]=The two BAR domains form a tightly packed dimer with a crescent-like shape, a hallmark of BAR domain dimers. The helix α1 forms an antiparallel helix bundle with its symmetry counterpart because it packs against α3 of the other protomer on the convex side of the dimer. A huge solvent accessible surface (SAS) area gets buried in the dimer interface. The addition of each α4 helix to the canonical BAR motif results in a large increase in buried SAS on the two protomers, corresponding to over 40% of the total buried SAS. Other BAR domains (N-BARs) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). In some structures of the family an independently folded PH domain is also included in the structure, so only a part of the structure undergoes MSF. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000905,MF7000906,MF7000154,MF7000907 [UniProt ID chain A]=Q9UKG1 [UniProt boundaries chain A]=6-374 [UniProt coverage chain A]=52% [Name chain A]=DCC-interacting protein 13-alpha [UniProt sequence chain A]=MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNEQLEEFLANIGTSVQNVRREMDSDIETMQQTIEDLEVASDPLYVPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPAAGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQENKRLFGFVLRTSSGRSESNLSSVCYIFESNNEGEKICDSVGLAKQIALHAELDRRASEKQKEIERVKEKQQKELNKQKQIEKDLEEQSRLIAASSRPNQASSEGQFVVLSSSQSEESDLGEGGKKRESEA [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q9UKG1 [UniProt boundaries chain A-2]=6-374 [UniProt coverage chain A-2]=52% [Name chain A-2]=DCC-interacting protein 13-alpha [UniProt sequence chain A-2]=MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNEQLEEFLANIGTSVQNVRREMDSDIETMQQTIEDLEVASDPLYVPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPAAGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQENKRLFGFVLRTSSGRSESNLSSVCYIFESNNEGEKICDSVGLAKQIALHAELDRRASEKQKEIERVKEKQQKELNKQKQIEKDLEEQSRLIAASSRPNQASSEGQFVVLSSSQSEESDLGEGGKKRESEA [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Homo sapiens [Accession]=MF7000905 [Entry] [Entry number]=1090 [Entry name]=BAR-PH domain of APPL1 [PDB ID]=2q13 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=APPL BAR domain [Sequence domain]=APPL BAR domain [Evidence level]=Direct evidence [Evidence text]=The two BAR domains form a tightly packed dimer with a crescent-like shape, a hallmark of BAR domain dimers. The helix α1 forms an antiparallel helix bundle with its symmetry counterpart because it packs against α3 of the other protomer on the convex side of the dimer. A huge solvent accessible surface (SAS) area gets buried in the dimer interface. The addition of each α4 helix to the canonical BAR motif results in a large increase in buried SAS on the two protomers, corresponding to over 40% of the total buried SAS. Other BAR domains (N-BARs) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). In some structures of the family an independently folded PH domain is also included in the structure, so only a part of the structure undergoes MSF. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000905,MF7000906,MF7000154,MF7000907 [UniProt ID chain A]=Q9UKG1 [UniProt boundaries chain A]=5-378 [UniProt coverage chain A]=52% [Name chain A]=DCC-interacting protein 13-alpha [UniProt sequence chain A]=MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNEQLEEFLANIGTSVQNVRREMDSDIETMQQTIEDLEVASDPLYVPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPAAGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQENKRLFGFVLRTSSGRSESNLSSVCYIFESNNEGEKICDSVGLAKQIALHAELDRRASEKQKEIERVKEKQQKELNKQKQIEKDLEEQSRLIAASSRPNQASSEGQFVVLSSSQSEESDLGEGGKKRESEA [Source organism chain A]=Homo sapiens [UniProt ID chain A-2]=Q9UKG1 [UniProt boundaries chain A-2]=5-378 [UniProt coverage chain A-2]=52% [Name chain A-2]=DCC-interacting protein 13-alpha [UniProt sequence chain A-2]=MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNEQLEEFLANIGTSVQNVRREMDSDIETMQQTIEDLEVASDPLYVPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPAAGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQENKRLFGFVLRTSSGRSESNLSSVCYIFESNNEGEKICDSVGLAKQIALHAELDRRASEKQKEIERVKEKQQKELNKQKQIEKDLEEQSRLIAASSRPNQASSEGQFVVLSSSQSEESDLGEGGKKRESEA [Source organism chain A-2]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=Homo sapiens [Accession]=MF7000906 [Entry] [Entry number]=1091 [Entry name]=BAR-PH domain of ACAP1 [PDB ID]=4nsw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=APPL BAR domain [Sequence domain]=APPL BAR domain [Evidence level]=Direct evidence [Evidence text]=The two BAR domains form a tightly packed dimer with a crescent-like shape, a hallmark of BAR domain dimers. The helix α1 forms an antiparallel helix bundle with its symmetry counterpart because it packs against α3 of the other protomer on the convex side of the dimer. A huge solvent accessible surface (SAS) area gets buried in the dimer interface. The addition of each α4 helix to the canonical BAR motif results in a large increase in buried SAS on the two protomers, corresponding to over 40% of the total buried SAS. Other BAR domains (N-BARs) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187). In some structures of the family an independently folded PH domain is also included in the structure, so only a part of the structure undergoes MSF. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000905,MF7000906,MF7000154,MF7000907 [UniProt ID chain A]=Q15027 [UniProt boundaries chain A]=1-364 [UniProt coverage chain A]=49% [Name chain A]=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 [UniProt sequence chain A]=MTVKLDFEECLKDSPRFRASIELVEAEVSELETRLEKLLKLGTGLLESGRHYLAASRAFVVGICDLARLGPPEPMMAECLEKFTVSLNHKLDSHAELLDATQHTLQQQIQTLVKEGLRGFREARRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALRTARAGYRGRALDYALQINVIEDKRKFDIMEFVLRLVEAQATHFQQGHEELSRLSQYRKELGAQLHQLVLNSAREKRDMEQRHVLLKQKELGGEEPEPSLREGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQLVYQKKYKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSTSKSCLLQADSERLLQLWVSAVQSSIASAFSQARLDDSPRGPGQGSGHLAIGSAATLGSGGMARGREPGGVGHVVAQVQSVDGNAQCCDCREPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEPELVKLMCELGNVIINQIYEARVEAMAVKKPGPSCSRQEKEAWIHAKYVEKKFLTKLPEIRGRRGGRGRPRGQPPVPPKPSIRPRPGSLRSKPEPPSEDLGSLHPGALLFRASGHPPSLPTMADALAHGADVNWVNGGQDNATPLIQATAANSLLACEFLLQNGANVNQADSAGRGPLHHATILGHTGLACLFLKRGADLGARDSEGRDPLTIAMETANADIVTLLRLAKMREAEAAQGQAGDETYLDIFRDFSLMASDDPEKLSRRSHDLHTL [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q15027 [UniProt boundaries chain B]=1-361 [UniProt coverage chain B]=48% [Name chain B]=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 [UniProt sequence chain B]=MTVKLDFEECLKDSPRFRASIELVEAEVSELETRLEKLLKLGTGLLESGRHYLAASRAFVVGICDLARLGPPEPMMAECLEKFTVSLNHKLDSHAELLDATQHTLQQQIQTLVKEGLRGFREARRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALRTARAGYRGRALDYALQINVIEDKRKFDIMEFVLRLVEAQATHFQQGHEELSRLSQYRKELGAQLHQLVLNSAREKRDMEQRHVLLKQKELGGEEPEPSLREGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQLVYQKKYKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSTSKSCLLQADSERLLQLWVSAVQSSIASAFSQARLDDSPRGPGQGSGHLAIGSAATLGSGGMARGREPGGVGHVVAQVQSVDGNAQCCDCREPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEPELVKLMCELGNVIINQIYEARVEAMAVKKPGPSCSRQEKEAWIHAKYVEKKFLTKLPEIRGRRGGRGRPRGQPPVPPKPSIRPRPGSLRSKPEPPSEDLGSLHPGALLFRASGHPPSLPTMADALAHGADVNWVNGGQDNATPLIQATAANSLLACEFLLQNGANVNQADSAGRGPLHHATILGHTGLACLFLKRGADLGARDSEGRDPLTIAMETANADIVTLLRLAKMREAEAAQGQAGDETYLDIFRDFSLMASDDPEKLSRRSHDLHTL [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Homo sapiens [Accession]=MF7000907 [Entry] [Entry number]=1092 [Entry name]=H49N mutant dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase with TDP (Aneurinibacillus thermoaerophilus) [PDB ID]=2pae [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=WxcM-like, C-terminal [Evidence level]=No contradicting information [Evidence text]=Domain-swapped dimer with extensive subunit-subunit interface mainly contributed by beta sheet augmentation (PMID:17459872). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000908,MF7000909,MF7000910,MF7000911 [UniProt ID chain A]=Q6T1W8 [UniProt boundaries chain A]=1-136 [UniProt coverage chain A]=97% [Name chain A]=TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase [UniProt sequence chain A]=MENKVINFKKIIDSRGSLVAIEENKNIPFSIKRVYYIFDTKGEEPRGFHAHKKLEQVLVCLNGSCRVILDDGNIIQEITLDSPAVGLYVGPAVWHEMHDFSSDCVMMVLASDYYDETDYIRQYDNFKKYIAKINLEKEG [Source organism chain A]=Aneurinibacillus thermoaerophilus [UniProt ID chain B]=Q6T1W8 [UniProt boundaries chain B]=2-135 [UniProt coverage chain B]=96% [Name chain B]=TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase [UniProt sequence chain B]=MENKVINFKKIIDSRGSLVAIEENKNIPFSIKRVYYIFDTKGEEPRGFHAHKKLEQVLVCLNGSCRVILDDGNIIQEITLDSPAVGLYVGPAVWHEMHDFSSDCVMMVLASDYYDETDYIRQYDNFKKYIAKINLEKEG [Source organism chain B]=Aneurinibacillus thermoaerophilus [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Aneurinibacillus thermoaerophilus [Accession]=MF7000908 [Entry] [Entry number]=1093 [Entry name]=Wild-Type dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase with TDP (Aneurinibacillus thermoaerophilus) [PDB ID]=2pa7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=WxcM-like, C-terminal [Evidence level]=No contradicting information [Evidence text]=Domain-swapped dimer with extensive subunit-subunit interface mainly contributed by beta sheet augmentation (PMID:17459872). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000908,MF7000909,MF7000910,MF7000911 [UniProt ID chain A]=Q6T1W8 [UniProt boundaries chain A]=2-136 [UniProt coverage chain A]=97% [Name chain A]=TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase [UniProt sequence chain A]=MENKVINFKKIIDSRGSLVAIEENKNIPFSIKRVYYIFDTKGEEPRGFHAHKKLEQVLVCLNGSCRVILDDGNIIQEITLDSPAVGLYVGPAVWHEMHDFSSDCVMMVLASDYYDETDYIRQYDNFKKYIAKINLEKEG [Source organism chain A]=Aneurinibacillus thermoaerophilus [UniProt ID chain B]=Q6T1W8 [UniProt boundaries chain B]=2-135 [UniProt coverage chain B]=96% [Name chain B]=TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase [UniProt sequence chain B]=MENKVINFKKIIDSRGSLVAIEENKNIPFSIKRVYYIFDTKGEEPRGFHAHKKLEQVLVCLNGSCRVILDDGNIIQEITLDSPAVGLYVGPAVWHEMHDFSSDCVMMVLASDYYDETDYIRQYDNFKKYIAKINLEKEG [Source organism chain B]=Aneurinibacillus thermoaerophilus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Aneurinibacillus thermoaerophilus [Accession]=MF7000909 [Entry] [Entry number]=1094 [Entry name]=H51N mutant dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase with TDP (Aneurinibacillus thermoaerophilus) [PDB ID]=2pak [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=WxcM-like, C-terminal [Evidence level]=No contradicting information [Evidence text]=Domain-swapped dimer with extensive subunit-subunit interface mainly contributed by beta sheet augmentation (PMID:17459872). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000908,MF7000909,MF7000910,MF7000911 [UniProt ID chain A]=Q6T1W8 [UniProt boundaries chain A]=2-136 [UniProt coverage chain A]=97% [Name chain A]=TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase [UniProt sequence chain A]=MENKVINFKKIIDSRGSLVAIEENKNIPFSIKRVYYIFDTKGEEPRGFHAHKKLEQVLVCLNGSCRVILDDGNIIQEITLDSPAVGLYVGPAVWHEMHDFSSDCVMMVLASDYYDETDYIRQYDNFKKYIAKINLEKEG [Source organism chain A]=Aneurinibacillus thermoaerophilus [UniProt ID chain B]=Q6T1W8 [UniProt boundaries chain B]=2-135 [UniProt coverage chain B]=96% [Name chain B]=TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase [UniProt sequence chain B]=MENKVINFKKIIDSRGSLVAIEENKNIPFSIKRVYYIFDTKGEEPRGFHAHKKLEQVLVCLNGSCRVILDDGNIIQEITLDSPAVGLYVGPAVWHEMHDFSSDCVMMVLASDYYDETDYIRQYDNFKKYIAKINLEKEG [Source organism chain B]=Aneurinibacillus thermoaerophilus [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Aneurinibacillus thermoaerophilus [Accession]=MF7000910 [Entry] [Entry number]=1095 [Entry name]=H49N, H51N double mutant dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase with TDP (Aneurinibacillus thermoaerophilus) [PDB ID]=2pam [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=WxcM-like, C-terminal [Evidence level]=No contradicting information [Evidence text]=Domain-swapped dimer with extensive subunit-subunit interface mainly contributed by beta sheet augmentation (PMID:17459872). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000908,MF7000909,MF7000910,MF7000911 [UniProt ID chain A]=Q6T1W8 [UniProt boundaries chain A]=2-136 [UniProt coverage chain A]=97% [Name chain A]=TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase [UniProt sequence chain A]=MENKVINFKKIIDSRGSLVAIEENKNIPFSIKRVYYIFDTKGEEPRGFHAHKKLEQVLVCLNGSCRVILDDGNIIQEITLDSPAVGLYVGPAVWHEMHDFSSDCVMMVLASDYYDETDYIRQYDNFKKYIAKINLEKEG [Source organism chain A]=Aneurinibacillus thermoaerophilus [UniProt ID chain B]=Q6T1W8 [UniProt boundaries chain B]=2-135 [UniProt coverage chain B]=96% [Name chain B]=TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase [UniProt sequence chain B]=MENKVINFKKIIDSRGSLVAIEENKNIPFSIKRVYYIFDTKGEEPRGFHAHKKLEQVLVCLNGSCRVILDDGNIIQEITLDSPAVGLYVGPAVWHEMHDFSSDCVMMVLASDYYDETDYIRQYDNFKKYIAKINLEKEG [Source organism chain B]=Aneurinibacillus thermoaerophilus [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Aneurinibacillus thermoaerophilus [Accession]=MF7000911 [Entry] [Entry number]=1096 [Entry name]=Bi-functional enzyme [PDB ID]=6j22 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Histidine biosynthesis bifunctional protein [Evidence level]=Indirect evidence [Evidence text]=HisIE and MtHISN2 are proteins with with discrete and directly interacting pyrophosphohydrolase and cyclohydrolase domains. They form a tight dimer with large buried interface. The dimer is formed by two mutually swapped polypeptide chains, forming a bilobial protein. The existence of a monomeric form of either PRA-PH or PRA-CH domain is highly improbable. The dimeric form is consistent with the size-exclusion elution profile. In case of HisIE dimerization is very important for catalytic activity, since its catalytic pocket is formed by both protomers. Arg201 from one monomer is required to stabilize helix 4 in the other monomer, thus making it suitable for substrate binding (PMID:31235255, PMID:33958623). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000912,MF7000913,MF7000914 [UniProt ID chain A]=P37793 [UniProt boundaries chain A]=2-201 [UniProt coverage chain A]=98% [Name chain A]=Histidine biosynthesis bifunctional protein HisIE [UniProt sequence chain A]=MLTEQQRRELDWEKTDGLMPVIVQHAVSGEVLMLGYMNPEALDKTIESGKVTFFSRTKQRLWIKGETSGNFLNVVSIAPDCDNDTLLVLANPIGPTCHKGTSSCFGNTAHQWLFLYQLEQLLAERKYADPETSYTAKLYASGTKRIAQKVGEEGVETALAATVHDRFELTNEASDLMYHLLVLLQDQDLDLTTVIENLHKRHQ [Source organism chain A]=Shigella flexneri [UniProt ID chain B]=P37793 [UniProt boundaries chain B]=3-201 [UniProt coverage chain B]=98% [Name chain B]=Histidine biosynthesis bifunctional protein HisIE [UniProt sequence chain B]=MLTEQQRRELDWEKTDGLMPVIVQHAVSGEVLMLGYMNPEALDKTIESGKVTFFSRTKQRLWIKGETSGNFLNVVSIAPDCDNDTLLVLANPIGPTCHKGTSSCFGNTAHQWLFLYQLEQLLAERKYADPETSYTAKLYASGTKRIAQKVGEEGVETALAATVHDRFELTNEASDLMYHLLVLLQDQDLDLTTVIENLHKRHQ [Source organism chain B]=Shigella flexneri [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Shigella flexneri [Accession]=MF7000912 [Entry] [Entry number]=1097 [Entry name]=Bi-functional enzyme [PDB ID]=6j2l [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Histidine biosynthesis bifunctional protein [Evidence level]=Indirect evidence [Evidence text]=HisIE and MtHISN2 are proteins with with discrete and directly interacting pyrophosphohydrolase and cyclohydrolase domains. They form a tight dimer with large buried interface. The dimer is formed by two mutually swapped polypeptide chains, forming a bilobial protein. The existence of a monomeric form of either PRA-PH or PRA-CH domain is highly improbable. The dimeric form is consistent with the size-exclusion elution profile. In case of HisIE dimerization is very important for catalytic activity, since its catalytic pocket is formed by both protomers. Arg201 from one monomer is required to stabilize helix 4 in the other monomer, thus making it suitable for substrate binding (PMID:31235255, PMID:33958623). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000912,MF7000913,MF7000914 [UniProt ID chain A]=P37793 [UniProt boundaries chain A]=2-201 [UniProt coverage chain A]=98% [Name chain A]=Histidine biosynthesis bifunctional protein HisIE [UniProt sequence chain A]=MLTEQQRRELDWEKTDGLMPVIVQHAVSGEVLMLGYMNPEALDKTIESGKVTFFSRTKQRLWIKGETSGNFLNVVSIAPDCDNDTLLVLANPIGPTCHKGTSSCFGNTAHQWLFLYQLEQLLAERKYADPETSYTAKLYASGTKRIAQKVGEEGVETALAATVHDRFELTNEASDLMYHLLVLLQDQDLDLTTVIENLHKRHQ [Source organism chain A]=Shigella flexneri [UniProt ID chain B]=P37793 [UniProt boundaries chain B]=3-201 [UniProt coverage chain B]=98% [Name chain B]=Histidine biosynthesis bifunctional protein HisIE [UniProt sequence chain B]=MLTEQQRRELDWEKTDGLMPVIVQHAVSGEVLMLGYMNPEALDKTIESGKVTFFSRTKQRLWIKGETSGNFLNVVSIAPDCDNDTLLVLANPIGPTCHKGTSSCFGNTAHQWLFLYQLEQLLAERKYADPETSYTAKLYASGTKRIAQKVGEEGVETALAATVHDRFELTNEASDLMYHLLVLLQDQDLDLTTVIENLHKRHQ [Source organism chain B]=Shigella flexneri [ExpTech]=X-ray [Resolution]=2.17 [Source organism]=Shigella flexneri [Accession]=MF7000913 [Entry] [Entry number]=1098 [Entry name]=MtHISN2, a bifunctional enzyme [PDB ID]=7bgm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Histidine biosynthesis bifunctional protein [Evidence level]=Indirect evidence [Evidence text]=HisIE and MtHISN2 are proteins with with discrete and directly interacting pyrophosphohydrolase and cyclohydrolase domains. They form a tight dimer with large buried interface. The dimer is formed by two mutually swapped polypeptide chains, forming a bilobial protein. The existence of a monomeric form of either PRA-PH or PRA-CH domain is highly improbable. The dimeric form is consistent with the size-exclusion elution profile. In case of HisIE dimerization is very important for catalytic activity, since its catalytic pocket is formed by both protomers. Arg201 from one monomer is required to stabilize helix 4 in the other monomer, thus making it suitable for substrate binding (PMID:31235255, PMID:33958623). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000912,MF7000913,MF7000914 [UniProt ID chain A]=A0A072U2X9 [UniProt boundaries chain A]=49-264 [UniProt coverage chain A]=76% [Name chain A]=Histidine biosynthesis hisIE protein [UniProt sequence chain A]=MALSNVHMLQSARGFQKCNLSFSSHGYPRRGYRTNHLAFASMHTSDPKVDSLLDSVKWDNKGLAVAIAQNVDTGAILMQGFANREAVATTISSRKATFYSRSRSSLWTKGETSNNFINVHDVFLDCDRDSIIYLGKPDGPTCHTGAETCYYTPVFDLLKEEEVEGNKLALTSLYALESTISQRKAEVVEENGKPSWTKRLLLNDKLLCSKIREEANELCETLENNEDKSRTASEMADVLYHAMVLLALKDVKVEEVLQVLRQRFSKSGIEEKRSRPTQKSVEN [Source organism chain A]=Medicago truncatula [UniProt ID chain B]=A0A072U2X9 [UniProt boundaries chain B]=49-265 [UniProt coverage chain B]=76% [Name chain B]=Histidine biosynthesis hisIE protein [UniProt sequence chain B]=MALSNVHMLQSARGFQKCNLSFSSHGYPRRGYRTNHLAFASMHTSDPKVDSLLDSVKWDNKGLAVAIAQNVDTGAILMQGFANREAVATTISSRKATFYSRSRSSLWTKGETSNNFINVHDVFLDCDRDSIIYLGKPDGPTCHTGAETCYYTPVFDLLKEEEVEGNKLALTSLYALESTISQRKAEVVEENGKPSWTKRLLLNDKLLCSKIREEANELCETLENNEDKSRTASEMADVLYHAMVLLALKDVKVEEVLQVLRQRFSKSGIEEKRSRPTQKSVEN [Source organism chain B]=Medicago truncatula [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Medicago truncatula [Accession]=MF7000914 [Entry] [Entry number]=1099 [Entry name]=PC4 homolog BPSL1147 (Burkholderia pseudomallei K96243) [PDB ID]=5a4o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=PC4-like fold [Sequence domain]=Transcriptional Coactivator p15 (PC4) [Evidence level]=Direct evidence [Evidence text]=In PC4 fold dimers there is beta sheet augmentation as well as coiled coil formation by helices from the two different monomers. The interface is quite large and there are many inter-chain hydrogen bonds and salt bridges, most of them are formed by conserved residues (PMID:22948907, PMID:24029071). The guanidine hydrochloride induced unfolding of PC4 (monitored using fluorescence) was best fitted to a two-state model (PMID:34534740). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000282,MF7000281,MF7000915,MF7000353 [UniProt ID chain A]=Q63VU8 [UniProt boundaries chain A]=2-75 [UniProt coverage chain A]=98% [Name chain A]=Transcriptional coactivator p15 (PC4) C-terminal domain-containing protein [UniProt sequence chain A]=MSAYDSGKTIADVQKSATQRIRISHRWYRGRRYVDVRLVVVDRDGDFVPTRQGISIRPELLAQVIQGLLLASREG [Source organism chain A]=Burkholderia pseudomallei [UniProt ID chain B]=Q63VU8 [UniProt boundaries chain B]=2-75 [UniProt coverage chain B]=98% [Name chain B]=Transcriptional coactivator p15 (PC4) C-terminal domain-containing protein [UniProt sequence chain B]=MSAYDSGKTIADVQKSATQRIRISHRWYRGRRYVDVRLVVVDRDGDFVPTRQGISIRPELLAQVIQGLLLASREG [Source organism chain B]=Burkholderia pseudomallei [ExpTech]=X-ray [Resolution]=1.76 [Source organism]=Burkholderia pseudomallei [Accession]=MF7000915 [Entry] [Entry number]=1100 [Entry name]=Amphiphysin BAR domain (Drosophila) [PDB ID]=1uru [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=N-BAR domain [Sequence domain]=N-BAR domain [Evidence level]=Direct evidence [Evidence text]=The human AmphyphisinII/Bin1 and Endophilin BAR domains (N-BARs) display two-state equilibrium unfolding from the dimeric to unfolded monomeric forms (PMID:26368922, PMID:34423187). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000916,MF7000125,MF7000126,MF7000124 [UniProt ID chain A]=Q7KLE5 [UniProt boundaries chain A]=26-242 [UniProt coverage chain A]=36% [Name chain A]=Amphiphysin [UniProt sequence chain A]=MTENKGIMLAKSVQKHAGRAKEKILQNLGKVDRTADEIFDDHLNNFNRQQASANRLQKEFNNYIRCVRAAQAASKTLMDSVCEIYEPQWSGYDALQAQTGASESLWADFAHKLGDQVLIPLNTYTGQFPEMKKKVEKRNRKLIDYDGQRHSFQNLQANANKRKDDVKLTKGREQLEEARRTYEILNTELHDELPALYDSRILFLVTNLQTLFATEQVFHNETAKIYSELEAIVDKLATESQRGSNTLRKQTSNPIKTSSPVQSPVNKLNNANINSNYQNQITTNGGSSLANSPTSTSSSLQEPRFDSVSSTPEPRPESPAAALVSATPSSPVENGVTTKSLERPELSGLNASAKATTTTQTSPTEDKAVVSEAVKPSETEGAAVAASVTPAPPATPAQINGNNNEPSIVKEGGKQPKELPSTTSNAEAAAEAAANNGNSIEEHKQKKLGNDTTVTATETVTVTQHSVTSTDTDNIVTISDTNTDTDTKTSTGTSQKGRPVPVVNRHSVNNLNKNPFEDDDERIYEVPADANTADLPPGVLYRVKATYGYAKEDVDELSFEIGDLIRVIEYDDPEDQEEGWLMGQKEGTNEKGLFPANFTRPI [Source organism chain A]=Drosophila melanogaster [UniProt ID chain A-2]=Q7KLE5 [UniProt boundaries chain A-2]=26-242 [UniProt coverage chain A-2]=36% [Name chain A-2]=Amphiphysin [UniProt sequence chain A-2]=MTENKGIMLAKSVQKHAGRAKEKILQNLGKVDRTADEIFDDHLNNFNRQQASANRLQKEFNNYIRCVRAAQAASKTLMDSVCEIYEPQWSGYDALQAQTGASESLWADFAHKLGDQVLIPLNTYTGQFPEMKKKVEKRNRKLIDYDGQRHSFQNLQANANKRKDDVKLTKGREQLEEARRTYEILNTELHDELPALYDSRILFLVTNLQTLFATEQVFHNETAKIYSELEAIVDKLATESQRGSNTLRKQTSNPIKTSSPVQSPVNKLNNANINSNYQNQITTNGGSSLANSPTSTSSSLQEPRFDSVSSTPEPRPESPAAALVSATPSSPVENGVTTKSLERPELSGLNASAKATTTTQTSPTEDKAVVSEAVKPSETEGAAVAASVTPAPPATPAQINGNNNEPSIVKEGGKQPKELPSTTSNAEAAAEAAANNGNSIEEHKQKKLGNDTTVTATETVTVTQHSVTSTDTDNIVTISDTNTDTDTKTSTGTSQKGRPVPVVNRHSVNNLNKNPFEDDDERIYEVPADANTADLPPGVLYRVKATYGYAKEDVDELSFEIGDLIRVIEYDDPEDQEEGWLMGQKEGTNEKGLFPANFTRPI [Source organism chain A-2]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Drosophila melanogaster [Accession]=MF7000916 [Entry] [Entry number]=1101 [Entry name]=Cytoplasmic serine chemotaxis receptor [PDB ID]=1qu7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Methyl-accepting chemotaxis protein (MCP) signalling domain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:16622408). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000917,MF7000147,MF7000263,MF7000264 [UniProt ID chain A]=P02942 [UniProt boundaries chain A]=294-520 [UniProt coverage chain A]=41% [Name chain A]=Methyl-accepting chemotaxis protein I [UniProt sequence chain A]=MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P02942 [UniProt boundaries chain B]=300-520 [UniProt coverage chain B]=40% [Name chain B]=Methyl-accepting chemotaxis protein I [UniProt sequence chain B]=MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.60 [Source organism]=Escherichia coli [Accession]=MF7000917 [Entry] [Entry number]=1102 [Entry name]=N-terminal domain of MazE9 antitoxin (nMazE9) (Mycobacterium tuberculosis) [PDB ID]=8imh [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=Ribbon-helix-helix protein, copG family [Evidence level]=Direct evidence [Evidence text]=A thermal unfolding experiment showed no transition for MazE9 indicating disordered state of the protein (PMID:36275627). Also, the interacting chains form a ribbon-helix-helix (RHH) structure (PMID:37737533). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2120006,MF2120034,MF7000918 [UniProt ID chain A]=P0CL61 [UniProt boundaries chain A]=1-40 [UniProt coverage chain A]=52% [Name chain A]=Antitoxin MazE9 [UniProt sequence chain A]=MKLSVSLSDDDVAILDAYVKRAGLPSRSAGLQHAIRVLRYPTLEDDYANAWQEWSAAGDTDAWEQTVGDGVGDAPR [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P0CL61 [UniProt boundaries chain B]=1-40 [UniProt coverage chain B]=52% [Name chain B]=Antitoxin MazE9 [UniProt sequence chain B]=MKLSVSLSDDDVAILDAYVKRAGLPSRSAGLQHAIRVLRYPTLEDDYANAWQEWSAAGDTDAWEQTVGDGVGDAPR [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000918 [Entry] [Entry number]=1103 [Entry name]=Multifunctional protein VP3 of Birnaviruses [PDB ID]=2r18 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Capsid proteins [Sequence domain]=Birnavirus VP3 protein [Evidence level]=Direct evidence [Evidence text]=Multidomain viral capsid VP3 protein with an all-helical dimerization domain. Within the dimerization domain the three helices of the monomers tightly interact with eachother (dimer resembles entwined U’s) with large, hydrophobic interafce. Hydrophobic core assembled from the two monomers (PMID:33239452). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000919,MF7000920,MF7000921 [UniProt ID chain A]=P25220 [UniProt boundaries chain A]=827-955 [UniProt coverage chain A]=12% [Name chain A]=Structural polyprotein [UniProt sequence chain A]=MPTTGPASIPDDTLEKHTLRSETSTYNLTVGDTGSGLIVFFPGFPGSIVGAHYTLQSNGNYKFDQMLLTAQNLPASYNYCRLVSRSLTVRSSTLPGGVYALNGTINAVTFQGSLSELTDVSYNGLMSATANINDKIGNVLVGEGVTVLSLPTSYDLGYVRLGDPIPAIGLDPKMVATCDSSDRPRVYTITAADDYQFSSQYQPGGVTITLFSANIDAITSLSVGGELVFRTSVHGLVLGATIYLIGFDGTTVITRAVAANTGLTTGTDNLMPFNLVIPTNEITQPITSIKLEIVTSKSGGQAGDQMLWSARGSLAVTIHGGNYPGALRPVTLVAYERVATGSVVTVAGVSNFELIPNPELAKNLVTEYGRFDPGAMNYTKLILSERDRLGIKTVWPTREYTDFREYFMEVADLNSPLKIAGAFGFKDIIRAIRRIAVPVVSTLFPPAAPLAHAIGEGVDYLLGDEAQAASGTARAASGKARAASGRIRQLTLAADKGYEVVANLFQVPQNPVVDGILASPGVLRGAHNLDCVLREGATLFPVVITTVEDAMTPKALNSKMFAVIEGVREDLQPPSQRGSFIRTLSGHRVYGYAPDGVLPLETGRDYTVVPIDDVWDDSIMLSKDPIPPIVGNSGNLAIAYMDVFRPKVPIHVAMTGALNACGEIEKVSFRSTKLATAHRLGLKLAGPGAFDVNTGPNWATFIKRFPHNPRDWDRLPYLNLPYLPPNAGRQYHLAMAASEFKETPELESAVRAMEAAANVDPLFQSALSVFMWLEENGIVTDMANFALSDPNAHRMRNFLANAPQAGSKSQRAKYGTAGYGVEARGPTPEEAQREKDTRISKKMETMGIYFATPEWVALNGHRGPSPGQLKYWQNTREIPDPNEDYLDYVHAEKSRLASEEQILRAATSIYGAPGQAEPPQAFIDEVAKVYEINHGRGPNQEQMKDLLLTAMEMKHRNPRRALPKPKPKPNAPTQRPPGRLGRWIRTVSDEDLE [Source organism chain A]=disease virus) [UniProt ID chain A-2]=P25220 [UniProt boundaries chain A-2]=827-955 [UniProt coverage chain A-2]=12% [Name chain A-2]=Structural polyprotein [UniProt sequence chain A-2]=MPTTGPASIPDDTLEKHTLRSETSTYNLTVGDTGSGLIVFFPGFPGSIVGAHYTLQSNGNYKFDQMLLTAQNLPASYNYCRLVSRSLTVRSSTLPGGVYALNGTINAVTFQGSLSELTDVSYNGLMSATANINDKIGNVLVGEGVTVLSLPTSYDLGYVRLGDPIPAIGLDPKMVATCDSSDRPRVYTITAADDYQFSSQYQPGGVTITLFSANIDAITSLSVGGELVFRTSVHGLVLGATIYLIGFDGTTVITRAVAANTGLTTGTDNLMPFNLVIPTNEITQPITSIKLEIVTSKSGGQAGDQMLWSARGSLAVTIHGGNYPGALRPVTLVAYERVATGSVVTVAGVSNFELIPNPELAKNLVTEYGRFDPGAMNYTKLILSERDRLGIKTVWPTREYTDFREYFMEVADLNSPLKIAGAFGFKDIIRAIRRIAVPVVSTLFPPAAPLAHAIGEGVDYLLGDEAQAASGTARAASGKARAASGRIRQLTLAADKGYEVVANLFQVPQNPVVDGILASPGVLRGAHNLDCVLREGATLFPVVITTVEDAMTPKALNSKMFAVIEGVREDLQPPSQRGSFIRTLSGHRVYGYAPDGVLPLETGRDYTVVPIDDVWDDSIMLSKDPIPPIVGNSGNLAIAYMDVFRPKVPIHVAMTGALNACGEIEKVSFRSTKLATAHRLGLKLAGPGAFDVNTGPNWATFIKRFPHNPRDWDRLPYLNLPYLPPNAGRQYHLAMAASEFKETPELESAVRAMEAAANVDPLFQSALSVFMWLEENGIVTDMANFALSDPNAHRMRNFLANAPQAGSKSQRAKYGTAGYGVEARGPTPEEAQREKDTRISKKMETMGIYFATPEWVALNGHRGPSPGQLKYWQNTREIPDPNEDYLDYVHAEKSRLASEEQILRAATSIYGAPGQAEPPQAFIDEVAKVYEINHGRGPNQEQMKDLLLTAMEMKHRNPRRALPKPKPKPNAPTQRPPGRLGRWIRTVSDEDLE [Source organism chain A-2]=disease virus) [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=disease virus) [Accession]=MF7000919 [Entry] [Entry number]=1104 [Entry name]=N-terminal domain of Drosophila X Virus VP3 [PDB ID]=6shw [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Capsid proteins [Sequence domain]=Birnavirus VP3 protein [Evidence level]=Direct evidence [Evidence text]=Three helices in the monomers that are tightly interacting with eachother (dimer resembles entwined U’s) with large, hydrophobic interafce. Hydrophobic core assembled from the two monomers (PMID:33239452). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000919,MF7000920,MF7000921 [UniProt ID chain A]=Q96724 [UniProt boundaries chain A]=766-813 [UniProt coverage chain A]=4% [Name chain A]=Structural polyprotein [UniProt sequence chain A]=MNTTNEYLKTLLNPAQFISDIPDDIMIRHVNSAQTITYNLKSGASGTGLIVVYPNTPSSISGFHYIWDSATSNWVFDQYIYTAQELKDSYDYGRLISGSLSIKSSTLPAGVYALNGTFNAVWFQGTLSEVSDYSYDRILSITSNPLDKVGNVLVGDGIEVLSLPQGFNNPYVRLGDKSPSTLSSPTHITNTSQNLATGGAYMIPVTTVPGQGFHNKEFSINVDSVGPVDILWSGQMTMQDEWTVTANYQPLNISGTLIANSQRTLTWSNTGVSNGSHYMNMNNLNVSLFHENPPPEPVAAIKININYGNNTNGDSSFSVDSSFTINVIGGATIGVNSPTVGVGYQGVAEGTAITISGINNYELVPNPDLQKNLPMTYGTCDPHDLTYIKYILSNREQLGLRSVMTLADYNRMKMYMHVLTNYHVDEREASSFDFWQLLKQIKNVAVPLAATLAPQFAPIIGAADGLANAILGDSASGRPVGNSASGMPISMSRRLRNAYSADSPLGEEHWLPNENENFNKFDIIYDVSHSSMALFPVIMMEHDKVIPSDPEELYIAVSLTESLRKQIPNLNDMPYYEMGGHRVYNSVSSNVRSGNFLRSDYILLPCYQLLEGRLASSTSPNKVTGTSHQLAIYAADDLLKSGVLGKAPFAAFTGSVVGSSVGEVFGINLKLQLTDSLGIPLLGNSPGLVQVKTLTSLDKKIKDMGDVKRRTPKQTLPHWTAGSASMNPFMNTNPFLEELDQPIPSNAAKPISEETRDLFLSDGQTIPSSQEKIATIHEYLLEHKELEEAMFSLISQGRGRSLINMVVKSALNIETQSREVTGERRQRLERKLRNLENQGIYVDESKIMSRGRISKEDTELAMRIARKNQKDAKLRRIYSNNASIQESYTVDDFVSYWMEQESLPTGIQIAMWLKGDDWSQPIPPRVQRRHYDSYIMMLGPSPTQEQADAVKDLVDDIYDRNQGKGPSQEQARELSHAVRRLISHSLVNQPATAPRVPPRRIVSAQTAQTDPPGRRAALDRLRRVRGEDNDIV [Source organism chain A]=Drosophila x virus [UniProt ID chain A-2]=Q96724 [UniProt boundaries chain A-2]=766-813 [UniProt coverage chain A-2]=4% [Name chain A-2]=Structural polyprotein [UniProt sequence chain A-2]=MNTTNEYLKTLLNPAQFISDIPDDIMIRHVNSAQTITYNLKSGASGTGLIVVYPNTPSSISGFHYIWDSATSNWVFDQYIYTAQELKDSYDYGRLISGSLSIKSSTLPAGVYALNGTFNAVWFQGTLSEVSDYSYDRILSITSNPLDKVGNVLVGDGIEVLSLPQGFNNPYVRLGDKSPSTLSSPTHITNTSQNLATGGAYMIPVTTVPGQGFHNKEFSINVDSVGPVDILWSGQMTMQDEWTVTANYQPLNISGTLIANSQRTLTWSNTGVSNGSHYMNMNNLNVSLFHENPPPEPVAAIKININYGNNTNGDSSFSVDSSFTINVIGGATIGVNSPTVGVGYQGVAEGTAITISGINNYELVPNPDLQKNLPMTYGTCDPHDLTYIKYILSNREQLGLRSVMTLADYNRMKMYMHVLTNYHVDEREASSFDFWQLLKQIKNVAVPLAATLAPQFAPIIGAADGLANAILGDSASGRPVGNSASGMPISMSRRLRNAYSADSPLGEEHWLPNENENFNKFDIIYDVSHSSMALFPVIMMEHDKVIPSDPEELYIAVSLTESLRKQIPNLNDMPYYEMGGHRVYNSVSSNVRSGNFLRSDYILLPCYQLLEGRLASSTSPNKVTGTSHQLAIYAADDLLKSGVLGKAPFAAFTGSVVGSSVGEVFGINLKLQLTDSLGIPLLGNSPGLVQVKTLTSLDKKIKDMGDVKRRTPKQTLPHWTAGSASMNPFMNTNPFLEELDQPIPSNAAKPISEETRDLFLSDGQTIPSSQEKIATIHEYLLEHKELEEAMFSLISQGRGRSLINMVVKSALNIETQSREVTGERRQRLERKLRNLENQGIYVDESKIMSRGRISKEDTELAMRIARKNQKDAKLRRIYSNNASIQESYTVDDFVSYWMEQESLPTGIQIAMWLKGDDWSQPIPPRVQRRHYDSYIMMLGPSPTQEQADAVKDLVDDIYDRNQGKGPSQEQARELSHAVRRLISHSLVNQPATAPRVPPRRIVSAQTAQTDPPGRRAALDRLRRVRGEDNDIV [Source organism chain A-2]=Drosophila x virus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Drosophila x virus [Accession]=MF7000920 [Entry] [Entry number]=1105 [Entry name]=N-terminal domain of Drosophila X virus VP3 [PDB ID]=6si6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Capsid proteins [Sequence domain]=Birnavirus VP3 protein [Evidence level]=Direct evidence [Evidence text]=Three helices in the monomers that are tightly interacting with eachother (dimer resembles entwined U’s) with large, hydrophobic interafce. Hydrophobic core assembled from the two monomers (PMID:33239452). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000919,MF7000920,MF7000921 [UniProt ID chain A]=Q96724 [UniProt boundaries chain A]=767-813 [UniProt coverage chain A]=4% [Name chain A]=Structural polyprotein [UniProt sequence chain A]=MNTTNEYLKTLLNPAQFISDIPDDIMIRHVNSAQTITYNLKSGASGTGLIVVYPNTPSSISGFHYIWDSATSNWVFDQYIYTAQELKDSYDYGRLISGSLSIKSSTLPAGVYALNGTFNAVWFQGTLSEVSDYSYDRILSITSNPLDKVGNVLVGDGIEVLSLPQGFNNPYVRLGDKSPSTLSSPTHITNTSQNLATGGAYMIPVTTVPGQGFHNKEFSINVDSVGPVDILWSGQMTMQDEWTVTANYQPLNISGTLIANSQRTLTWSNTGVSNGSHYMNMNNLNVSLFHENPPPEPVAAIKININYGNNTNGDSSFSVDSSFTINVIGGATIGVNSPTVGVGYQGVAEGTAITISGINNYELVPNPDLQKNLPMTYGTCDPHDLTYIKYILSNREQLGLRSVMTLADYNRMKMYMHVLTNYHVDEREASSFDFWQLLKQIKNVAVPLAATLAPQFAPIIGAADGLANAILGDSASGRPVGNSASGMPISMSRRLRNAYSADSPLGEEHWLPNENENFNKFDIIYDVSHSSMALFPVIMMEHDKVIPSDPEELYIAVSLTESLRKQIPNLNDMPYYEMGGHRVYNSVSSNVRSGNFLRSDYILLPCYQLLEGRLASSTSPNKVTGTSHQLAIYAADDLLKSGVLGKAPFAAFTGSVVGSSVGEVFGINLKLQLTDSLGIPLLGNSPGLVQVKTLTSLDKKIKDMGDVKRRTPKQTLPHWTAGSASMNPFMNTNPFLEELDQPIPSNAAKPISEETRDLFLSDGQTIPSSQEKIATIHEYLLEHKELEEAMFSLISQGRGRSLINMVVKSALNIETQSREVTGERRQRLERKLRNLENQGIYVDESKIMSRGRISKEDTELAMRIARKNQKDAKLRRIYSNNASIQESYTVDDFVSYWMEQESLPTGIQIAMWLKGDDWSQPIPPRVQRRHYDSYIMMLGPSPTQEQADAVKDLVDDIYDRNQGKGPSQEQARELSHAVRRLISHSLVNQPATAPRVPPRRIVSAQTAQTDPPGRRAALDRLRRVRGEDNDIV [Source organism chain A]=Drosophila x virus [UniProt ID chain B]=Q96724 [UniProt boundaries chain B]=765-815 [UniProt coverage chain B]=4% [Name chain B]=Structural polyprotein [UniProt sequence chain B]=MNTTNEYLKTLLNPAQFISDIPDDIMIRHVNSAQTITYNLKSGASGTGLIVVYPNTPSSISGFHYIWDSATSNWVFDQYIYTAQELKDSYDYGRLISGSLSIKSSTLPAGVYALNGTFNAVWFQGTLSEVSDYSYDRILSITSNPLDKVGNVLVGDGIEVLSLPQGFNNPYVRLGDKSPSTLSSPTHITNTSQNLATGGAYMIPVTTVPGQGFHNKEFSINVDSVGPVDILWSGQMTMQDEWTVTANYQPLNISGTLIANSQRTLTWSNTGVSNGSHYMNMNNLNVSLFHENPPPEPVAAIKININYGNNTNGDSSFSVDSSFTINVIGGATIGVNSPTVGVGYQGVAEGTAITISGINNYELVPNPDLQKNLPMTYGTCDPHDLTYIKYILSNREQLGLRSVMTLADYNRMKMYMHVLTNYHVDEREASSFDFWQLLKQIKNVAVPLAATLAPQFAPIIGAADGLANAILGDSASGRPVGNSASGMPISMSRRLRNAYSADSPLGEEHWLPNENENFNKFDIIYDVSHSSMALFPVIMMEHDKVIPSDPEELYIAVSLTESLRKQIPNLNDMPYYEMGGHRVYNSVSSNVRSGNFLRSDYILLPCYQLLEGRLASSTSPNKVTGTSHQLAIYAADDLLKSGVLGKAPFAAFTGSVVGSSVGEVFGINLKLQLTDSLGIPLLGNSPGLVQVKTLTSLDKKIKDMGDVKRRTPKQTLPHWTAGSASMNPFMNTNPFLEELDQPIPSNAAKPISEETRDLFLSDGQTIPSSQEKIATIHEYLLEHKELEEAMFSLISQGRGRSLINMVVKSALNIETQSREVTGERRQRLERKLRNLENQGIYVDESKIMSRGRISKEDTELAMRIARKNQKDAKLRRIYSNNASIQESYTVDDFVSYWMEQESLPTGIQIAMWLKGDDWSQPIPPRVQRRHYDSYIMMLGPSPTQEQADAVKDLVDDIYDRNQGKGPSQEQARELSHAVRRLISHSLVNQPATAPRVPPRRIVSAQTAQTDPPGRRAALDRLRRVRGEDNDIV [Source organism chain B]=Drosophila x virus [ExpTech]=X-ray [Resolution]=1.98 [Source organism]=Drosophila x virus [Accession]=MF7000921 [Entry] [Entry number]=1106 [Entry name]=Poly-HAMP domains from the P. aeruginosa soluble receptor Aer2 [PDB ID]=3lnr [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=HAMP-type four helix bundle domain [Sequence domain]=Methyl-accepting chemotaxis protein McpB, HAMP domains [Evidence level]=Indirect evidence [Evidence text]=Aer2 1–172 is a symmetric dimer containing three HAMP domains. The basic construction unit of each HAMP domain is a monomeric unit of two parallel α-helices joined by a linker. This unit dimerizes and coils around a central supercoil axis to form a parallel four-helix bundle. The second and third HAMP domains are concatenated to form an interwoven di-HAMP structure (PMID:20399181). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000922,MF7000923,MF7000924 [UniProt ID chain A]=Q9I6V6 [UniProt boundaries chain A]=1-157 [UniProt coverage chain A]=23% [Name chain A]=Methyl-accepting chemotaxis protein McpB [UniProt sequence chain A]=MGLFNAHAVAQQRADRIATLLQSFADGQLDTAVGEAPAPGYERLYDSLRALQRQLREQRAELQQVESLEAGLAEMSRQHEAGWIDQTIPAERLEGRAARIAKGVNELVAAHIAVKMKVVSVVTAYGQGNFEPLMDRLPGKKAQITEAIDGVRERLRGAAEATSAQLATAAYNARIKSALDNVSANVMIADNDLNIIYMNRTVSEMLGRAEADIRKQLPNFDAGRLMGANIDVFHKNPAHQRHLLANLTGVHKAELNLGGRRFSLDVVPVFNDANERLGSAVQWTDRTEEHRAEQEVSQLVQAAAAGDFSKRVEEAGKEGFFLRLAKDLNSLVDTADRGLRDVSRMLGALAQGDLTQRIEADYQGTFGQLKDFSNDTAQSLSRMLGQIREAADTINTAASEIASGNAELSARTEQQASSLEETASSMEELTSTVKLNAENARQANSLAANASEVATQGGTVVQKVVSTMSSINESARKIADIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLAQRSAAAAKEIKTLISDSVDKVENGNTLVAQAGQTMSDIVVAIRRVTDIMSEIAAASAEQSTGIEEVNSAVSQMDDMTQQNAALVEEAAAAAEAMQEQAGLLNQSVAVFRLDTPPSVVQLASARPSAPRPSAPAPLARSGMARASKARKEDGWEEF [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain A-2]=Q9I6V6 [UniProt boundaries chain A-2]=1-157 [UniProt coverage chain A-2]=23% [Name chain A-2]=Methyl-accepting chemotaxis protein McpB [UniProt sequence chain A-2]=MGLFNAHAVAQQRADRIATLLQSFADGQLDTAVGEAPAPGYERLYDSLRALQRQLREQRAELQQVESLEAGLAEMSRQHEAGWIDQTIPAERLEGRAARIAKGVNELVAAHIAVKMKVVSVVTAYGQGNFEPLMDRLPGKKAQITEAIDGVRERLRGAAEATSAQLATAAYNARIKSALDNVSANVMIADNDLNIIYMNRTVSEMLGRAEADIRKQLPNFDAGRLMGANIDVFHKNPAHQRHLLANLTGVHKAELNLGGRRFSLDVVPVFNDANERLGSAVQWTDRTEEHRAEQEVSQLVQAAAAGDFSKRVEEAGKEGFFLRLAKDLNSLVDTADRGLRDVSRMLGALAQGDLTQRIEADYQGTFGQLKDFSNDTAQSLSRMLGQIREAADTINTAASEIASGNAELSARTEQQASSLEETASSMEELTSTVKLNAENARQANSLAANASEVATQGGTVVQKVVSTMSSINESARKIADIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLAQRSAAAAKEIKTLISDSVDKVENGNTLVAQAGQTMSDIVVAIRRVTDIMSEIAAASAEQSTGIEEVNSAVSQMDDMTQQNAALVEEAAAAAEAMQEQAGLLNQSVAVFRLDTPPSVVQLASARPSAPRPSAPAPLARSGMARASKARKEDGWEEF [Source organism chain A-2]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.64 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000922 [Entry] [Entry number]=1107 [Entry name]=Aer2 poly-HAMP domains: L44H HAMP1 CW-lock mutant [PDB ID]=4i3m [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=HAMP-type four helix bundle domain [Sequence domain]=Methyl-accepting chemotaxis protein McpB, HAMP domains [Evidence level]=Indirect evidence [Evidence text]=Aer2 1–172 is a symmetric dimer containing three HAMP domains. The basic construction unit of each HAMP domain is a monomeric unit of two parallel α-helices joined by a linker. This unit dimerizes and coils around a central supercoil axis to form a parallel four-helix bundle. The second and third HAMP domains are concatenated to form an interwoven di-HAMP structure (PMID:20399181). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000922,MF7000923,MF7000924 [UniProt ID chain A]=Q9I6V6 [UniProt boundaries chain A]=7-156 [UniProt coverage chain A]=22% [Name chain A]=Methyl-accepting chemotaxis protein McpB [UniProt sequence chain A]=MGLFNAHAVAQQRADRIATLLQSFADGQLDTAVGEAPAPGYERLYDSLRALQRQLREQRAELQQVESLEAGLAEMSRQHEAGWIDQTIPAERLEGRAARIAKGVNELVAAHIAVKMKVVSVVTAYGQGNFEPLMDRLPGKKAQITEAIDGVRERLRGAAEATSAQLATAAYNARIKSALDNVSANVMIADNDLNIIYMNRTVSEMLGRAEADIRKQLPNFDAGRLMGANIDVFHKNPAHQRHLLANLTGVHKAELNLGGRRFSLDVVPVFNDANERLGSAVQWTDRTEEHRAEQEVSQLVQAAAAGDFSKRVEEAGKEGFFLRLAKDLNSLVDTADRGLRDVSRMLGALAQGDLTQRIEADYQGTFGQLKDFSNDTAQSLSRMLGQIREAADTINTAASEIASGNAELSARTEQQASSLEETASSMEELTSTVKLNAENARQANSLAANASEVATQGGTVVQKVVSTMSSINESARKIADIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLAQRSAAAAKEIKTLISDSVDKVENGNTLVAQAGQTMSDIVVAIRRVTDIMSEIAAASAEQSTGIEEVNSAVSQMDDMTQQNAALVEEAAAAAEAMQEQAGLLNQSVAVFRLDTPPSVVQLASARPSAPRPSAPAPLARSGMARASKARKEDGWEEF [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain A-2]=Q9I6V6 [UniProt boundaries chain A-2]=7-156 [UniProt coverage chain A-2]=22% [Name chain A-2]=Methyl-accepting chemotaxis protein McpB [UniProt sequence chain A-2]=MGLFNAHAVAQQRADRIATLLQSFADGQLDTAVGEAPAPGYERLYDSLRALQRQLREQRAELQQVESLEAGLAEMSRQHEAGWIDQTIPAERLEGRAARIAKGVNELVAAHIAVKMKVVSVVTAYGQGNFEPLMDRLPGKKAQITEAIDGVRERLRGAAEATSAQLATAAYNARIKSALDNVSANVMIADNDLNIIYMNRTVSEMLGRAEADIRKQLPNFDAGRLMGANIDVFHKNPAHQRHLLANLTGVHKAELNLGGRRFSLDVVPVFNDANERLGSAVQWTDRTEEHRAEQEVSQLVQAAAAGDFSKRVEEAGKEGFFLRLAKDLNSLVDTADRGLRDVSRMLGALAQGDLTQRIEADYQGTFGQLKDFSNDTAQSLSRMLGQIREAADTINTAASEIASGNAELSARTEQQASSLEETASSMEELTSTVKLNAENARQANSLAANASEVATQGGTVVQKVVSTMSSINESARKIADIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLAQRSAAAAKEIKTLISDSVDKVENGNTLVAQAGQTMSDIVVAIRRVTDIMSEIAAASAEQSTGIEEVNSAVSQMDDMTQQNAALVEEAAAAAEAMQEQAGLLNQSVAVFRLDTPPSVVQLASARPSAPRPSAPAPLARSGMARASKARKEDGWEEF [Source organism chain A-2]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=1.95 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000923 [Entry] [Entry number]=1108 [Entry name]=Aer2 poly-HAMP domains: V33G HAMP1 inverted signaling mutant [PDB ID]=4i44 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=HAMP-type four helix bundle domain [Sequence domain]=Methyl-accepting chemotaxis protein McpB, HAMP domains [Evidence level]=Indirect evidence [Evidence text]=Aer2 1–172 is a symmetric dimer containing three HAMP domains. The basic construction unit of each HAMP domain is a monomeric unit of two parallel α-helices joined by a linker. This unit dimerizes and coils around a central supercoil axis to form a parallel four-helix bundle. The second and third HAMP domains are concatenated to form an interwoven di-HAMP structure (PMID:20399181). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000922,MF7000923,MF7000924 [UniProt ID chain A]=Q9I6V6 [UniProt boundaries chain A]=1-157 [UniProt coverage chain A]=23% [Name chain A]=Methyl-accepting chemotaxis protein McpB [UniProt sequence chain A]=MGLFNAHAVAQQRADRIATLLQSFADGQLDTAVGEAPAPGYERLYDSLRALQRQLREQRAELQQVESLEAGLAEMSRQHEAGWIDQTIPAERLEGRAARIAKGVNELVAAHIAVKMKVVSVVTAYGQGNFEPLMDRLPGKKAQITEAIDGVRERLRGAAEATSAQLATAAYNARIKSALDNVSANVMIADNDLNIIYMNRTVSEMLGRAEADIRKQLPNFDAGRLMGANIDVFHKNPAHQRHLLANLTGVHKAELNLGGRRFSLDVVPVFNDANERLGSAVQWTDRTEEHRAEQEVSQLVQAAAAGDFSKRVEEAGKEGFFLRLAKDLNSLVDTADRGLRDVSRMLGALAQGDLTQRIEADYQGTFGQLKDFSNDTAQSLSRMLGQIREAADTINTAASEIASGNAELSARTEQQASSLEETASSMEELTSTVKLNAENARQANSLAANASEVATQGGTVVQKVVSTMSSINESARKIADIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLAQRSAAAAKEIKTLISDSVDKVENGNTLVAQAGQTMSDIVVAIRRVTDIMSEIAAASAEQSTGIEEVNSAVSQMDDMTQQNAALVEEAAAAAEAMQEQAGLLNQSVAVFRLDTPPSVVQLASARPSAPRPSAPAPLARSGMARASKARKEDGWEEF [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain A-2]=Q9I6V6 [UniProt boundaries chain A-2]=1-157 [UniProt coverage chain A-2]=23% [Name chain A-2]=Methyl-accepting chemotaxis protein McpB [UniProt sequence chain A-2]=MGLFNAHAVAQQRADRIATLLQSFADGQLDTAVGEAPAPGYERLYDSLRALQRQLREQRAELQQVESLEAGLAEMSRQHEAGWIDQTIPAERLEGRAARIAKGVNELVAAHIAVKMKVVSVVTAYGQGNFEPLMDRLPGKKAQITEAIDGVRERLRGAAEATSAQLATAAYNARIKSALDNVSANVMIADNDLNIIYMNRTVSEMLGRAEADIRKQLPNFDAGRLMGANIDVFHKNPAHQRHLLANLTGVHKAELNLGGRRFSLDVVPVFNDANERLGSAVQWTDRTEEHRAEQEVSQLVQAAAAGDFSKRVEEAGKEGFFLRLAKDLNSLVDTADRGLRDVSRMLGALAQGDLTQRIEADYQGTFGQLKDFSNDTAQSLSRMLGQIREAADTINTAASEIASGNAELSARTEQQASSLEETASSMEELTSTVKLNAENARQANSLAANASEVATQGGTVVQKVVSTMSSINESARKIADIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLAQRSAAAAKEIKTLISDSVDKVENGNTLVAQAGQTMSDIVVAIRRVTDIMSEIAAASAEQSTGIEEVNSAVSQMDDMTQQNAALVEEAAAAAEAMQEQAGLLNQSVAVFRLDTPPSVVQLASARPSAPRPSAPAPLARSGMARASKARKEDGWEEF [Source organism chain A-2]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.88 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000924 [Entry] [Entry number]=1109 [Entry name]=6xhis-tagged phi3T_93 protein [PDB ID]=8ant [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=phi3T_93 [Evidence level]=No contradicting information [Evidence text]=The α1 helices of two phi3T_93 monomers interact, resulting in a W-shaped tight and globular dimer. Size exclusion chromatography coupled to multi-angle light scattering (SEC–MALS) analysis confirmed the dimeric organization of phi3T_93 in solution (PMID:38177302). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000925,MF7000926,MF7000927 [UniProt ID chain A]=A0A1P8CWW1 [UniProt boundaries chain A]=1-68 [UniProt coverage chain A]=83% [Name chain A]=Uncharacterized protein [UniProt sequence chain A]=MTNNKYYTEENKKKVWKKHMIVLKFLEQPGISEAYLNYLQEEIHNDEWIGFENEFFEELTGKPVINVGDKIKATKQYSAVH [Source organism chain A]=Bacillus phage phi3T [UniProt ID chain B]=A0A1P8CWW1 [UniProt boundaries chain B]=1-69 [UniProt coverage chain B]=85% [Name chain B]=Uncharacterized protein [UniProt sequence chain B]=MTNNKYYTEENKKKVWKKHMIVLKFLEQPGISEAYLNYLQEEIHNDEWIGFENEFFEELTGKPVINVGDKIKATKQYSAVH [Source organism chain B]=Bacillus phage phi3T [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Bacillus phage phi3T [Accession]=MF7000925 [Entry] [Entry number]=1110 [Entry name]=phi3T_93 protein L23D mutant [PDB ID]=8c8e [Chains]=C,A [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=phi3T_93 [Evidence level]=No contradicting information [Evidence text]=The α1 helices of two phi3T_93 monomers interact, resulting in a W-shaped tight and globular dimer. Size exclusion chromatography coupled to multi-angle light scattering (SEC–MALS) analysis confirmed the dimeric organization of phi3T_93 in solution (PMID:38177302). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000925,MF7000926,MF7000927 [UniProt ID chain C]=A0A1P8CWW1 [UniProt boundaries chain C]=1-67 [UniProt coverage chain C]=82% [Name chain C]=Uncharacterized protein [UniProt sequence chain C]=MTNNKYYTEENKKKVWKKHMIVLKFLEQPGISEAYLNYLQEEIHNDEWIGFENEFFEELTGKPVINVGDKIKATKQYSAVH [Source organism chain C]=Bacillus phage phi3T [UniProt ID chain A]=A0A1P8CWW1 [UniProt boundaries chain A]=1-67 [UniProt coverage chain A]=82% [Name chain A]=Uncharacterized protein [UniProt sequence chain A]=MTNNKYYTEENKKKVWKKHMIVLKFLEQPGISEAYLNYLQEEIHNDEWIGFENEFFEELTGKPVINVGDKIKATKQYSAVH [Source organism chain A]=Bacillus phage phi3T [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Bacillus phage phi3T [Accession]=MF7000926 [Entry] [Entry number]=1111 [Entry name]=phi3T-93 protein [PDB ID]=8anu [Chains]=C,A [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=phi3T_93 [Evidence level]=No contradicting information [Evidence text]=The α1 helices of two phi3T_93 monomers interact, resulting in a W-shaped tight and globular dimer. Size exclusion chromatography coupled to multi-angle light scattering (SEC–MALS) analysis confirmed the dimeric organization of phi3T_93 in solution (PMID:38177302). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000925,MF7000926,MF7000927 [UniProt ID chain C]=A0A1P8CWW1 [UniProt boundaries chain C]=1-67 [UniProt coverage chain C]=82% [Name chain C]=Uncharacterized protein [UniProt sequence chain C]=MTNNKYYTEENKKKVWKKHMIVLKFLEQPGISEAYLNYLQEEIHNDEWIGFENEFFEELTGKPVINVGDKIKATKQYSAVH [Source organism chain C]=Bacillus phage phi3T [UniProt ID chain A]=A0A1P8CWW1 [UniProt boundaries chain A]=1-68 [UniProt coverage chain A]=83% [Name chain A]=Uncharacterized protein [UniProt sequence chain A]=MTNNKYYTEENKKKVWKKHMIVLKFLEQPGISEAYLNYLQEEIHNDEWIGFENEFFEELTGKPVINVGDKIKATKQYSAVH [Source organism chain A]=Bacillus phage phi3T [ExpTech]=X-ray [Resolution]=2.31 [Source organism]=Bacillus phage phi3T [Accession]=MF7000927 [Entry] [Entry number]=1112 [Entry name]=GBS1074, an Esat-6 homologue from Streptococcus [PDB ID]=3o9o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Proteins of 100 residues with WXG [Evidence level]=Direct evidence [Evidence text]=Predicted coiled coil and validated disordered segments make up more than 50% of the structure. Antiparallel coiled-coil monomers form a four-helix bundle. Coiled coils are highly versatile folding units (PMID:11166216) showing cooperative binding and folding (PMID:9811815). The well-defined core of the CFP-10·ESAT-6 complex consists of two similar helix–turn–helix hairpin structures formed from the individual proteins, which have an extensive hydrophobic contact surface and lie antiparallel to each other to form a four-helix bundle (PMID:15973432). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000120,MF7000928,MF7000929 [UniProt ID chain A]=Q8E5F8 [UniProt boundaries chain A]=4-95 [UniProt coverage chain A]=95% [Name chain A]=ESAT-6-like protein [UniProt sequence chain A]=MAQIKLTPEELRSSAQKYTAGSQQVTEVLNLLTQEQAVIDENWDGSTFDSFEAQFNELSPKITEFAQLLEDINQQLLKVADIIEQTDADIASQISG [Source organism chain A]=Streptococcus agalactiae serotype III [UniProt ID chain B]=Q8E5F8 [UniProt boundaries chain B]=1-95 [UniProt coverage chain B]=98% [Name chain B]=ESAT-6-like protein [UniProt sequence chain B]=MAQIKLTPEELRSSAQKYTAGSQQVTEVLNLLTQEQAVIDENWDGSTFDSFEAQFNELSPKITEFAQLLEDINQQLLKVADIIEQTDADIASQISG [Source organism chain B]=Streptococcus agalactiae serotype III [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Streptococcus agalactiae serotype III [Accession]=MF7000928 [Entry] [Entry number]=1113 [Entry name]=Homodimeric WXG-100 family protein from Streptococcus agalactiae [PDB ID]=3gwk [Chains]=C,E [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Proteins of 100 residues with WXG [Evidence level]=Direct evidence [Evidence text]=Antiparallel coiled-coil monomers form a four-helix bundle. Thermal denaturation circular dichroism curve looked two state, but no fitting was carried out (PMID:24586681). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain C]=N/A [Evidence chain E]=N/A [Similar structures]=MF7000120,MF7000928,MF7000929 [UniProt ID chain C]=Q8DZR0 [UniProt boundaries chain C]=3-96 [UniProt coverage chain C]=97% [Name chain C]=ESAT-6-like protein SAG1039 [UniProt sequence chain C]=MAQIKLTPEELRSSAQKYTAGSQQVTEVLNLLTQEQAVIDENWDGSTFDSFEAQFNELSPKITEFAQLLEDINQQLLKVADIIEQTDADIASQISG [Source organism chain C]=Streptococcus agalactiae serotype V [UniProt ID chain E]=Q8DZR0 [UniProt boundaries chain E]=3-96 [UniProt coverage chain E]=97% [Name chain E]=ESAT-6-like protein SAG1039 [UniProt sequence chain E]=MAQIKLTPEELRSSAQKYTAGSQQVTEVLNLLTQEQAVIDENWDGSTFDSFEAQFNELSPKITEFAQLLEDINQQLLKVADIIEQTDADIASQISG [Source organism chain E]=Streptococcus agalactiae serotype V [ExpTech]=X-ray [Resolution]=1.30 [Source organism]=Streptococcus agalactiae serotype V [Accession]=MF7000929 [Entry] [Entry number]=1114 [Entry name]=ChsB1 in complex with NAD+ [PDB ID]=7lgb [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Short chain dehydrogenase [Evidence level]=No contradicting information [Evidence text]=There is a knot-like interface between individual monomers. The structure looks like a domain-swapped Rossmann fold unit. The two largest helices, α7 and α9, which are parallel, form the majority of the dimer interface. Analytical ultracentrifugation sedimentation velocity analysis suggests homodimeric structure (PMID:33826843). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000930,MF7000931 [UniProt ID chain A]=O53547 [UniProt boundaries chain A]=16-304 [UniProt coverage chain A]=91% [Name chain A]=Hydroxyacyl-CoA dehydrogenase ChsB1 [UniProt sequence chain A]=MKLTESNRSPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVVDEIGAAAADAGAKAVAVAGDISQRATADELLASAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRDKAKDAEGGSVFGRLVNTSSEAGLVGPVGQANYAAAKAGITALTLSAARALGRYGVCANVICPRARTAMTADVFGAAPDVEAGQIDPLSPQHVVSLVQFLASPAAAEVNGQVFIVYGPQVTLVSPPHMERRFSADGTSWDPTELTATLRDYFAGRDPEQSFSATDLMRQ [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=O53547 [UniProt boundaries chain A-2]=16-304 [UniProt coverage chain A-2]=91% [Name chain A-2]=Hydroxyacyl-CoA dehydrogenase ChsB1 [UniProt sequence chain A-2]=MKLTESNRSPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVVDEIGAAAADAGAKAVAVAGDISQRATADELLASAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRDKAKDAEGGSVFGRLVNTSSEAGLVGPVGQANYAAAKAGITALTLSAARALGRYGVCANVICPRARTAMTADVFGAAPDVEAGQIDPLSPQHVVSLVQFLASPAAAEVNGQVFIVYGPQVTLVSPPHMERRFSADGTSWDPTELTATLRDYFAGRDPEQSFSATDLMRQ [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.21 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000930 [Entry] [Entry number]=1115 [Entry name]=ChsB1 [PDB ID]=7lg9 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Short chain dehydrogenase [Evidence level]=No contradicting information [Evidence text]=There is a knot-like interface between individual monomers. The structure looks like a domain-swapped Rossmann fold unit. The two largest helices, α7 and α9, which are parallel, form the majority of the dimer interface. Analytical ultracentrifugation sedimentation velocity analysis suggests homodimeric structure (PMID:33826843). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000930,MF7000931 [UniProt ID chain A]=O53547 [UniProt boundaries chain A]=15-304 [UniProt coverage chain A]=91% [Name chain A]=Hydroxyacyl-CoA dehydrogenase ChsB1 [UniProt sequence chain A]=MKLTESNRSPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVVDEIGAAAADAGAKAVAVAGDISQRATADELLASAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRDKAKDAEGGSVFGRLVNTSSEAGLVGPVGQANYAAAKAGITALTLSAARALGRYGVCANVICPRARTAMTADVFGAAPDVEAGQIDPLSPQHVVSLVQFLASPAAAEVNGQVFIVYGPQVTLVSPPHMERRFSADGTSWDPTELTATLRDYFAGRDPEQSFSATDLMRQ [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=O53547 [UniProt boundaries chain B]=16-304 [UniProt coverage chain B]=91% [Name chain B]=Hydroxyacyl-CoA dehydrogenase ChsB1 [UniProt sequence chain B]=MKLTESNRSPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVVDEIGAAAADAGAKAVAVAGDISQRATADELLASAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRDKAKDAEGGSVFGRLVNTSSEAGLVGPVGQANYAAAKAGITALTLSAARALGRYGVCANVICPRARTAMTADVFGAAPDVEAGQIDPLSPQHVVSLVQFLASPAAAEVNGQVFIVYGPQVTLVSPPHMERRFSADGTSWDPTELTATLRDYFAGRDPEQSFSATDLMRQ [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.03 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000931 [Entry] [Entry number]=1116 [Entry name]=PSPC1/NONO paraspeckle proteins' heterodimer [PDB ID]=3sde [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=NOPS+RRMs+CC [Sequence domain]=NOPS (NUC059) domain,RNA recognition motif [Evidence level]=Indirect evidence [Evidence text]=PSPC1-NONO DBHS domain heterodimers form an extensively intertwined dimer with very large surface, including a long, antiparallel coiled-coil dimerization region. The different DBHS proteins are typically copurified from mammalian cells, suggesting that they act as obligate homo- or heterodimers (PMID:22416126). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000932,MF7000933,MF7000934 [UniProt ID chain A]=Q8WXF1 [UniProt boundaries chain A]=66-320 [UniProt coverage chain A]=48% [Name chain A]=Paraspeckle component 1 [UniProt sequence chain A]=MMLRGNLKQVRIEKNPARLRALESAVGESEPAAAAAMALALAGEPAPPAPAPPEDHPDEEMGFTIDIKSFLKPGEKTYTQRCRLFVGNLPTDITEEDFKRLFERYGEPSEVFINRDRGFGFIRLESRTLAEIAKAELDGTILKSRPLRIRFATHGAALTVKNLSPVVSNELLEQAFSQFGPVEKAVVVVDDRGRATGKGFVEFAAKPPARKALERCGDGAFLLTTTPRPVIVEPMEQFDDEDGLPEKLMQKTQQYHKEREQPPRFAQPGTFEFEYASRWKALDEMEKQQREQVDRNIREAKEKLEAEMEAARHEHQLMLMRQDLMRRQEELRRLEELRNQELQKRKQIQLRHEEEHRRREEEMIRHREQEELRRQQEGFKPNYMENREQEMRMGDMGPRGAINMGDAFSPAPAGNQGPPPMMGMNMNNRATIPGPPMGPGPAMGPEGAANMGTPMMPDNGAVHNDRFPQGPPSQMGSPMGSRTGSETPQAPMSGVGPVSGGPGGFGRGSQGGNFEGPNKRRRY [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q15233 [UniProt boundaries chain B]=66-304 [UniProt coverage chain B]=50% [Name chain B]=Non-POU domain-containing octamer-binding protein [UniProt sequence chain B]=MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPAGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRAAPGAEFAPNKRRRY [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Homo sapiens [Accession]=MF7000932 [Entry] [Entry number]=1117 [Entry name]=NONO-1 homodimer from C. elegans [PDB ID]=5ca5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=NOPS+RRMs+CC [Sequence domain]=NOPS (NUC059) domain,RNA recognition motif [Evidence level]=Indirect evidence [Evidence text]=PSPC1-NONO DBHS domain heterodimers form an extensively intertwined dimer with very large surface, including a long, antiparallel coiled-coil dimerization region. The different DBHS proteins are typically copurified from mammalian cells, suggesting that they act as obligate homo- or heterodimers (PMID:22416126). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000932,MF7000933,MF7000934 [UniProt ID chain A]=B3GWA1 [UniProt boundaries chain A]=106-353 [UniProt coverage chain A]=44% [Name chain A]=RRM domain-containing protein [UniProt sequence chain A]=MSGARRDNRRSNGRDDSSRVAKAENDRKPGRENRGGDEKRGNSNNAARSGGGGGGNRGGAERGIAPAQQPYDNNGGHRSGGGGGRSGGGGTSFNGAAFTESQLMDEVPKKKFTGRCRLFVGNLPNEVKETELKELFSPHGDIAECYLSGKGFAFLRLDTRAHAESAKEAIDGRIIHGRQVRVRFAVHGAAIRVKELSPTVSNEMLYHAFSHFGDVERAVHIVDEKGRPTGEGIVEFERKPNCNEAMAAIRDKVFLLTASPKPLICEVLEPRDEDDGLAERMIPRTPGLSKERELGPRFPTPNSFEYVYGMKWKELYVVEQKRRAQLDEELRESRRRLESDMELAYQDYQAQMLREDLQRRQQELERLEAARRERMRGLGGPPPGMPGGVPPQAQPFNPHGGSMFGGPGGPGGPPPFGQPFQQAPQGMFNVPTGPPPLMGGGGDPRGPPGGMGGPPGHGGMGGPPGHGGQGGPPGHGGMGGPPPGQGGPGGPGGPGGPGGMLPKSHGRSNMIEGVQRLLQIFKSDNGPPGGMPGRDYPPQQGPGGMFGSYGDGGYPPEKKQRR [Source organism chain A]=Caenorhabditis elegans [UniProt ID chain B]=B3GWA1 [UniProt boundaries chain B]=106-353 [UniProt coverage chain B]=44% [Name chain B]=RRM domain-containing protein [UniProt sequence chain B]=MSGARRDNRRSNGRDDSSRVAKAENDRKPGRENRGGDEKRGNSNNAARSGGGGGGNRGGAERGIAPAQQPYDNNGGHRSGGGGGRSGGGGTSFNGAAFTESQLMDEVPKKKFTGRCRLFVGNLPNEVKETELKELFSPHGDIAECYLSGKGFAFLRLDTRAHAESAKEAIDGRIIHGRQVRVRFAVHGAAIRVKELSPTVSNEMLYHAFSHFGDVERAVHIVDEKGRPTGEGIVEFERKPNCNEAMAAIRDKVFLLTASPKPLICEVLEPRDEDDGLAERMIPRTPGLSKERELGPRFPTPNSFEYVYGMKWKELYVVEQKRRAQLDEELRESRRRLESDMELAYQDYQAQMLREDLQRRQQELERLEAARRERMRGLGGPPPGMPGGVPPQAQPFNPHGGSMFGGPGGPGGPPPFGQPFQQAPQGMFNVPTGPPPLMGGGGDPRGPPGGMGGPPGHGGMGGPPGHGGQGGPPGHGGMGGPPPGQGGPGGPGGPGGPGGMLPKSHGRSNMIEGVQRLLQIFKSDNGPPGGMPGRDYPPQQGPGGMFGSYGDGGYPPEKKQRR [Source organism chain B]=Caenorhabditis elegans [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Caenorhabditis elegans [Accession]=MF7000933 [Entry] [Entry number]=1118 [Entry name]=human SFPQ/NONO DBHS heterodimer [PDB ID]=7lrq [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=NOPS+RRMs+CC [Sequence domain]=NOPS (NUC059) domain,RNA recognition motif [Evidence level]=Indirect evidence [Evidence text]=PSPC1-NONO DBHS domain heterodimers form an extensively intertwined dimer with very large surface, including a long, antiparallel coiled-coil dimerization region. The different DBHS proteins are typically copurified from mammalian cells, suggesting that they act as obligate homo- or heterodimers (PMID:22416126). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000932,MF7000933,MF7000934 [UniProt ID chain A]=P23246 [UniProt boundaries chain A]=290-528 [UniProt coverage chain A]=33% [Name chain A]=Splicing factor, proline- and glutamine-rich [UniProt sequence chain A]=MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q15233 [UniProt boundaries chain B]=56-308 [UniProt coverage chain B]=53% [Name chain B]=Non-POU domain-containing octamer-binding protein [UniProt sequence chain B]=MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPAGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRAAPGAEFAPNKRRRY [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Homo sapiens [Accession]=MF7000934 [Entry] [Entry number]=1119 [Entry name]=Dimerization domain of the doublesex protein (Drosophila melanogaster) [PDB ID]=1zv1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Doublesex dimerisation domain [Evidence level]=Indirect evidence [Evidence text]=The interface of the doublesex dimerisation domain is very tight, large and hydrophobic, the interaction of the monomers is very strong Kd < 1nM (PMID:18184648, PMID:16049008). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000935,MF7000936,MF7000937 [UniProt ID chain A]=P23023 [UniProt boundaries chain A]=353-408 [UniProt coverage chain A]=10% [Name chain A]=Protein doublesex [UniProt sequence chain A]=MVSEENWNSDTMSDSDMIDSKNDVCGGASSSSGSSISPRTPPNCARCRNHGLKITLKGHKRYCKFRYCTCEKCRLTADRQRVMALQTALRRAQAQDEQRALHMHEVPPANPAATTLLSHHHHVAAPAHVHAHHVHAHHAHGGHHSHHGHVLHHQQAAAAAAAAPSAPASHLGGSSTAASSIHGHAHAHHVHMAAAAAASVAQHQHQSHPHSHHHHHQNHHQHPHQQPATQTALRSPPHSDHGGSVGPATSSSGGGAPSSSNAAAATSSNGSSGGGGGGGGGSSGGGAGGGRSSGTSVITSADHHMTTVPTPAQSLEGSCDSSSPSPSSTSGAAILPISVSVNRKNGANVPLGQDVFLDYCQKLLEKFRYPWELMPLMYVILKDADANIEEASRRIEEARVEINRTVAQIYYNYYTPMALVNGAPMYLTYPSIEQGRYGAHFTHLPLTQICPPTPEPLALSRSPSSPSGPSAVHNQKPSRPGSSNGTVHSAASPTMVTTMATTSSTPTLSRRQRSRSATPTTPPPPPPAHSSSNGAYHHGHHLVSSTAAT [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=P23023 [UniProt boundaries chain B]=353-408 [UniProt coverage chain B]=10% [Name chain B]=Protein doublesex [UniProt sequence chain B]=MVSEENWNSDTMSDSDMIDSKNDVCGGASSSSGSSISPRTPPNCARCRNHGLKITLKGHKRYCKFRYCTCEKCRLTADRQRVMALQTALRRAQAQDEQRALHMHEVPPANPAATTLLSHHHHVAAPAHVHAHHVHAHHAHGGHHSHHGHVLHHQQAAAAAAAAPSAPASHLGGSSTAASSIHGHAHAHHVHMAAAAAASVAQHQHQSHPHSHHHHHQNHHQHPHQQPATQTALRSPPHSDHGGSVGPATSSSGGGAPSSSNAAAATSSNGSSGGGGGGGGGSSGGGAGGGRSSGTSVITSADHHMTTVPTPAQSLEGSCDSSSPSPSSTSGAAILPISVSVNRKNGANVPLGQDVFLDYCQKLLEKFRYPWELMPLMYVILKDADANIEEASRRIEEARVEINRTVAQIYYNYYTPMALVNGAPMYLTYPSIEQGRYGAHFTHLPLTQICPPTPEPLALSRSPSSPSGPSAVHNQKPSRPGSSNGTVHSAASPTMVTTMATTSSTPTLSRRQRSRSATPTTPPPPPPAHSSSNGAYHHGHHLVSSTAAT [Source organism chain B]=Drosophila melanogaster [ExpTech]=X-ray [Resolution]=1.60 [Source organism]=Drosophila melanogaster [Accession]=MF7000935 [Entry] [Entry number]=1120 [Entry name]=Doublesex protein, long (Drosophila melanogaster) [PDB ID]=2jz1 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Doublesex dimerisation domain [Evidence level]=Indirect evidence [Evidence text]=The interface of the doublesex dimerisation domain is very tight, large and hydrophobic, the interaction of the monomers is very strong Kd < 1nM (PMID:18184648, PMID:16049008). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000935,MF7000936,MF7000937 [UniProt ID chain A]=P23023 [UniProt boundaries chain A]=350-421 [UniProt coverage chain A]=13% [Name chain A]=Protein doublesex [UniProt sequence chain A]=MVSEENWNSDTMSDSDMIDSKNDVCGGASSSSGSSISPRTPPNCARCRNHGLKITLKGHKRYCKFRYCTCEKCRLTADRQRVMALQTALRRAQAQDEQRALHMHEVPPANPAATTLLSHHHHVAAPAHVHAHHVHAHHAHGGHHSHHGHVLHHQQAAAAAAAAPSAPASHLGGSSTAASSIHGHAHAHHVHMAAAAAASVAQHQHQSHPHSHHHHHQNHHQHPHQQPATQTALRSPPHSDHGGSVGPATSSSGGGAPSSSNAAAATSSNGSSGGGGGGGGGSSGGGAGGGRSSGTSVITSADHHMTTVPTPAQSLEGSCDSSSPSPSSTSGAAILPISVSVNRKNGANVPLGQDVFLDYCQKLLEKFRYPWELMPLMYVILKDADANIEEASRRIEEARVEINRTVAQIYYNYYTPMALVNGAPMYLTYPSIEQGRYGAHFTHLPLTQICPPTPEPLALSRSPSSPSGPSAVHNQKPSRPGSSNGTVHSAASPTMVTTMATTSSTPTLSRRQRSRSATPTTPPPPPPAHSSSNGAYHHGHHLVSSTAAT [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=P23023 [UniProt boundaries chain B]=350-421 [UniProt coverage chain B]=13% [Name chain B]=Protein doublesex [UniProt sequence chain B]=MVSEENWNSDTMSDSDMIDSKNDVCGGASSSSGSSISPRTPPNCARCRNHGLKITLKGHKRYCKFRYCTCEKCRLTADRQRVMALQTALRRAQAQDEQRALHMHEVPPANPAATTLLSHHHHVAAPAHVHAHHVHAHHAHGGHHSHHGHVLHHQQAAAAAAAAPSAPASHLGGSSTAASSIHGHAHAHHVHMAAAAAASVAQHQHQSHPHSHHHHHQNHHQHPHQQPATQTALRSPPHSDHGGSVGPATSSSGGGAPSSSNAAAATSSNGSSGGGGGGGGGSSGGGAGGGRSSGTSVITSADHHMTTVPTPAQSLEGSCDSSSPSPSSTSGAAILPISVSVNRKNGANVPLGQDVFLDYCQKLLEKFRYPWELMPLMYVILKDADANIEEASRRIEEARVEINRTVAQIYYNYYTPMALVNGAPMYLTYPSIEQGRYGAHFTHLPLTQICPPTPEPLALSRSPSSPSGPSAVHNQKPSRPGSSNGTVHSAASPTMVTTMATTSSTPTLSRRQRSRSATPTTPPPPPPAHSSSNGAYHHGHHLVSSTAAT [Source organism chain B]=Drosophila melanogaster [ExpTech]=NMR [Resolution]=N/A [Source organism]=Drosophila melanogaster [Accession]=MF7000936 [Entry] [Entry number]=1121 [Entry name]=Doublesex protein, short (Drosophila melanogaster) [PDB ID]=2jz0 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Doublesex dimerisation domain [Evidence level]=Indirect evidence [Evidence text]=The interface of the doublesex dimerisation domain is very tight, large and hydrophobic, the interaction of the monomers is very strong Kd < 1nM (PMID:18184648, PMID:16049008). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000935,MF7000936,MF7000937 [UniProt ID chain A]=P23023 [UniProt boundaries chain A]=350-408 [UniProt coverage chain A]=10% [Name chain A]=Protein doublesex [UniProt sequence chain A]=MVSEENWNSDTMSDSDMIDSKNDVCGGASSSSGSSISPRTPPNCARCRNHGLKITLKGHKRYCKFRYCTCEKCRLTADRQRVMALQTALRRAQAQDEQRALHMHEVPPANPAATTLLSHHHHVAAPAHVHAHHVHAHHAHGGHHSHHGHVLHHQQAAAAAAAAPSAPASHLGGSSTAASSIHGHAHAHHVHMAAAAAASVAQHQHQSHPHSHHHHHQNHHQHPHQQPATQTALRSPPHSDHGGSVGPATSSSGGGAPSSSNAAAATSSNGSSGGGGGGGGGSSGGGAGGGRSSGTSVITSADHHMTTVPTPAQSLEGSCDSSSPSPSSTSGAAILPISVSVNRKNGANVPLGQDVFLDYCQKLLEKFRYPWELMPLMYVILKDADANIEEASRRIEEARVEINRTVAQIYYNYYTPMALVNGAPMYLTYPSIEQGRYGAHFTHLPLTQICPPTPEPLALSRSPSSPSGPSAVHNQKPSRPGSSNGTVHSAASPTMVTTMATTSSTPTLSRRQRSRSATPTTPPPPPPAHSSSNGAYHHGHHLVSSTAAT [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=P23023 [UniProt boundaries chain B]=350-408 [UniProt coverage chain B]=10% [Name chain B]=Protein doublesex [UniProt sequence chain B]=MVSEENWNSDTMSDSDMIDSKNDVCGGASSSSGSSISPRTPPNCARCRNHGLKITLKGHKRYCKFRYCTCEKCRLTADRQRVMALQTALRRAQAQDEQRALHMHEVPPANPAATTLLSHHHHVAAPAHVHAHHVHAHHAHGGHHSHHGHVLHHQQAAAAAAAAPSAPASHLGGSSTAASSIHGHAHAHHVHMAAAAAASVAQHQHQSHPHSHHHHHQNHHQHPHQQPATQTALRSPPHSDHGGSVGPATSSSGGGAPSSSNAAAATSSNGSSGGGGGGGGGSSGGGAGGGRSSGTSVITSADHHMTTVPTPAQSLEGSCDSSSPSPSSTSGAAILPISVSVNRKNGANVPLGQDVFLDYCQKLLEKFRYPWELMPLMYVILKDADANIEEASRRIEEARVEINRTVAQIYYNYYTPMALVNGAPMYLTYPSIEQGRYGAHFTHLPLTQICPPTPEPLALSRSPSSPSGPSAVHNQKPSRPGSSNGTVHSAASPTMVTTMATTSSTPTLSRRQRSRSATPTTPPPPPPAHSSSNGAYHHGHHLVSSTAAT [Source organism chain B]=Drosophila melanogaster [ExpTech]=NMR [Resolution]=N/A [Source organism]=Drosophila melanogaster [Accession]=MF7000937 [Entry] [Entry number]=1122 [Entry name]=Methicillin resistance regulatory protein, MecI [PDB ID]=1sd6 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Penicillinase repressor [Evidence level]=Direct evidence [Evidence text]=Each monomer has α1-β1-α2-α3-β2-wing-β3-α4-α5-α6 fold topology and consists of N-terminal and C-terminal domains. The C-terminal domains (helices α4-α5-α6) from both monomers are spirally intertwined at one of the vertices of the triangle to hold the dimer together. Helices α4 and α4' form an antiparallel coiled coil-like structure, while α5-α6 from both monomers form a 4-helix bundle-like structure as a second layer of the dimerization domain. Such structures indicate a large and tight dimer interface and imply that the monomeric chains would be unfolded in isolation (PMID:15716455). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000938,MF7000939,MF7000940 [UniProt ID chain A]=P68262 [UniProt boundaries chain A]=5-123 [UniProt coverage chain A]=96% [Name chain A]=Methicillin resistance regulatory protein MecI [UniProt sequence chain A]=MDNKTYEISSAEWEVMNIIWMKKYASANNIIEEIQMQKDWSPKTIRTLITRLYKKGFIDRKKDNKIFQYYSLVEESDIKYKTSKNFINKVYKGGFNSLVLNFVEKEDLSQDEIEELRNILNKK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=P68262 [UniProt boundaries chain B]=5-122 [UniProt coverage chain B]=95% [Name chain B]=Methicillin resistance regulatory protein MecI [UniProt sequence chain B]=MDNKTYEISSAEWEVMNIIWMKKYASANNIIEEIQMQKDWSPKTIRTLITRLYKKGFIDRKKDNKIFQYYSLVEESDIKYKTSKNFINKVYKGGFNSLVLNFVEKEDLSQDEIEELRNILNKK [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.65 [Source organism]=Staphylococcus aureus [Accession]=MF7000938 [Entry] [Entry number]=1123 [Entry name]=SeMet derivative of Methicillin resistance regulatory protein, MecI [PDB ID]=1sd7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Penicillinase repressor [Evidence level]=Direct evidence [Evidence text]=Each monomer has α1-β1-α2-α3-β2-wing-β3-α4-α5-α6 fold topology and consists of N-terminal and C-terminal domains. The C-terminal domains (helices α4-α5-α6) from both monomers are spirally intertwined at one of the vertices of the triangle to hold the dimer together. Helices α4 and α4' form an antiparallel coiled coil-like structure, while α5-α6 from both monomers form a 4-helix bundle-like structure as a second layer of the dimerization domain. Such structures indicate a large and tight dimer interface and imply that the monomeric chains would be unfolded in isolation (PMID:15716455). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000938,MF7000939,MF7000940 [UniProt ID chain A]=P68262 [UniProt boundaries chain A]=5-123 [UniProt coverage chain A]=96% [Name chain A]=Methicillin resistance regulatory protein MecI [UniProt sequence chain A]=MDNKTYEISSAEWEVMNIIWMKKYASANNIIEEIQMQKDWSPKTIRTLITRLYKKGFIDRKKDNKIFQYYSLVEESDIKYKTSKNFINKVYKGGFNSLVLNFVEKEDLSQDEIEELRNILNKK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=P68262 [UniProt boundaries chain B]=5-122 [UniProt coverage chain B]=95% [Name chain B]=Methicillin resistance regulatory protein MecI [UniProt sequence chain B]=MDNKTYEISSAEWEVMNIIWMKKYASANNIIEEIQMQKDWSPKTIRTLITRLYKKGFIDRKKDNKIFQYYSLVEESDIKYKTSKNFINKVYKGGFNSLVLNFVEKEDLSQDEIEELRNILNKK [Source organism chain B]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=2.65 [Source organism]=Staphylococcus aureus [Accession]=MF7000939 [Entry] [Entry number]=1124 [Entry name]=Rv1846c, a putative transcriptional regulatory protein (Mycobacterium tuberculosis) [PDB ID]=2g9w [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Penicillinase repressor [Evidence level]=Direct evidence [Evidence text]=Each monomer has α1-β1-α2-α3-β2-wing-β3-α4-α5-α6 fold topology and consists of N-terminal and C-terminal domains. The C-terminal domains (helices α4-α5-α6) from both monomers are spirally intertwined at one of the vertices of the triangle to hold the dimer together. Helices α4 and α4' form an antiparallel coiled coil-like structure, while α5-α6 from both monomers form a 4-helix bundle-like structure as a second layer of the dimerization domain. Such structures indicate a large and tight dimer interface and imply that the monomeric chains would be unfolded in isolation (PMID:15716455). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000938,MF7000939,MF7000940 [UniProt ID chain A]=P9WMJ5 [UniProt boundaries chain A]=3-124 [UniProt coverage chain A]=88% [Name chain A]=Transcriptional regulator BlaI [UniProt sequence chain A]=MAKLTRLGDLERAVMDHLWSRTEPQTVRQVHEALSARRDLAYTTVMTVLQRLAKKNLVLQIRDDRAHRYAPVHGRDELVAGLMVDALAQAEDSGSRQAALVHFVERVGADEADALRRALAELEAGHGNRPPAGAATET [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WMJ5 [UniProt boundaries chain B]=3-124 [UniProt coverage chain B]=88% [Name chain B]=Transcriptional regulator BlaI [UniProt sequence chain B]=MAKLTRLGDLERAVMDHLWSRTEPQTVRQVHEALSARRDLAYTTVMTVLQRLAKKNLVLQIRDDRAHRYAPVHGRDELVAGLMVDALAQAEDSGSRQAALVHFVERVGADEADALRRALAELEAGHGNRPPAGAATET [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.80 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000940 [Entry] [Entry number]=1125 [Entry name]=DNA-binding domain of MetR (Escherichia coli) [PDB ID]=5fo5 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (lysR type) transcriptional regulator [Evidence level]=No contradicting information [Evidence text]=Winged-helix–turn–helix DNA-binding domain and a coiled coil dimerization region with extensive hydrophobic contacts that stabilize the large dimerization interface (PMID:27303893). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000941,MF7000942 [UniProt ID chain A]=P0A9F9 [UniProt boundaries chain A]=1-88 [UniProt coverage chain A]=27% [Name chain A]=HTH-type transcriptional regulator MetR [UniProt sequence chain A]=MIEVKHLKTLQALRNCGSLAAAAATLHQTQSALSHQFSDLEQRLGFRLFVRKSQPLRFTPQGEILLQLANQVLPQISQALQACNEPQQTRLRIAIECHSCIQWLTPALENFHKNWPQVEMDFKSGVTFDPQPALQQGELDLVMTSDILPRSGLHYSPMFDYEVRLVLAPDHPLAAKTRITPEDLASETLLIYPVQRSRLDVWRHFLQPAGVSPSLKSVDNTLLLIQMVAARMGIAALPHWVVESFERQGLVVTKTLGEGLWSRLYAAVRDGEQRQPVTEAFIRSARNHACDHLPFVKSAERPTYDAPTVRPGSPARL [Source organism chain A]=Escherichia coli [UniProt ID chain A-2]=P0A9F9 [UniProt boundaries chain A-2]=1-88 [UniProt coverage chain A-2]=27% [Name chain A-2]=HTH-type transcriptional regulator MetR [UniProt sequence chain A-2]=MIEVKHLKTLQALRNCGSLAAAAATLHQTQSALSHQFSDLEQRLGFRLFVRKSQPLRFTPQGEILLQLANQVLPQISQALQACNEPQQTRLRIAIECHSCIQWLTPALENFHKNWPQVEMDFKSGVTFDPQPALQQGELDLVMTSDILPRSGLHYSPMFDYEVRLVLAPDHPLAAKTRITPEDLASETLLIYPVQRSRLDVWRHFLQPAGVSPSLKSVDNTLLLIQMVAARMGIAALPHWVVESFERQGLVVTKTLGEGLWSRLYAAVRDGEQRQPVTEAFIRSARNHACDHLPFVKSAERPTYDAPTVRPGSPARL [Source organism chain A-2]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.16 [Source organism]=Escherichia coli [Accession]=MF7000941 [Entry] [Entry number]=1126 [Entry name]=PaCysB NTD domain [PDB ID]=5z4y [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (lysR type) transcriptional regulator [Evidence level]=No contradicting information [Evidence text]=Winged-helix–turn–helix DNA-binding domain and a coiled coil dimerization region with extensive hydrophobic contacts that stabilize the large dimerization interface (PMID:27303893). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000941,MF7000942 [UniProt ID chain A]=O05926 [UniProt boundaries chain A]=1-88 [UniProt coverage chain A]=27% [Name chain A]=CysB [UniProt sequence chain A]=MKLQQLRYIWEVAHHDLNVSATAQSLYTSQPGISKQIRLLEDELGVEVFARSGKHLTRVTPAGERIIHTAGEILRKVESIKQIAQEFSNEKKGTLSIATTHTQARYALPNVISGFIKQYPDVSLHMHQGTPMQIAEMAADGTVDFAIATEALELFGDLIMMPCYRWNRCVIVPHGHPLTKLPKLTLEALAEQPIVTYVFGFTGRSKLDEAFSQRGLVPKVVFTAADADVIKTYVRLGLGVGIVAHMAVDPKLDNDLVILDASHLFESSVTKIGFRRGTFLRGFMCDFIEKFAPHLTRELLAKAVQCHNKAELDELFDGIELPVY [Source organism chain A]=Pseudomonas aeruginosa [UniProt ID chain B]=O05926 [UniProt boundaries chain B]=1-88 [UniProt coverage chain B]=27% [Name chain B]=CysB [UniProt sequence chain B]=MKLQQLRYIWEVAHHDLNVSATAQSLYTSQPGISKQIRLLEDELGVEVFARSGKHLTRVTPAGERIIHTAGEILRKVESIKQIAQEFSNEKKGTLSIATTHTQARYALPNVISGFIKQYPDVSLHMHQGTPMQIAEMAADGTVDFAIATEALELFGDLIMMPCYRWNRCVIVPHGHPLTKLPKLTLEALAEQPIVTYVFGFTGRSKLDEAFSQRGLVPKVVFTAADADVIKTYVRLGLGVGIVAHMAVDPKLDNDLVILDASHLFESSVTKIGFRRGTFLRGFMCDFIEKFAPHLTRELLAKAVQCHNKAELDELFDGIELPVY [Source organism chain B]=Pseudomonas aeruginosa [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Pseudomonas aeruginosa [Accession]=MF7000942 [Entry] [Entry number]=1127 [Entry name]=Rubella virus capsid protein (residues 127-277) [PDB ID]=4hbe [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Capsid proteins [Sequence domain]=Rubella capsid protein [Evidence level]=Indirect evidence [Evidence text]=RV capsid proteins form a tight, disulfide-linked dimer. There is beta sheet augmentation between the monomers. The resultant 10-stranded, left-handed twisted sheet forms a partially open β-barrel with the two helices lying in the center of the barrel. The β-strands A and B from one monomer are inserted into the BH loop of the other monomer, forming a tightly bound dimeric structure consistent with the previous observation that the RV capsid protein forms dimers when isolated from the virion (PMID:24282305). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000943,MF7000944,MF7000945 [UniProt ID chain A]=P08563 [UniProt boundaries chain A]=150-247 [UniProt coverage chain A]=9% [Name chain A]=Structural polyprotein [UniProt sequence chain A]=MASTTPITMEDLQKALEAQSRALRAGLAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRKDWSRAPPPPEERQESRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDTAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLAAVAVGTARAGLQPRADMAAPPMPPQPPRAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHHRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTSLTTAANSTTAATPATAPPPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGTRCPELVSPMGRATCSPASALWLATANALSLDHAFAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQTPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPTAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRALAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDVGAFPPGKFVTAALLNTPPPYQVSCGGESDRASARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALLLAGLLACCAKCLYYLRGAIAPR [Source organism chain A]=Rubella virus [UniProt ID chain B]=P08563 [UniProt boundaries chain B]=150-247 [UniProt coverage chain B]=9% [Name chain B]=Structural polyprotein [UniProt sequence chain B]=MASTTPITMEDLQKALEAQSRALRAGLAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRKDWSRAPPPPEERQESRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDTAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLAAVAVGTARAGLQPRADMAAPPMPPQPPRAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHHRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTSLTTAANSTTAATPATAPPPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGTRCPELVSPMGRATCSPASALWLATANALSLDHAFAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQTPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPTAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRALAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDVGAFPPGKFVTAALLNTPPPYQVSCGGESDRASARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALLLAGLLACCAKCLYYLRGAIAPR [Source organism chain B]=Rubella virus [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Rubella virus [Accession]=MF7000943 [Entry] [Entry number]=1128 [Entry name]=Rubella virus capsid protein [PDB ID]=5khe [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Capsid proteins [Sequence domain]=Rubella capsid protein [Evidence level]=Indirect evidence [Evidence text]=RV capsid proteins form a tight, disulfide-linked dimer. There is beta sheet augmentation between the monomers. The resultant 10-stranded, left-handed twisted sheet forms a partially open β-barrel with the two helices lying in the center of the barrel. The β-strands A and B from one monomer are inserted into the BH loop of the other monomer, forming a tightly bound dimeric structure consistent with the previous observation that the RV capsid protein forms dimers when isolated from the virion (PMID:24282305). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000943,MF7000944,MF7000945 [UniProt ID chain A]=P07566 [UniProt boundaries chain A]=150-247 [UniProt coverage chain A]=9% [Name chain A]=Structural polyprotein [UniProt sequence chain A]=MASTTPITMEDLQKALEAQSRALRAELAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRRDWSRAPPPPEERQETRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDSAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLATVAVGTARAGLQPRADMAAPPTLPQPPCAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHYRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTPLTTAANSTTAATPATAPAPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGARCPELVSPMGRATCSPASALWLATANALSLDHALAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQAPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPAAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRTLAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDLGAVPPGKFVTAALLNTPPPYQVSCGGESDRATARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALPLAGLLACCAKCLYYLRGAIAPR [Source organism chain A]=Rubella virus [UniProt ID chain B]=P07566 [UniProt boundaries chain B]=150-247 [UniProt coverage chain B]=9% [Name chain B]=Structural polyprotein [UniProt sequence chain B]=MASTTPITMEDLQKALEAQSRALRAELAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRRDWSRAPPPPEERQETRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDSAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLATVAVGTARAGLQPRADMAAPPTLPQPPCAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHYRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTPLTTAANSTTAATPATAPAPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGARCPELVSPMGRATCSPASALWLATANALSLDHALAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQAPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPAAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRTLAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDLGAVPPGKFVTAALLNTPPPYQVSCGGESDRATARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALPLAGLLACCAKCLYYLRGAIAPR [Source organism chain B]=Rubella virus [ExpTech]=Electron Microscopy [Resolution]=35.00 [Source organism]=Rubella virus [Accession]=MF7000944 [Entry] [Entry number]=1129 [Entry name]=Rubella virus capsid protein [PDB ID]=5khf [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Capsid proteins [Sequence domain]=Rubella capsid protein [Evidence level]=Indirect evidence [Evidence text]=RV capsid proteins form a tight, disulfide-linked dimer. There is beta sheet augmentation between the monomers. The resultant 10-stranded, left-handed twisted sheet forms a partially open β-barrel with the two helices lying in the center of the barrel. The β-strands A and B from one monomer are inserted into the BH loop of the other monomer, forming a tightly bound dimeric structure consistent with the previous observation that the RV capsid protein forms dimers when isolated from the virion (PMID:24282305). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000943,MF7000944,MF7000945 [UniProt ID chain A]=P07566 [UniProt boundaries chain A]=150-247 [UniProt coverage chain A]=9% [Name chain A]=Structural polyprotein [UniProt sequence chain A]=MASTTPITMEDLQKALEAQSRALRAELAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRRDWSRAPPPPEERQETRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDSAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLATVAVGTARAGLQPRADMAAPPTLPQPPCAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHYRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTPLTTAANSTTAATPATAPAPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGARCPELVSPMGRATCSPASALWLATANALSLDHALAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQAPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPAAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRTLAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDLGAVPPGKFVTAALLNTPPPYQVSCGGESDRATARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALPLAGLLACCAKCLYYLRGAIAPR [Source organism chain A]=Rubella virus [UniProt ID chain B]=P07566 [UniProt boundaries chain B]=150-247 [UniProt coverage chain B]=9% [Name chain B]=Structural polyprotein [UniProt sequence chain B]=MASTTPITMEDLQKALEAQSRALRAELAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRRDWSRAPPPPEERQETRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDSAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLATVAVGTARAGLQPRADMAAPPTLPQPPCAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHYRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTPLTTAANSTTAATPATAPAPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGARCPELVSPMGRATCSPASALWLATANALSLDHALAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQAPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPAAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRTLAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDLGAVPPGKFVTAALLNTPPPYQVSCGGESDRATARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALPLAGLLACCAKCLYYLRGAIAPR [Source organism chain B]=Rubella virus [ExpTech]=Electron Microscopy [Resolution]=35.00 [Source organism]=Rubella virus [Accession]=MF7000945 [Entry] [Entry number]=1130 [Entry name]=C-terminal dimerization domain of infectious bronchitis virus nucleocapsid protein [PDB ID]=2ge7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Nucleocapsid proteins [Sequence domain]=Coronavirus nucleocapsid [Evidence level]=Direct evidence [Evidence text]=The CTD of nucleocapsid proteins forms a tightly intertwined dimer with an intermolecular four-stranded central β-sheet platform flanked by α-helices that buries a large surface. It is a dimer in solution even at very low concentrations (PMID:16775348, PMID:28331093). Thermal transition of the CTD was fully reversible and cooperative, with a van't Hoff enthalpy/calorimetric enthalpy ratio of 1.03, which implies two-state folding (PMID:25700263). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000946,MF7000107,MF7000947 [UniProt ID chain A]=P32923 [UniProt boundaries chain A]=226-332 [UniProt coverage chain A]=26% [Name chain A]=Nucleoprotein [UniProt sequence chain A]=MASGKATGKTDAPAPVIKLGGPRPPKVGSSGNASWFQAIKAKKLNSPQPKFEGSGVPDNENFKTSQQHGYWRRQARFKPGKGRRKPVPDAWYFYYTGTGPAADLNWGDSQDGIVWVAAKGADVKSRSNQGTRDPDKFDQYPLRFSDGGPDGNFRWDFIPLNRGRSGRSTAASSAASSRPPSREGSRGRRSGSEDDLIARAAKIIQDQQKKGSRITKAKADEMAHRRYCKRTIPPGYKVDQVFGPRTKGKEGNFGDDKMNEEGIKDGRVTAMLNLVPSSHACLFGSRVTPKLQPDGLHLKFEFTTVVPRDDPQFDNYVKICDQCVDGVGTRPKDDEPKPKSRSSSRPATRTSSPAPRQQRLKKEKRPKKQDDEVDKALTSDEERNNAQLEFDDEPKVINWGDSALGENEL [Source organism chain A]=Avian infectious bronchitis virus [UniProt ID chain B]=P32923 [UniProt boundaries chain B]=226-333 [UniProt coverage chain B]=26% [Name chain B]=Nucleoprotein [UniProt sequence chain B]=MASGKATGKTDAPAPVIKLGGPRPPKVGSSGNASWFQAIKAKKLNSPQPKFEGSGVPDNENFKTSQQHGYWRRQARFKPGKGRRKPVPDAWYFYYTGTGPAADLNWGDSQDGIVWVAAKGADVKSRSNQGTRDPDKFDQYPLRFSDGGPDGNFRWDFIPLNRGRSGRSTAASSAASSRPPSREGSRGRRSGSEDDLIARAAKIIQDQQKKGSRITKAKADEMAHRRYCKRTIPPGYKVDQVFGPRTKGKEGNFGDDKMNEEGIKDGRVTAMLNLVPSSHACLFGSRVTPKLQPDGLHLKFEFTTVVPRDDPQFDNYVKICDQCVDGVGTRPKDDEPKPKSRSSSRPATRTSSPAPRQQRLKKEKRPKKQDDEVDKALTSDEERNNAQLEFDDEPKVINWGDSALGENEL [Source organism chain B]=Avian infectious bronchitis virus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Avian infectious bronchitis virus [Accession]=MF7000946 [Entry] [Entry number]=1131 [Entry name]=C-Terminal domain of human Coronavirus Nl63 nucleocapsid protein [PDB ID]=5epw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Viral proteins [Subclass]=Nucleocapsid proteins [Sequence domain]=Coronavirus nucleocapsid [Evidence level]=Direct evidence [Evidence text]=The CTD of nucleocapsid proteins forms a tightly intertwined dimer with an intermolecular four-stranded central β-sheet platform flanked by α-helices that buries a large surface. It is a dimer in solution even at very low concentrations (PMID:16775348, PMID:28331093). Thermal transition of the CTD was fully reversible and cooperative, with a van't Hoff enthalpy/calorimetric enthalpy ratio of 1.03, which implies two-state folding (PMID:25700263). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000946,MF7000107,MF7000947 [UniProt ID chain A]=Q6Q1R8 [UniProt boundaries chain A]=228-331 [UniProt coverage chain A]=27% [Name chain A]=Nucleoprotein [UniProt sequence chain A]=MASVNWADDRAARKKFPPPSFYMPLLVSSDKAPYRVIPRNLVPIGKGNKDEQIGYWNVQERWRMRRGQRVDLPPKVHFYYLGTGPHKDLKFRQRSDGVVWVAKEGAKTVNTSLGNRKRNQKPLEPKFSIALPPELSVVEFEDRSNNSSRASSRSSTRNNSRDSSRSTSRQQSRTRSDSNQSSSDLVAAVTLALKNLGFDNQSKSPSSSGTSTPKKPNKPLSQPRADKPSQLKKPRWKRVPTREENVIQCFGPRDFNHNMGDSDLVQNGVDAKGFPQLAELIPNQAALFFDSEVSTDEVGDNVQITYTYKMLVAKDNKNLPKFIEQISAFTKPSSIKEMQSQSSHVAQNTVLNASIPESKPLADDDSAIIEIVNEVLH [Source organism chain A]=Human coronavirus NL63 [UniProt ID chain B]=Q6Q1R8 [UniProt boundaries chain B]=228-337 [UniProt coverage chain B]=29% [Name chain B]=Nucleoprotein [UniProt sequence chain B]=MASVNWADDRAARKKFPPPSFYMPLLVSSDKAPYRVIPRNLVPIGKGNKDEQIGYWNVQERWRMRRGQRVDLPPKVHFYYLGTGPHKDLKFRQRSDGVVWVAKEGAKTVNTSLGNRKRNQKPLEPKFSIALPPELSVVEFEDRSNNSSRASSRSSTRNNSRDSSRSTSRQQSRTRSDSNQSSSDLVAAVTLALKNLGFDNQSKSPSSSGTSTPKKPNKPLSQPRADKPSQLKKPRWKRVPTREENVIQCFGPRDFNHNMGDSDLVQNGVDAKGFPQLAELIPNQAALFFDSEVSTDEVGDNVQITYTYKMLVAKDNKNLPKFIEQISAFTKPSSIKEMQSQSSHVAQNTVLNASIPESKPLADDDSAIIEIVNEVLH [Source organism chain B]=Human coronavirus NL63 [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Human coronavirus NL63 [Accession]=MF7000947 [Entry] [Entry number]=1132 [Entry name]=N-domain of the K+/H+ antiporter subunit KhtT at pH 7.5 [PDB ID]=7aht [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=K(+)/H(+) antiporter subunit KhtT [Evidence level]=No contradicting information [Evidence text]=The dimeric arrangement of the N-domain is an integral part of its fold since the buried surface area is extensive (PMID:33790011). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000948,MF7000949,MF7000950 [UniProt ID chain A]=O07535 [UniProt boundaries chain A]=2-68 [UniProt coverage chain A]=40% [Name chain A]=K(+)/H(+) antiporter subunit KhtT [UniProt sequence chain A]=MNIKENDLPGIGKKFEIETRSHEKMTIIIHDDGRREIYRFNDRDPDELLSNISLDDSEARQIAAILGGMVYKPQALESIEMAFSDLIIEWFKVEKGAKSIGRTLGELDVRQNYDVTVIAIIKHNQEKLLNPGADSIIEENDTLVLSGERKHLKKLIHDFLSGEGV [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=O07535 [UniProt boundaries chain B]=2-68 [UniProt coverage chain B]=40% [Name chain B]=K(+)/H(+) antiporter subunit KhtT [UniProt sequence chain B]=MNIKENDLPGIGKKFEIETRSHEKMTIIIHDDGRREIYRFNDRDPDELLSNISLDDSEARQIAAILGGMVYKPQALESIEMAFSDLIIEWFKVEKGAKSIGRTLGELDVRQNYDVTVIAIIKHNQEKLLNPGADSIIEENDTLVLSGERKHLKKLIHDFLSGEGV [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=2.16 [Source organism]=Bacillus subtilis [Accession]=MF7000948 [Entry] [Entry number]=1133 [Entry name]=N-domain of the K+/H+ antiporter subunit KhtT at pH 8.5 [PDB ID]=7agy [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=K(+)/H(+) antiporter subunit KhtT [Evidence level]=No contradicting information [Evidence text]=The dimeric arrangement of the N-domain is an integral part of its fold since the buried surface area is extensive (PMID:33790011). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000948,MF7000949,MF7000950 [UniProt ID chain A]=O07535 [UniProt boundaries chain A]=2-68 [UniProt coverage chain A]=40% [Name chain A]=K(+)/H(+) antiporter subunit KhtT [UniProt sequence chain A]=MNIKENDLPGIGKKFEIETRSHEKMTIIIHDDGRREIYRFNDRDPDELLSNISLDDSEARQIAAILGGMVYKPQALESIEMAFSDLIIEWFKVEKGAKSIGRTLGELDVRQNYDVTVIAIIKHNQEKLLNPGADSIIEENDTLVLSGERKHLKKLIHDFLSGEGV [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=O07535 [UniProt boundaries chain B]=2-68 [UniProt coverage chain B]=40% [Name chain B]=K(+)/H(+) antiporter subunit KhtT [UniProt sequence chain B]=MNIKENDLPGIGKKFEIETRSHEKMTIIIHDDGRREIYRFNDRDPDELLSNISLDDSEARQIAAILGGMVYKPQALESIEMAFSDLIIEWFKVEKGAKSIGRTLGELDVRQNYDVTVIAIIKHNQEKLLNPGADSIIEENDTLVLSGERKHLKKLIHDFLSGEGV [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.54 [Source organism]=Bacillus subtilis [Accession]=MF7000949 [Entry] [Entry number]=1134 [Entry name]=N-domain of the K+/H+ antiporter subunit KhtT at pH 6.5 [PDB ID]=7agw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=K(+)/H(+) antiporter subunit KhtT [Evidence level]=No contradicting information [Evidence text]=The dimeric arrangement of the N-domain is an integral part of its fold since the buried surface area is extensive (PMID:33790011). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000948,MF7000949,MF7000950 [UniProt ID chain A]=O07535 [UniProt boundaries chain A]=2-68 [UniProt coverage chain A]=40% [Name chain A]=K(+)/H(+) antiporter subunit KhtT [UniProt sequence chain A]=MNIKENDLPGIGKKFEIETRSHEKMTIIIHDDGRREIYRFNDRDPDELLSNISLDDSEARQIAAILGGMVYKPQALESIEMAFSDLIIEWFKVEKGAKSIGRTLGELDVRQNYDVTVIAIIKHNQEKLLNPGADSIIEENDTLVLSGERKHLKKLIHDFLSGEGV [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=O07535 [UniProt boundaries chain B]=2-68 [UniProt coverage chain B]=40% [Name chain B]=K(+)/H(+) antiporter subunit KhtT [UniProt sequence chain B]=MNIKENDLPGIGKKFEIETRSHEKMTIIIHDDGRREIYRFNDRDPDELLSNISLDDSEARQIAAILGGMVYKPQALESIEMAFSDLIIEWFKVEKGAKSIGRTLGELDVRQNYDVTVIAIIKHNQEKLLNPGADSIIEENDTLVLSGERKHLKKLIHDFLSGEGV [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.51 [Source organism]=Bacillus subtilis [Accession]=MF7000950 [Entry] [Entry number]=1135 [Entry name]=Carbon storage regulator protein, CsrA [PDB ID]=1y00 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Global regulator protein family [Evidence level]=No contradicting information [Evidence text]=The crystallographic packing of the CsrA structure indicates that a dimer, formed by intertwining of β-strands β1 and β5, is the biologically relevant oligomeric form (PMID:16104018). The protein behaves as a dimer during size-exclusion chromatography (PMID:16359708). Mass spectrometry of glutaraldehyde-cross-linked CsrA confirmed that CsrA exists as a dimer of identical subunits (PMID:12867454). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000951,MF7000952,MF7000953 [UniProt ID chain A]=P69913 [UniProt boundaries chain A]=1-61 [UniProt coverage chain A]=100% [Name chain A]=Carbon storage regulator [UniProt sequence chain A]=MLILTRRVGETLMIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKSQQSSY [Source organism chain A]=Escherichia coli [UniProt ID chain B]=P69913 [UniProt boundaries chain B]=1-61 [UniProt coverage chain B]=100% [Name chain B]=Carbon storage regulator [UniProt sequence chain B]=MLILTRRVGETLMIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKSQQSSY [Source organism chain B]=Escherichia coli [ExpTech]=NMR [Resolution]=N/A [Source organism]=Escherichia coli [Accession]=MF7000951 [Entry] [Entry number]=1136 [Entry name]=Putative carbon storage regulator protein, CsrAsra (Pseudomonas aeruginosa) [PDB ID]=1vpz [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Global regulator protein family [Evidence level]=No contradicting information [Evidence text]=The crystallographic packing of the CsrA structure indicates that a dimer, formed by intertwining of β-strands β1 and β5, is the biologically relevant oligomeric form (PMID:16104018). The protein behaves as a dimer during size-exclusion chromatography (PMID:16359708). Mass spectrometry of glutaraldehyde-cross-linked CsrA confirmed that CsrA exists as a dimer of identical subunits (PMID:12867454). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000951,MF7000952,MF7000953 [UniProt ID chain A]=O69078 [UniProt boundaries chain A]=1-55 [UniProt coverage chain A]=90% [Name chain A]=Translational regulator CsrA [UniProt sequence chain A]=MLILTRRVGETLMVGDDVTVTVLGVKGNQVRIGVNAPKEVAVHREEIYQRIQKEKDQEPNH [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain B]=O69078 [UniProt boundaries chain B]=1-53 [UniProt coverage chain B]=86% [Name chain B]=Translational regulator CsrA [UniProt sequence chain B]=MLILTRRVGETLMVGDDVTVTVLGVKGNQVRIGVNAPKEVAVHREEIYQRIQKEKDQEPNH [Source organism chain B]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000952 [Entry] [Entry number]=1137 [Entry name]=RmsA CsrA [PDB ID]=2bti [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Global regulator protein family [Evidence level]=No contradicting information [Evidence text]=The crystallographic packing of the CsrA structure indicates that a dimer, formed by intertwining of β-strands β1 and β5, is the biologically relevant oligomeric form (PMID:16104018). The protein behaves as a dimer during size-exclusion chromatography (PMID:16359708). Mass spectrometry of glutaraldehyde-cross-linked CsrA confirmed that CsrA exists as a dimer of identical subunits (PMID:12867454). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000951,MF7000952,MF7000953 [UniProt ID chain A]=A1JK11 [UniProt boundaries chain A]=1-58 [UniProt coverage chain A]=95% [Name chain A]=Translational regulator CsrA [UniProt sequence chain A]=MLILTRRVGETLMIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKSQPTTY [Source organism chain A]=8081) [UniProt ID chain B]=A1JK11 [UniProt boundaries chain B]=1-56 [UniProt coverage chain B]=91% [Name chain B]=Translational regulator CsrA [UniProt sequence chain B]=MLILTRRVGETLMIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKSQPTTY [Source organism chain B]=8081) [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=8081) [Accession]=MF7000953 [Entry] [Entry number]=1138 [Entry name]=Homodimerization domain of Sgt2 [PDB ID]=2lxb [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Homodimerisation domain of SGTA [Evidence level]=Indirect evidence [Evidence text]=The dimer interface is highly hydrophobic, the hydrophobic core is contributed by both monomers, mutations introduced to block dimer formation yielded no soluble protein (PMID:23297211). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000954,MF7000955,MF7000956 [UniProt ID chain A]=Q12118 [UniProt boundaries chain A]=2-72 [UniProt coverage chain A]=20% [Name chain A]=Small glutamine-rich tetratricopeptide repeat-containing protein 2 [UniProt sequence chain A]=MSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEFKGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYELAINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAKYAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDASQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAEGFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQ [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=Q12118 [UniProt boundaries chain B]=2-72 [UniProt coverage chain B]=20% [Name chain B]=Small glutamine-rich tetratricopeptide repeat-containing protein 2 [UniProt sequence chain B]=MSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEFKGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYELAINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAKYAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDASQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAEGFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQ [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000954 [Entry] [Entry number]=1139 [Entry name]=N-terminal dimerization domain of Sgt2 [PDB ID]=4asv [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Homodimerisation domain of SGTA [Evidence level]=Indirect evidence [Evidence text]=The dimer interface is highly hydrophobic, the hydrophobic core is contributed by both monomers, mutations introduced to block dimer formation yielded no soluble protein (PMID:23297211). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000954,MF7000955,MF7000956 [UniProt ID chain A]=Q12118 [UniProt boundaries chain A]=1-78 [UniProt coverage chain A]=22% [Name chain A]=Small glutamine-rich tetratricopeptide repeat-containing protein 2 [UniProt sequence chain A]=MSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEFKGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYELAINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAKYAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDASQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAEGFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQ [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=Q12118 [UniProt boundaries chain B]=1-78 [UniProt coverage chain B]=22% [Name chain B]=Small glutamine-rich tetratricopeptide repeat-containing protein 2 [UniProt sequence chain B]=MSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEFKGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYELAINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAKYAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDASQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAEGFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQ [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000955 [Entry] [Entry number]=1140 [Entry name]=N-terminal domain of SGTA [PDB ID]=4cpg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=Homodimerisation domain of SGTA [Evidence level]=Indirect evidence [Evidence text]=The dimer interface is highly hydrophobic, the hydrophobic core is contributed by both monomers, mutations introduced to block dimer formation yielded no soluble protein (PMID:23297211). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000954,MF7000955,MF7000956 [UniProt ID chain A]=O43765 [UniProt boundaries chain A]=1-69 [UniProt coverage chain A]=22% [Name chain A]=Small glutamine-rich tetratricopeptide repeat-containing protein alpha [UniProt sequence chain A]=MDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNNPQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIRSRTPSASNDDQQE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=O43765 [UniProt boundaries chain B]=1-69 [UniProt coverage chain B]=22% [Name chain B]=Small glutamine-rich tetratricopeptide repeat-containing protein alpha [UniProt sequence chain B]=MDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNNPQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIRSRTPSASNDDQQE [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7000956 [Entry] [Entry number]=1141 [Entry name]=N-terminal BAR domain IRSp53/BAIAP2 [PDB ID]=1y2o [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=I-BAR [Sequence domain]=I-BAR domain [Evidence level]=Direct evidence [Evidence text]=The IMD monomer folds as a coiled coil of three extended α-helices and a shorter C-terminal helix that is separated by an 8-residue linker from the preceding helix 3. Helix 4 packs tightly against the other three helices, and thus represents an integral part of the domain. The fold of the IMD monomer closely resembles that of the BAR (Bin/amphiphysin/Rvs) domain of arfaptin2 and amphiphysin, but due to helix 4, its dimer interface is even more extensive. Dimer is the only molecular species of IMD detected in solution (PMID:15635447). The homologous human AmphyphisinII/Bin1 and Endophilin BAR domains (N-BARs) display two-state equilibrium unfolding from the dimeric to unfolded monomeric forms (PMID:26368922, PMID:34423187), which most probably holds for the IMD dimer as well. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000957,MF7000958,MF7000959 [UniProt ID chain A]=Q9UQB8 [UniProt boundaries chain A]=1-248 [UniProt coverage chain A]=44% [Name chain A]=BAR/IMD domain-containing adapter protein 2 [UniProt sequence chain A]=MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSRNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9UQB8 [UniProt boundaries chain B]=1-248 [UniProt coverage chain B]=44% [Name chain B]=BAR/IMD domain-containing adapter protein 2 [UniProt sequence chain B]=MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSRNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Homo sapiens [Accession]=MF7000957 [Entry] [Entry number]=1142 [Entry name]=F-actin-binding BAR/IMD domain of MTSS1 [PDB ID]=2d1l [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=I-BAR [Sequence domain]=I-BAR domain [Evidence level]=Direct evidence [Evidence text]=The IMD monomer folds as a coiled coil of three extended α-helices and a shorter C-terminal helix that is separated by an 8-residue linker from the preceding helix 3. Helix 4 packs tightly against the other three helices, and thus represents an integral part of the domain. The fold of the IMD monomer closely resembles that of the BAR (Bin/amphiphysin/Rvs) domain of arfaptin2 and amphiphysin, but due to helix 4, its dimer interface is even more extensive. Dimer is the only molecular species of IMD detected in solution (PMID:15635447). The homologous human AmphyphisinII/Bin1 and Endophilin BAR domains (N-BARs) display two-state equilibrium unfolding from the dimeric to unfolded monomeric forms (PMID:26368922, PMID:34423187), which most probably holds for the IMD dimer as well. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000957,MF7000958,MF7000959 [UniProt ID chain A]=Q8R1S4 [UniProt boundaries chain A]=1-246 [UniProt coverage chain A]=32% [Name chain A]=Protein MTSS 1 [UniProt sequence chain A]=MEAVIEKECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKNKSSDTLKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLPSSSEQVILDLKGSDYSWSYQTPPSSPSTTMSRKSSVCSSLNSVNSSDSRSSGSHSHSPSSHYRYRSSNLAQQAPVRLSSVSSHDSGFISQDAFQSKSPSPMPPEAANQLSNGFSHCSLSSESHAGPVGAGPFPHCLPASRLLPRVTSVHLPDYAHYYTIGPGMFPSSQIPSWKDWAKPGPYDQPLVNTLQRRKEKREPDSNGGGPTTTGGPPAGAEEAQRPRSMTVSAATRPGEEMAACEELTLALSRGLQLDVQRSSRDSLQCSSGYSTQTTTPCCSEDTIPSQVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRFS [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q8R1S4 [UniProt boundaries chain B]=1-242 [UniProt coverage chain B]=31% [Name chain B]=Protein MTSS 1 [UniProt sequence chain B]=MEAVIEKECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKNKSSDTLKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLPSSSEQVILDLKGSDYSWSYQTPPSSPSTTMSRKSSVCSSLNSVNSSDSRSSGSHSHSPSSHYRYRSSNLAQQAPVRLSSVSSHDSGFISQDAFQSKSPSPMPPEAANQLSNGFSHCSLSSESHAGPVGAGPFPHCLPASRLLPRVTSVHLPDYAHYYTIGPGMFPSSQIPSWKDWAKPGPYDQPLVNTLQRRKEKREPDSNGGGPTTTGGPPAGAEEAQRPRSMTVSAATRPGEEMAACEELTLALSRGLQLDVQRSSRDSLQCSSGYSTQTTTPCCSEDTIPSQVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRFS [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.85 [Source organism]=Mus musculus [Accession]=MF7000958 [Entry] [Entry number]=1143 [Entry name]=I-BAR domain of PinkBAR [PDB ID]=3ok8 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=BAR domains [Subclass]=I-BAR [Sequence domain]=I-BAR domain [Evidence level]=Direct evidence [Evidence text]=The IMD monomer folds as a coiled coil of three extended α-helices and a shorter C-terminal helix that is separated by an 8-residue linker from the preceding helix 3. Helix 4 packs tightly against the other three helices, and thus represents an integral part of the domain. The fold of the IMD monomer closely resembles that of the BAR (Bin/amphiphysin/Rvs) domain of arfaptin2 and amphiphysin, but due to helix 4, its dimer interface is even more extensive. Dimer is the only molecular species of IMD detected in solution (PMID:15635447). The homologous human AmphyphisinII/Bin1 and Endophilin BAR domains (N-BARs) display two-state equilibrium unfolding from the dimeric to unfolded monomeric forms (PMID:26368922, PMID:34423187), which most probably holds for the IMD dimer as well. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000957,MF7000958,MF7000959 [UniProt ID chain A]=Q80Y61 [UniProt boundaries chain A]=2-220 [UniProt coverage chain A]=41% [Name chain A]=BAR/IMD domain-containing adapter protein 2-like 2 [UniProt sequence chain A]=MAPEMDQFYRSTMAIYKSIMEQFNPALENLVYLGNNYLRAFHALSEAAEVYFSAIQKIGEQALQSSTSQILGEILVQMSDTQRHLNSDLEVVVQTFHGDLLQHMEKNTKLDMQFIKDSCQHYEIEYRHRAANLEKCMSELWRMERKRDKNAREMKESVNRLHAQMQAFVSESKRAAELEEKRRYRFLAEKHLLLSNTFLQFLGRARGMLQNRVLLWKEQSEASRSPSRAHSPGLLGPALGPPYPSGRLTPTRLDMPPRPLGEYGSPRSRHGSGSYGPEPAEARSASQLEPDRRSLPRTPSASSLYASSTQRSRSNSFGERLGGGGARRVRALVSHSEGANHTLLRFSAGDVVEVLVPEAQNGWLYGKLEGSSASGWFPEAYVKPVEEIPVNPMNPVAPMNSMAPMSPMNELPSRSYPLRGSHSLDDLLDRPGNPTASSEYWDSQSRSRTPSRVPSRAPSPAPPPLPSSRRSSVGSMGAATDVKKLMSWEQNPPELFPRGTNPFATVKLRPTVTNDRSAPLIR [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q80Y61 [UniProt boundaries chain B]=2-220 [UniProt coverage chain B]=41% [Name chain B]=BAR/IMD domain-containing adapter protein 2-like 2 [UniProt sequence chain B]=MAPEMDQFYRSTMAIYKSIMEQFNPALENLVYLGNNYLRAFHALSEAAEVYFSAIQKIGEQALQSSTSQILGEILVQMSDTQRHLNSDLEVVVQTFHGDLLQHMEKNTKLDMQFIKDSCQHYEIEYRHRAANLEKCMSELWRMERKRDKNAREMKESVNRLHAQMQAFVSESKRAAELEEKRRYRFLAEKHLLLSNTFLQFLGRARGMLQNRVLLWKEQSEASRSPSRAHSPGLLGPALGPPYPSGRLTPTRLDMPPRPLGEYGSPRSRHGSGSYGPEPAEARSASQLEPDRRSLPRTPSASSLYASSTQRSRSNSFGERLGGGGARRVRALVSHSEGANHTLLRFSAGDVVEVLVPEAQNGWLYGKLEGSSASGWFPEAYVKPVEEIPVNPMNPVAPMNSMAPMSPMNELPSRSYPLRGSHSLDDLLDRPGNPTASSEYWDSQSRSRTPSRVPSRAPSPAPPPLPSSRRSSVGSMGAATDVKKLMSWEQNPPELFPRGTNPFATVKLRPTVTNDRSAPLIR [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Mus musculus [Accession]=MF7000959 [Entry] [Entry number]=1144 [Entry name]=YtrA, a GntR-family transcription factor (Shewanella oneidensis) [PDB ID]=6sbs [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Bacterial regulatory proteins, gntR family [Evidence level]=Indirect evidence [Evidence text]=YtrA has a multi-subdomain structure. Each monomeric unit displays an N-terminal DNA-binding domain harboring the typical GntR-like wHTH motif (α1–α3) and a short C-terminal E-O domain, consisting of two α helices (α4–α5) that mediate dimerization, which is a typical feature for YtrA-like regulators. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000152,MF7000960 [UniProt ID chain A]=Q4J7S4 [UniProt boundaries chain A]=3-100 [UniProt coverage chain A]=80% [Name chain A]=Regulatory protein [UniProt sequence chain A]=MTSIIKIDLESKTPIYKQIADQIIELIAKGELKPGDKLPSIRELASMLGVNMLTVNKAYNYLVDEGFIVVQKRRYVVKSEVRDESWRNMLRVIIYRALASNMSKDEIVNEINRVVSEVNSK [Source organism chain A]=15157 / NCIMB 11770) [UniProt ID chain B]=Q4J7S4 [UniProt boundaries chain B]=5-120 [UniProt coverage chain B]=95% [Name chain B]=Regulatory protein [UniProt sequence chain B]=MTSIIKIDLESKTPIYKQIADQIIELIAKGELKPGDKLPSIRELASMLGVNMLTVNKAYNYLVDEGFIVVQKRRYVVKSEVRDESWRNMLRVIIYRALASNMSKDEIVNEINRVVSEVNSK [Source organism chain B]=15157 / NCIMB 11770) [ExpTech]=X-ray [Resolution]=2.80 [Source organism]=15157 / NCIMB 11770) [Accession]=MF7000960 [Entry] [Entry number]=1145 [Entry name]=Lethocerus Myosin II [PDB ID]=7kog [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Myosin heavy chain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:33782130). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=MF7000961,MF7000962 [UniProt ID chain B]=A0A221IRH5 [UniProt boundaries chain B]=854-1930 [UniProt coverage chain B]=54% [Name chain B]=Myosin heavy chain isoform Mhc_X1 [UniProt sequence chain B]=MPGSKPTKTEEEDDPTPYLFVSLEQKRIDQTKPYDAKKACWVPDEHEGFVQGEIRGTKGDIVSVHLPNGETKDFKKDQVGQVNPPKFEKCEDMSNLTYLNDASVLYNLKQRYYNKLIYTYSGLFCVAINPYKRFPVYTMRCAKLYRGKRRNEVPPHIFAISDGAYVNMLTNKENQSMLITGESGAGKTENTKKVIAYFATVGASTKKEEAASAASQKKGTLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPSGKLAGADIETYLLEKARVISQQSLERSYHIFYQVMSGAVPGVKELCLLSNDIYEYNYVSQGKVTIPSVDDGEEFQATDQAFDVLGFTQEEKDDIYKITASVMHMGCMKFKQRGREEQAEADGTAEGERVAKLLGLEAADLYKNLLKPRIKVGNEFVTQGRNLNQVIYSVGALSKGVFDRLFKFLVKKCNETLDTKQKRQHFIGVLDIAGFEIFDFNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYTREGITWAFIDFGMDLVACIDLIEKPMGILSILEEESMFPKATDKTFEEKLMNNHLGKSPNFQKPKPPKPGCQAAHFAISHYAGVVSYNLTGWLEKNKDPLNDTVVDQFKKGSNKLLVEIFADHPGQSGAPEAGGGGKGGRGKKGGGFATVSSSYKEQLNNLMTTLKSTQPHFVRCIIPNELKQPGLIDSHLVMHQLTCNGVLEGIRICRKGFPNRMVYPDFKLRYMILAPATMAAEPDPKKAADKCLKEVGLESETYRIGHTKVFFRAGVLGQLEEMRDERLSKIIGWMQSHIRGYLARKQFKKYQDQRLSLQVVQRNLRKYMALRTWPWWKMWTKVKPLLNVANVEEEMRKLEELVATTQAALEKEEKARKEVEALNAKLIQEKTDLLRNLEGEKGSISSIQEKAAKLQAQKSDLESQLMDTQERLQQEEDNRNQMFQQKKKLEQEVGGLKKDIEDLELSLQKSDQDKASKDHQIRNLNDEIAHQDELINKLNKEKKMQGEHTQKTAEELQASEDKVNHLTKVKAKLEQTLDELEDSLEREKKLRGDVEKAKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKEIASLTAKLEDEQSIVSKTQKQIKELQSRIEELEEEVEAERQARGKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAEMSKLRRDLEESNIQHESTLANLRKKHNDAVSEMGEQIDQLNKLKTKAEHDRTHVQNDLNNTRHALDQMCREKAATEKIAKQLQHQVNEIQGKLDEANRTLNDFDSAKKKLSIENSDLLRQLEEAESQVSQLSKIKVSLTTQLEDTKRLADEEARERATLLGKFRNLEHDLDNIREQLEEEAEGKADIQRQLSKANAEAQLWRTKYESEGVARAEELEEAKRKLQARLAEAEETIESLNQKVIALEKTKQRLATEVEDLQLEVDRATAIANAAEKKAKAIDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEAQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKQKKRLEVEKDELQAALEEAEAALEQEENKVLRSQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANSEAQKTIKKYQQQLKDVQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELGDAHEQINELAAQATSASAAKRKLEGELQTLHADLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALETQIKELQIRLDEAETNALKGGKKAIAKLEQRVRELENELDGEQRRHADAQKNLRKSERRIKELSFQADEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAIAKFRTKGGRAGSAARAMSPVAHRPPVKHPLDGSTFPPRFDLHEDMM [Source organism chain B]=Lethocerus indicus [UniProt ID chain A]=A0A221IRH5 [UniProt boundaries chain A]=854-1930 [UniProt coverage chain A]=54% [Name chain A]=Myosin heavy chain isoform Mhc_X1 [UniProt sequence chain A]=MPGSKPTKTEEEDDPTPYLFVSLEQKRIDQTKPYDAKKACWVPDEHEGFVQGEIRGTKGDIVSVHLPNGETKDFKKDQVGQVNPPKFEKCEDMSNLTYLNDASVLYNLKQRYYNKLIYTYSGLFCVAINPYKRFPVYTMRCAKLYRGKRRNEVPPHIFAISDGAYVNMLTNKENQSMLITGESGAGKTENTKKVIAYFATVGASTKKEEAASAASQKKGTLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPSGKLAGADIETYLLEKARVISQQSLERSYHIFYQVMSGAVPGVKELCLLSNDIYEYNYVSQGKVTIPSVDDGEEFQATDQAFDVLGFTQEEKDDIYKITASVMHMGCMKFKQRGREEQAEADGTAEGERVAKLLGLEAADLYKNLLKPRIKVGNEFVTQGRNLNQVIYSVGALSKGVFDRLFKFLVKKCNETLDTKQKRQHFIGVLDIAGFEIFDFNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYTREGITWAFIDFGMDLVACIDLIEKPMGILSILEEESMFPKATDKTFEEKLMNNHLGKSPNFQKPKPPKPGCQAAHFAISHYAGVVSYNLTGWLEKNKDPLNDTVVDQFKKGSNKLLVEIFADHPGQSGAPEAGGGGKGGRGKKGGGFATVSSSYKEQLNNLMTTLKSTQPHFVRCIIPNELKQPGLIDSHLVMHQLTCNGVLEGIRICRKGFPNRMVYPDFKLRYMILAPATMAAEPDPKKAADKCLKEVGLESETYRIGHTKVFFRAGVLGQLEEMRDERLSKIIGWMQSHIRGYLARKQFKKYQDQRLSLQVVQRNLRKYMALRTWPWWKMWTKVKPLLNVANVEEEMRKLEELVATTQAALEKEEKARKEVEALNAKLIQEKTDLLRNLEGEKGSISSIQEKAAKLQAQKSDLESQLMDTQERLQQEEDNRNQMFQQKKKLEQEVGGLKKDIEDLELSLQKSDQDKASKDHQIRNLNDEIAHQDELINKLNKEKKMQGEHTQKTAEELQASEDKVNHLTKVKAKLEQTLDELEDSLEREKKLRGDVEKAKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKEIASLTAKLEDEQSIVSKTQKQIKELQSRIEELEEEVEAERQARGKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAEMSKLRRDLEESNIQHESTLANLRKKHNDAVSEMGEQIDQLNKLKTKAEHDRTHVQNDLNNTRHALDQMCREKAATEKIAKQLQHQVNEIQGKLDEANRTLNDFDSAKKKLSIENSDLLRQLEEAESQVSQLSKIKVSLTTQLEDTKRLADEEARERATLLGKFRNLEHDLDNIREQLEEEAEGKADIQRQLSKANAEAQLWRTKYESEGVARAEELEEAKRKLQARLAEAEETIESLNQKVIALEKTKQRLATEVEDLQLEVDRATAIANAAEKKAKAIDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEAQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKQKKRLEVEKDELQAALEEAEAALEQEENKVLRSQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANSEAQKTIKKYQQQLKDVQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELGDAHEQINELAAQATSASAAKRKLEGELQTLHADLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALETQIKELQIRLDEAETNALKGGKKAIAKLEQRVRELENELDGEQRRHADAQKNLRKSERRIKELSFQADEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAIAKFRTKGGRAGSAARAMSPVAHRPPVKHPLDGSTFPPRFDLHEDMM [Source organism chain A]=Lethocerus indicus [ExpTech]=Electron Microscopy [Resolution]=4.25 [Source organism]=Lethocerus indicus [Accession]=MF7000961 [Entry] [Entry number]=1146 [Entry name]=Myosin heavy chain (Drosophila melanogaster) [PDB ID]=8u95 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=Myosin heavy chain [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:37834384). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000961,MF7000962 [UniProt ID chain A]=M9ND95 [UniProt boundaries chain A]=913-1921 [UniProt coverage chain A]=51% [Name chain A]=Myosin heavy chain, isoform U [UniProt sequence chain A]=MPKPVANQEDEDPTPYLFVSLEQRRIDQSKPYDSKKSCWIPDEKEGYLLGEIKATKGDIVSVGLQGGETRDLKKDLLQQVNPPKYEKAEDMSNLTYLNDASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFRAGVLGQMEEFRDERLGKIMSWMQAWARGYLSRKGFKKLQEQRVALKVVQRNLRKYLQLRTWPWYKLWQKVKPLLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSVGRGASPAPTASKGRKSALLEQ [Source organism chain A]=Drosophila melanogaster [UniProt ID chain B]=M9ND95 [UniProt boundaries chain B]=913-1921 [UniProt coverage chain B]=51% [Name chain B]=Myosin heavy chain, isoform U [UniProt sequence chain B]=MPKPVANQEDEDPTPYLFVSLEQRRIDQSKPYDSKKSCWIPDEKEGYLLGEIKATKGDIVSVGLQGGETRDLKKDLLQQVNPPKYEKAEDMSNLTYLNDASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYQILNPKGIKGIEDPKKCTKVLIESTELNDDQYRLGNTKVFFRAGVLGQMEEFRDERLGKIMSWMQAWARGYLSRKGFKKLQEQRVALKVVQRNLRKYLQLRTWPWYKLWQKVKPLLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSVGRGASPAPTASKGRKSALLEQ [Source organism chain B]=Drosophila melanogaster [ExpTech]=Electron Microscopy [Resolution]=4.70 [Source organism]=Drosophila melanogaster [Accession]=MF7000962 [Entry] [Entry number]=1147 [Entry name]=Human nac dimerization domain [PDB ID]=3lkx [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=NAC domain [Evidence level]=Direct evidence [Evidence text]=The dimerization of NACα and NACβ buries 36% of the total solvent accessible surface area of the monomers, which is huge. Hydrogen bonding in two joint β-sheets and a hydrophobic core between the two sheets are the main driving force in dimerization. Therefore, an isolated NAC subunit of either NACα or NACβ is unlikely to stay as stable, soluble monomers in solution because of unsaturated hydrogen bonding potential and extensively exposed hydrophobic surface. Accordingly, αNAC and βNAC form a stable heterodimer in solution (PMID:21203952). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000963,MF7000964 [UniProt ID chain A]=P20290 [UniProt boundaries chain A]=97-162 [UniProt coverage chain A]=32% [Name chain A]=Transcription factor BTF3 [UniProt sequence chain A]=MRRTGAPAQADSRGRGRARGGCPGGEATLSQPPPRGGTRGQEPQMKETIMNQEKLAKLQAQVRIGGKGTARRKKKVVHRTATADDKKLQFSLKKLGVNNISGIEEVNMFTNQGTVIHFNNPKVQASLAANTFTITGHAETKQLTEMLPSILNQLGADSLTSLRRLAEALPKQSVDGKAPLATGEDDDDEVPDLVENFDEASKNEAN [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q13765 [UniProt boundaries chain B]=84-136 [UniProt coverage chain B]=24% [Name chain B]=Nascent polypeptide-associated complex subunit alpha [UniProt sequence chain B]=MPGEATETVPATEQELPQPQAETGSGTESDSDESVPELEEQDSTQATTQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAMSKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIEDLSQQAQLAAAEKFKVQGEAVSNIQENTQTPTVQEESEEEEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELTM [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Homo sapiens [Accession]=MF7000963 [Entry] [Entry number]=1148 [Entry name]=NAC domains of human NAC [PDB ID]=3mcb [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=NAC domain [Evidence level]=Direct evidence [Evidence text]=The dimerization of NACα and NACβ buries 36% of the total solvent accessible surface area of the monomers, which is huge. Hydrogen bonding in two joint β-sheets and a hydrophobic core between the two sheets are the main driving force in dimerization. Therefore, an isolated NAC subunit of either NACα or NACβ is unlikely to stay as stable, soluble monomers in solution because of unsaturated hydrogen bonding potential and extensively exposed hydrophobic surface. Accordingly, αNAC and βNAC form a stable heterodimer in solution (PMID:21203952). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000963,MF7000964 [UniProt ID chain A]=Q13765 [UniProt boundaries chain A]=79-132 [UniProt coverage chain A]=25% [Name chain A]=Nascent polypeptide-associated complex subunit alpha [UniProt sequence chain A]=MPGEATETVPATEQELPQPQAETGSGTESDSDESVPELEEQDSTQATTQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAMSKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIEDLSQQAQLAAAEKFKVQGEAVSNIQENTQTPTVQEESEEEEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELTM [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P20290 [UniProt boundaries chain B]=97-154 [UniProt coverage chain B]=28% [Name chain B]=Transcription factor BTF3 [UniProt sequence chain B]=MRRTGAPAQADSRGRGRARGGCPGGEATLSQPPPRGGTRGQEPQMKETIMNQEKLAKLQAQVRIGGKGTARRKKKVVHRTATADDKKLQFSLKKLGVNNISGIEEVNMFTNQGTVIHFNNPKVQASLAANTFTITGHAETKQLTEMLPSILNQLGADSLTSLRRLAEALPKQSVDGKAPLATGEDDDDEVPDLVENFDEASKNEAN [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Homo sapiens [Accession]=MF7000964 [Entry] [Entry number]=1149 [Entry name]=Human dynein light chain Dnlc2A [PDB ID]=2hz5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Roadblock/LC7 domain [Evidence level]=Indirect evidence [Evidence text]=Roadblock/LC7 domains are dimeric in solution (PMID:16083906). There are two layers in the dimer structure. One layer is formed by the two a2/a02, and the other by the continuous, antiparallel 10-stranded sheet (PMID:16970917). Dimerization is mediated by the simultaneous pairing of the edge b-strand (b3) of a five-stranded antiparallel b-sheet and by a seven turn a-helix (a2) that lies diagonally across the surface of the sheet. The dimer has a large interface with a large number of hydrophobic interactions (PMID:16083906). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000965,MF7000966 [UniProt ID chain A]=Q9NP97 [UniProt boundaries chain A]=5-94 [UniProt coverage chain A]=93% [Name chain A]=Dynein light chain roadblock-type 1 [UniProt sequence chain A]=MAEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYASLMHSFILKARSTVRDIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9NP97 [UniProt boundaries chain B]=8-95 [UniProt coverage chain B]=91% [Name chain B]=Dynein light chain roadblock-type 1 [UniProt sequence chain B]=MAEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYASLMHSFILKARSTVRDIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Homo sapiens [Accession]=MF7000965 [Entry] [Entry number]=1150 [Entry name]=MglB, mutant (R124A, E127A) [PDB ID]=3t1x [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Roadblock/LC7 domain [Evidence level]=Indirect evidence [Evidence text]=Roadblock/LC7 domains are dimeric in solution (PMID:16083906). There are two layers in the dimer structure. One layer is formed by the two a2/a02, and the other by the continuous, antiparallel 10-stranded sheet (PMID:16970917). Dimerization is mediated by the simultaneous pairing of the edge b-strand (b3) of a five-stranded antiparallel b-sheet and by a seven turn a-helix (a2) that lies diagonally across the surface of the sheet. The dimer has a large interface with a large number of hydrophobic interactions (PMID:16083906). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000965,MF7000966 [UniProt ID chain A]=Q5SJ83 [UniProt boundaries chain A]=6-139 [UniProt coverage chain A]=82% [Name chain A]=Probable gliding protein (MglB) [UniProt sequence chain A]=MVEPSLVLYGAPYERAVEVLEETLRETGARYALLIDRKGFVLAHKEALWAPKPPPLDTLATLVAGNAAATQALAKLLGEARFQEEVHQGERMGLYVDEAGEHALLVLVFDETAPLGKVKLHGKRAAEALARIAEEALANPPRLALDTEYREGAEALLDDLLRN [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SJ83 [UniProt boundaries chain A-2]=6-139 [UniProt coverage chain A-2]=82% [Name chain A-2]=Probable gliding protein (MglB) [UniProt sequence chain A-2]=MVEPSLVLYGAPYERAVEVLEETLRETGARYALLIDRKGFVLAHKEALWAPKPPPLDTLATLVAGNAAATQALAKLLGEARFQEEVHQGERMGLYVDEAGEHALLVLVFDETAPLGKVKLHGKRAAEALARIAEEALANPPRLALDTEYREGAEALLDDLLRN [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=2.91 [Source organism]=Thermus thermophilus [Accession]=MF7000966 [Entry] [Entry number]=1151 [Entry name]=Tet repressor class H with 5a,6- anhydrotetracycline-Mg [PDB ID]=2vpr [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=DNA-binding HTH domain and helical dimerization domain [Sequence domain]=Tetracyclin repressor-like, C-terminal domain [Evidence level]=Indirect evidence [Evidence text]=TetR-type helix-turn-helix (HTH) type DNA-binding domain plus C-terminal dimerization helices. The center of the core domain is a four-helix bundle involving helices 8, 8′, 10, and 10′. The [Tc:Mg] + binding sites are formed by α5–α9, α8′ and by α5′–α9′, α8, so both monomers contribute to both binding sites. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000967,MF7000968 [UniProt ID chain A]=P51561 [UniProt boundaries chain A]=2-207 [UniProt coverage chain A]=99% [Name chain A]=Tetracycline repressor protein class H [UniProt sequence chain A]=MAKLDKEQVIDDALILLNEVGIEGLTTRNVAQKIGVEQPTLYWHVKNKRALLDALAETILQKHHHHVLPLPNETWQDFLRNNAKSFRQALLMYRDGGKIHAGTRPSESQFETSEQQLQFLCDAGFSLSQAVYALSSIAHFTLGSVLETQEHQESQKEREKVETDTVAYPPLLTQAVAIMDSDNGDAAFLFVLDVMISGLETVLKSAK [Source organism chain A]=Pasteurella multocida [UniProt ID chain A-2]=P51561 [UniProt boundaries chain A-2]=2-207 [UniProt coverage chain A-2]=99% [Name chain A-2]=Tetracycline repressor protein class H [UniProt sequence chain A-2]=MAKLDKEQVIDDALILLNEVGIEGLTTRNVAQKIGVEQPTLYWHVKNKRALLDALAETILQKHHHHVLPLPNETWQDFLRNNAKSFRQALLMYRDGGKIHAGTRPSESQFETSEQQLQFLCDAGFSLSQAVYALSSIAHFTLGSVLETQEHQESQKEREKVETDTVAYPPLLTQAVAIMDSDNGDAAFLFVLDVMISGLETVLKSAK [Source organism chain A-2]=Pasteurella multocida [ExpTech]=X-ray [Resolution]=2.49 [Source organism]=Pasteurella multocida [Accession]=MF7000967 [Entry] [Entry number]=1152 [Entry name]=Transcriptional regulator Rv1219c (Mycobacterium tuberculosis) [PDB ID]=4nn1 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=DNA-binding HTH domain and helical dimerization domain [Sequence domain]=Tetracyclin repressor-like, C-terminal domain [Evidence level]=Indirect evidence [Evidence text]=TetR-type helix-turn-helix (HTH) type DNA-binding domain plus C-terminal dimerization helices. The center of the core domain is a four-helix bundle involving helices 8, 8′, 10, and 10′. The [Tc:Mg] + binding sites are formed by α5–α9, α8′ and by α5′–α9′, α8, so both monomers contribute to both binding sites. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000967,MF7000968 [UniProt ID chain A]=O86312 [UniProt boundaries chain A]=6-210 [UniProt coverage chain A]=96% [Name chain A]=HTH-type transcriptional regulatory protein RaaS [UniProt sequence chain A]=MRSADLTAHARIREAAIEQFGRHGFGVGLRAIAEAAGVSAALVIHHFGSKEGLRKACDDFVAEEIRSSKAAALKSNDPTTWLAQMAEIESYAPLMAYLVRSMQSGGELAKMLWQKMIDNAEEYLDEGVRAGTVKPSRDPRARARFLAITGGGGFLLYLQMHENPTDLRAALRDYAHDMVLPSLEVYTEGLLADRAMYEAFLAEAQQGEAHVG [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=O86312 [UniProt boundaries chain A-2]=6-210 [UniProt coverage chain A-2]=96% [Name chain A-2]=HTH-type transcriptional regulatory protein RaaS [UniProt sequence chain A-2]=MRSADLTAHARIREAAIEQFGRHGFGVGLRAIAEAAGVSAALVIHHFGSKEGLRKACDDFVAEEIRSSKAAALKSNDPTTWLAQMAEIESYAPLMAYLVRSMQSGGELAKMLWQKMIDNAEEYLDEGVRAGTVKPSRDPRARARFLAITGGGGFLLYLQMHENPTDLRAALRDYAHDMVLPSLEVYTEGLLADRAMYEAFLAEAQQGEAHVG [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=2.99 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000968 [Entry] [Entry number]=1153 [Entry name]=Mouse lipin-1 M-Lip domain [PDB ID]=7kih [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Lipin/Ned1/Smp2 multi-domain protein middle domain [Evidence level]=Direct evidence [Evidence text]=Thermal shift assay assessed by differential scanning fluorimetry fitted a Boltzmann sigmoid (PMID:34354069). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000969,MF7000970 [UniProt ID chain A]=Q91ZP3 [UniProt boundaries chain A]=494-581 [UniProt coverage chain A]=9% [Name chain A]=Phosphatidate phosphatase LPIN1 [UniProt sequence chain A]=MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVIRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKLGDNGEAFFVQETDNDQEIIPMYLATSPILSEGAARMESQLKRNSVDRIRCLDPTTAAQGLPPSDTPSTGSLGKKRRKRRRKAQLDNLKRDDNVNSSEDEDMFPIEMSSDEDTAPMDGSRTLPNDVPPFQDDIPKENFPSISTHPQSASYPSSDREWSPSPSSLVDCQRTPPHLAEGVLSSSCPLQSCHFHASESPSGSRPSTPKSDSELVSKSADRLTPKNNLEMLWLWGELPQAAKSSSPHKMKESSPLGSRKTPDKMNFQAIHSESSDTFSDQSPTMARGLLIHQSKAQTEMQFVNEEDLESLGAAAPPSPVAEELKAPYPNTAQSSSKTDSPSRKKDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPGGLPKQASDNGARSANQSPQSVGGSGIDSGVESTSDSLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKVGNKYYNWTTAAPLLLAMQAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGRNATIKEESKPEQCLTGKGHNTGEQPAQLGLATRIKHESSSSDEEHAAAKPSGSSHLSLLSNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFPLLKRSHSCDFPCSDTFSNFTFWREPLPPFENQDMHSASA [Source organism chain A]=Mus musculus [UniProt ID chain A-2]=Q91ZP3 [UniProt boundaries chain A-2]=494-581 [UniProt coverage chain A-2]=9% [Name chain A-2]=Phosphatidate phosphatase LPIN1 [UniProt sequence chain A-2]=MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVIRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKLGDNGEAFFVQETDNDQEIIPMYLATSPILSEGAARMESQLKRNSVDRIRCLDPTTAAQGLPPSDTPSTGSLGKKRRKRRRKAQLDNLKRDDNVNSSEDEDMFPIEMSSDEDTAPMDGSRTLPNDVPPFQDDIPKENFPSISTHPQSASYPSSDREWSPSPSSLVDCQRTPPHLAEGVLSSSCPLQSCHFHASESPSGSRPSTPKSDSELVSKSADRLTPKNNLEMLWLWGELPQAAKSSSPHKMKESSPLGSRKTPDKMNFQAIHSESSDTFSDQSPTMARGLLIHQSKAQTEMQFVNEEDLESLGAAAPPSPVAEELKAPYPNTAQSSSKTDSPSRKKDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPGGLPKQASDNGARSANQSPQSVGGSGIDSGVESTSDSLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKVGNKYYNWTTAAPLLLAMQAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGRNATIKEESKPEQCLTGKGHNTGEQPAQLGLATRIKHESSSSDEEHAAAKPSGSSHLSLLSNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFPLLKRSHSCDFPCSDTFSNFTFWREPLPPFENQDMHSASA [Source organism chain A-2]=Mus musculus [ExpTech]=X-ray [Resolution]=1.47 [Source organism]=Mus musculus [Accession]=MF7000969 [Entry] [Entry number]=1154 [Entry name]=Mouse lipin-1 M-Lip domain with Zn [PDB ID]=7kil [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=Lipin/Ned1/Smp2 multi-domain protein middle domain [Evidence level]=Direct evidence [Evidence text]=Thermal shift assay assessed by differential scanning fluorimetry fitted a Boltzmann sigmoid (PMID:34354069). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000969,MF7000970 [UniProt ID chain A]=Q91ZP3 [UniProt boundaries chain A]=494-581 [UniProt coverage chain A]=9% [Name chain A]=Phosphatidate phosphatase LPIN1 [UniProt sequence chain A]=MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVIRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKLGDNGEAFFVQETDNDQEIIPMYLATSPILSEGAARMESQLKRNSVDRIRCLDPTTAAQGLPPSDTPSTGSLGKKRRKRRRKAQLDNLKRDDNVNSSEDEDMFPIEMSSDEDTAPMDGSRTLPNDVPPFQDDIPKENFPSISTHPQSASYPSSDREWSPSPSSLVDCQRTPPHLAEGVLSSSCPLQSCHFHASESPSGSRPSTPKSDSELVSKSADRLTPKNNLEMLWLWGELPQAAKSSSPHKMKESSPLGSRKTPDKMNFQAIHSESSDTFSDQSPTMARGLLIHQSKAQTEMQFVNEEDLESLGAAAPPSPVAEELKAPYPNTAQSSSKTDSPSRKKDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPGGLPKQASDNGARSANQSPQSVGGSGIDSGVESTSDSLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKVGNKYYNWTTAAPLLLAMQAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGRNATIKEESKPEQCLTGKGHNTGEQPAQLGLATRIKHESSSSDEEHAAAKPSGSSHLSLLSNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFPLLKRSHSCDFPCSDTFSNFTFWREPLPPFENQDMHSASA [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q91ZP3 [UniProt boundaries chain B]=496-581 [UniProt coverage chain B]=9% [Name chain B]=Phosphatidate phosphatase LPIN1 [UniProt sequence chain B]=MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVIRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKLGDNGEAFFVQETDNDQEIIPMYLATSPILSEGAARMESQLKRNSVDRIRCLDPTTAAQGLPPSDTPSTGSLGKKRRKRRRKAQLDNLKRDDNVNSSEDEDMFPIEMSSDEDTAPMDGSRTLPNDVPPFQDDIPKENFPSISTHPQSASYPSSDREWSPSPSSLVDCQRTPPHLAEGVLSSSCPLQSCHFHASESPSGSRPSTPKSDSELVSKSADRLTPKNNLEMLWLWGELPQAAKSSSPHKMKESSPLGSRKTPDKMNFQAIHSESSDTFSDQSPTMARGLLIHQSKAQTEMQFVNEEDLESLGAAAPPSPVAEELKAPYPNTAQSSSKTDSPSRKKDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPGGLPKQASDNGARSANQSPQSVGGSGIDSGVESTSDSLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKVGNKYYNWTTAAPLLLAMQAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGRNATIKEESKPEQCLTGKGHNTGEQPAQLGLATRIKHESSSSDEEHAAAKPSGSSHLSLLSNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFPLLKRSHSCDFPCSDTFSNFTFWREPLPPFENQDMHSASA [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Mus musculus [Accession]=MF7000970 [Entry] [Entry number]=1155 [Entry name]=Rabbit ZAD-domain of ZNF_276 protein [PDB ID]=7ppp [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, AD-type [Sequence domain]=Zinc-finger associated domain (zf-AD) [Evidence level]=Direct evidence [Evidence text]=A common mechanism of dimerization of ZADs is dominated by hydrophobic interactions, which are part of one large hydrophobic core originating from the union of hydrophobic cores of adjacent monomers. The monomeric structure has two nearly perpendicular α-helices (α1 and α2) as well as looped regions knotted by a zinc ion. The helices of the monomers are definitely involved in helix packing interactions (PMID:35580610). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000971,MF7000432 [UniProt ID chain A]=A0A5F9DAT3 [UniProt boundaries chain A]=128-212 [UniProt coverage chain A]=13% [Name chain A]=Zinc finger protein 276 [UniProt sequence chain A]=MHHLFAHRGLVRGKPGVPYRDLGTERWVSASCLCLTRALLQGAPMASSLGSLGLGPSHHLPVEPMLSEALPFLALPRTPWQMLSVPGCLLSSPEGRVAVKGHFCWSPLLWHSDCWEAFRAGRALAMGHCRLCHGKFSSRSLRSISDRASGDSAERPFPGERVFVRDFQRLLGVAVHQDPALSQFVCRNCHAQFYQCHSLLESFLQRVNVSPMGQRKPCAKVGAQPPTVAEEGAFLGDLITSSSRCLHSLVGWVHGHAASCGALPTLQRTLASEYCGVIQAMWGCDQGHNYTMDTDSSCRALLLDSALSVKWAWDKEMAPQLTHSQASSPSGTAPQVSQGRGTTLPSMDVAPPPDGNPMGPGPGPPPQPSPPLIGAPEIARVTMTTPGSSILSPQMNSFEPYSEKKVSGKKSESKEAKKTEEPKIRKKPGPKPGWKKQLRSEREELPTIYKCPYQGCTAVYRGADGMKKHIKEHHEEVRERPCPHPGCNKVFMIDRYLQRHVKLIHTEVRNYICDECGQTFKQRKHLLVHQMRHSGAKPLQCEVCGFQCRQRASLKYHMTKHKAETELDFACDQCGRRFEKAHNLNVHMSMVHPLTQTQDKALPLEAEPPPGPPHPSGTTEGQAVKPEPT [Source organism chain A]=Oryctolagus cuniculus [UniProt ID chain B]=A0A5F9DAT3 [UniProt boundaries chain B]=128-212 [UniProt coverage chain B]=13% [Name chain B]=Zinc finger protein 276 [UniProt sequence chain B]=MHHLFAHRGLVRGKPGVPYRDLGTERWVSASCLCLTRALLQGAPMASSLGSLGLGPSHHLPVEPMLSEALPFLALPRTPWQMLSVPGCLLSSPEGRVAVKGHFCWSPLLWHSDCWEAFRAGRALAMGHCRLCHGKFSSRSLRSISDRASGDSAERPFPGERVFVRDFQRLLGVAVHQDPALSQFVCRNCHAQFYQCHSLLESFLQRVNVSPMGQRKPCAKVGAQPPTVAEEGAFLGDLITSSSRCLHSLVGWVHGHAASCGALPTLQRTLASEYCGVIQAMWGCDQGHNYTMDTDSSCRALLLDSALSVKWAWDKEMAPQLTHSQASSPSGTAPQVSQGRGTTLPSMDVAPPPDGNPMGPGPGPPPQPSPPLIGAPEIARVTMTTPGSSILSPQMNSFEPYSEKKVSGKKSESKEAKKTEEPKIRKKPGPKPGWKKQLRSEREELPTIYKCPYQGCTAVYRGADGMKKHIKEHHEEVRERPCPHPGCNKVFMIDRYLQRHVKLIHTEVRNYICDECGQTFKQRKHLLVHQMRHSGAKPLQCEVCGFQCRQRASLKYHMTKHKAETELDFACDQCGRRFEKAHNLNVHMSMVHPLTQTQDKALPLEAEPPPGPPHPSGTTEGQAVKPEPT [Source organism chain B]=Oryctolagus cuniculus [ExpTech]=X-ray [Resolution]=2.90 [Source organism]=Oryctolagus cuniculus [Accession]=MF7000971 [Entry] [Entry number]=1156 [Entry name]=SYCE3 [PDB ID]=6h86 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric, forming a 4-helix bundle) [Sequence domain]=Synaptonemal complex central element protein 3 [Evidence level]=Indirect evidence [Evidence text]=The authors claim that the extensive hydrophobic and hydrogen bonding interactions within the 4-helix bundle indicate highly stable dimer formation. SYCE3 is also seen in the dimeric form in solution and in cells by several methods (PMID:25394919). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000338,MF7000972 [UniProt ID chain A]=B5KM66 [UniProt boundaries chain A]=10-85 [UniProt coverage chain A]=86% [Name chain A]=Synaptonemal complex central element protein 3 [UniProt sequence chain A]=MADSDPGERSYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFLNCKEEMEKNWQELLTETKRKQ [Source organism chain A]=Mus musculus [UniProt ID chain B]=B5KM66 [UniProt boundaries chain B]=10-85 [UniProt coverage chain B]=86% [Name chain B]=Synaptonemal complex central element protein 3 [UniProt sequence chain B]=MADSDPGERSYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFLNCKEEMEKNWQELLTETKRKQ [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Mus musculus [Accession]=MF7000972 [Entry] [Entry number]=1157 [Entry name]=PigE (Serratia sp. FS14) [PDB ID]=4ppm [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Aminotransferase class-III [Evidence level]=Direct evidence [Evidence text]=The equilibrium unfolding of pig liver 4-aminobutyrate aminotransferase by urea was found to be a cooperative process. The kinetic results indicated that the aminotransferase unfolds in a single kinetic phase (PMID:8075151). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF2110019,MF7000973 [UniProt ID chain A]=A0A0J9X1Q5 [UniProt boundaries chain A]=372-853 [UniProt coverage chain A]=56% [Name chain A]=Aminotransferase PigE [UniProt sequence chain A]=MKFGFIAHPTSLGLKRYVKMLDLLQRNSTEQHSGYTRELWERQNLVPFMNFARITSATGATCEGVIKYMPLVADEMLADARGIAARVVQGIEELAGDGAELVGLGGFTSIVGRRGEATAEKSPVPVTSGNSLTTYAGYKALMQIQSWLEIRPEEEPVAIVGYPGSICLALSRLLLAHGFSLHLLHRAGNHDRSELLSHLPEEYHSRVTLTSDPEDLYPRCKLFAAATSAGGVIDPARLQPGSIFIDVALPRDIASETRPARDDILIIDGGCVTATDAVKLGGESLNVTIKQQLNGCMAETIVLALENRRENFSLGRYLAPEKVLEIGEIAERHGFFAYPLASYGERIDRQSVTNLKRYYHHDIYAGESADAALPASRLAFIDAVIAQTPAREDTLDRYHQYINPMMVDFLKLQRCDNVFRSAAGTQLYDDAGEAFLDMVAGYGCLNLGHNPQPVVNALKNYLDAQGPNFIQYISIPEQTAKLAEVLCRLAPGNMGRVFFSNSGTEAVEAAMKIAKASTGKPGIAYLRNSYHGKTLGALSITGRDKHRRYFTPLLDAMVEVPFGDLAALREALNREDVGALMIEPIQGEGGVHIPPAGYLQAVQQLCRETGVLLMVDEVQTGLGRTGKLFACEWDGIEPDVLMLSKSLSGGLIPIGATLCRADLWQKAYGTADRFLVHSSTYGGGNLASVVALSALREILAQDLVGHAERMGAYFKQALSEIAARYPFVSEVRGRGLMLGIQFDQAFTGAVNASAREFATRLPGDWHTTWKFLPDPVQAHLRAAMDRMEQALGEMFCMKFVTKLCQDHKILTFITANSSTVIRIQPPLIISKAEIDRFVGAFATVCEELSTFLD [Source organism chain A]=Serratia sp [UniProt ID chain B]=A0A0J9X1Q5 [UniProt boundaries chain B]=372-853 [UniProt coverage chain B]=56% [Name chain B]=Aminotransferase PigE [UniProt sequence chain B]=MKFGFIAHPTSLGLKRYVKMLDLLQRNSTEQHSGYTRELWERQNLVPFMNFARITSATGATCEGVIKYMPLVADEMLADARGIAARVVQGIEELAGDGAELVGLGGFTSIVGRRGEATAEKSPVPVTSGNSLTTYAGYKALMQIQSWLEIRPEEEPVAIVGYPGSICLALSRLLLAHGFSLHLLHRAGNHDRSELLSHLPEEYHSRVTLTSDPEDLYPRCKLFAAATSAGGVIDPARLQPGSIFIDVALPRDIASETRPARDDILIIDGGCVTATDAVKLGGESLNVTIKQQLNGCMAETIVLALENRRENFSLGRYLAPEKVLEIGEIAERHGFFAYPLASYGERIDRQSVTNLKRYYHHDIYAGESADAALPASRLAFIDAVIAQTPAREDTLDRYHQYINPMMVDFLKLQRCDNVFRSAAGTQLYDDAGEAFLDMVAGYGCLNLGHNPQPVVNALKNYLDAQGPNFIQYISIPEQTAKLAEVLCRLAPGNMGRVFFSNSGTEAVEAAMKIAKASTGKPGIAYLRNSYHGKTLGALSITGRDKHRRYFTPLLDAMVEVPFGDLAALREALNREDVGALMIEPIQGEGGVHIPPAGYLQAVQQLCRETGVLLMVDEVQTGLGRTGKLFACEWDGIEPDVLMLSKSLSGGLIPIGATLCRADLWQKAYGTADRFLVHSSTYGGGNLASVVALSALREILAQDLVGHAERMGAYFKQALSEIAARYPFVSEVRGRGLMLGIQFDQAFTGAVNASAREFATRLPGDWHTTWKFLPDPVQAHLRAAMDRMEQALGEMFCMKFVTKLCQDHKILTFITANSSTVIRIQPPLIISKAEIDRFVGAFATVCEELSTFLD [Source organism chain B]=Serratia sp [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Serratia sp [Accession]=MF7000973 [Entry] [Entry number]=1158 [Entry name]=Bre1 RING domain [PDB ID]=4r7e [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Zinc finger, RING type [Sequence domain]=Zinc finger, C3HC4 type (RING finger) [Evidence level]=No contradicting information [Evidence text]=The BRE1 and BRE1A RING domains are both homodimers in solution as confirmed by size-exclusion chromatography and multi-angle laser light scattering (MALLS) (PMID:27569044, PMID:25864391). The extended dimerization interface consists of symmetric RING domain-RING domain interactions and a coiled- coil interaction between the N-terminal a-helices (PMID:25864391). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000974,MF7000378 [UniProt ID chain A]=Q07457 [UniProt boundaries chain A]=632-700 [UniProt coverage chain A]=9% [Name chain A]=E3 ubiquitin-protein ligase BRE1 [UniProt sequence chain A]=MTAEPATKKIKLELSDPSEPLTQSDVIAFQKEALFRCINRRRVDFEALRKQYELSRRECIDVSRKLANIMALIVTLARFIETFCTDANEKQLCREIAQGDETLIVQRSDSFMKLLTKYGKPNTTDSNTNSNASDHIQELTTELKNLRKSKEELFYENSQLTEEISALKEYYTNIIRKYDRDESFTIKRVFKEDKTDAVKELREDEKESNENNIKSGNKDSSAINGDNTSKKSEKGDELVQAEDERKEDAENEKLELDLKFSDLRAEINSLSSTIKDLENIRRENEEELIKTRSEVSNLKKQQIAAADQDPDFKSYDHESLLAKIQHLTEQNAELSEINSSFLSKFQVLAKEKEIYTKKVREEFQKSLDSLVEMNSSLEKDVVRIRTARDDLLSKIAILEAEKSKTEVLSDLQHAIDILKEQWTKIDQRSNDTKSSSTQDALIKEIQDLEKGFRELSDLTHKKYSEIINHESVISKLTVEKTKADQKYFAAMRSKDSILIEIKTLSKSLSKSNELILQLKDSDRLLQQKIGNLHKQLDLSQNNERRLIDSSKTETLKIIDLNNTSTKLKRSLEKLQEESNKSIADMTHLETKLNDTEIELKHFKQKASHLESKCEKLHDTLFRGNNKNKGSSDEALVEELANFRTLVYCSLCSKNWKNMAIKTCGHVFCENCCKERLAARMRKCPTCNKAFSSNDLLTVHL [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain A-2]=Q07457 [UniProt boundaries chain A-2]=632-700 [UniProt coverage chain A-2]=9% [Name chain A-2]=E3 ubiquitin-protein ligase BRE1 [UniProt sequence chain A-2]=MTAEPATKKIKLELSDPSEPLTQSDVIAFQKEALFRCINRRRVDFEALRKQYELSRRECIDVSRKLANIMALIVTLARFIETFCTDANEKQLCREIAQGDETLIVQRSDSFMKLLTKYGKPNTTDSNTNSNASDHIQELTTELKNLRKSKEELFYENSQLTEEISALKEYYTNIIRKYDRDESFTIKRVFKEDKTDAVKELREDEKESNENNIKSGNKDSSAINGDNTSKKSEKGDELVQAEDERKEDAENEKLELDLKFSDLRAEINSLSSTIKDLENIRRENEEELIKTRSEVSNLKKQQIAAADQDPDFKSYDHESLLAKIQHLTEQNAELSEINSSFLSKFQVLAKEKEIYTKKVREEFQKSLDSLVEMNSSLEKDVVRIRTARDDLLSKIAILEAEKSKTEVLSDLQHAIDILKEQWTKIDQRSNDTKSSSTQDALIKEIQDLEKGFRELSDLTHKKYSEIINHESVISKLTVEKTKADQKYFAAMRSKDSILIEIKTLSKSLSKSNELILQLKDSDRLLQQKIGNLHKQLDLSQNNERRLIDSSKTETLKIIDLNNTSTKLKRSLEKLQEESNKSIADMTHLETKLNDTEIELKHFKQKASHLESKCEKLHDTLFRGNNKNKGSSDEALVEELANFRTLVYCSLCSKNWKNMAIKTCGHVFCENCCKERLAARMRKCPTCNKAFSSNDLLTVHL [Source organism chain A-2]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=2.25 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7000974 [Entry] [Entry number]=1159 [Entry name]=Domain-swapped guanine deaminase (Bacillus subtilis) [PDB ID]=1wkq [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=Analytical ultracentrifugation experiments demonstrated that the guanine deaminase enzyme exists in solution as a homodimer. The C-terminal segment is swapped to form an intersubunit active site and an intertwined dimer with an extensive interface. The dimer is stabilized mainly by the formation of the wide interhelical hydrophobic packing of helices. Interestingly, analysis of unswapped bGD model shows that domain swapping contributes not only to oligomerization and structural stability but also to substrate specificity (PMID:15180998). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O34598 [UniProt boundaries chain A]=1-156 [UniProt coverage chain A]=100% [Name chain A]=Guanine deaminase [UniProt sequence chain A]=MNHETFLKRAVTLACEGVNAGIGGPFGAVIVKDGAIIAEGQNNVTTSNDPTAHAEVTAIRKACKVLGAYQLDDCILYTSCEPCPMCLGAIYWARPKAVFYAAEHTDAAEAGFDDSFIYKEIDKPAEERTIPFYQVTLTEHLSPFQAWRNFANKKEY [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=O34598 [UniProt boundaries chain B]=2-156 [UniProt coverage chain B]=99% [Name chain B]=Guanine deaminase [UniProt sequence chain B]=MNHETFLKRAVTLACEGVNAGIGGPFGAVIVKDGAIIAEGQNNVTTSNDPTAHAEVTAIRKACKVLGAYQLDDCILYTSCEPCPMCLGAIYWARPKAVFYAAEHTDAAEAGFDDSFIYKEIDKPAEERTIPFYQVTLTEHLSPFQAWRNFANKKEY [Source organism chain B]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=1.17 [Source organism]=Bacillus subtilis [Accession]=MF7000975 [Entry] [Entry number]=1160 [Entry name]=tRNA-specific adenosine deaminase (Streptococcus pyogenes) [PDB ID]=2nx8 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=No contradicting information [Evidence text]=The tRNA-specific adenosine deaminase, spTadA is a dimer in solution as demonstrated by gel-filtration. Dimer formation buries a large surface which is mainly formed by hydrophobic and nonpolar interactions. From the structural aspects, dimerization appears to be important for specific binding with tRNA and enzyme functions. The authors also suggest that because of the nonpolar interface, the formation of a dimer is energetically favorable compared with the monomer in solution. (PMID:17554781). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q5XE14 [UniProt boundaries chain A]=1-165 [UniProt coverage chain A]=96% [Name chain A]=tRNA-specific adenosine deaminase [UniProt sequence chain A]=MPYSLEEQTYFMQEALKEAEKSLQKAEIPIGCVIVKDGEIIGRGHNAREESNQAIMHAEMMAINEANAHEGNWRLLDTTLFVTIEPCVMCSGAIGLARIPHVIYGASNQKFGGADSLYQILTDERLNHRVQVERGLLAADCANIMQTFFRQGRERKKIAKHLIKEQSDPFD [Source organism chain A]=Streptococcus pyogenes serotype M6 [UniProt ID chain A-2]=Q5XE14 [UniProt boundaries chain A-2]=1-165 [UniProt coverage chain A-2]=96% [Name chain A-2]=tRNA-specific adenosine deaminase [UniProt sequence chain A-2]=MPYSLEEQTYFMQEALKEAEKSLQKAEIPIGCVIVKDGEIIGRGHNAREESNQAIMHAEMMAINEANAHEGNWRLLDTTLFVTIEPCVMCSGAIGLARIPHVIYGASNQKFGGADSLYQILTDERLNHRVQVERGLLAADCANIMQTFFRQGRERKKIAKHLIKEQSDPFD [Source organism chain A-2]=Streptococcus pyogenes serotype M6 [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Streptococcus pyogenes serotype M6 [Accession]=MF7000976 [Entry] [Entry number]=1161 [Entry name]=Hypothetical protein TTHA1013 (Thermus thermophilus HB8) [PDB ID]=1wv8 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=TTHA1013/TTHA0281-like [Evidence level]=No contradicting information [Evidence text]=Crystal structure and gel filtration indicate that TTHA1756 intrinsically forms a dimer. THA1756 forms a dimer through the formation of an eight-stranded b-sheet with b4 of one subunit intervening between b1 and b4 of the other subunit (PMID:18338381). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000977,MF7000234 [UniProt ID chain A]=Q5SJJ5 [UniProt boundaries chain A]=2-72 [UniProt coverage chain A]=97% [Name chain A]=DUF1902 domain-containing protein [UniProt sequence chain A]=MRTLKVQALWDGEAGVWVAESDDVPGLATEAATLEELLAKLAVMVPELLEENGVALELPVELRLEATRPLVFS [Source organism chain A]=Thermus thermophilus [UniProt ID chain A-2]=Q5SJJ5 [UniProt boundaries chain A-2]=2-72 [UniProt coverage chain A-2]=97% [Name chain A-2]=DUF1902 domain-containing protein [UniProt sequence chain A-2]=MRTLKVQALWDGEAGVWVAESDDVPGLATEAATLEELLAKLAVMVPELLEENGVALELPVELRLEATRPLVFS [Source organism chain A-2]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=2.20 [Source organism]=Thermus thermophilus [Accession]=MF7000977 [Entry] [Entry number]=1162 [Entry name]=DNA-binding protein Sso10a (Sulfolobus solfataricus) [PDB ID]=1r7j [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArnR1-type) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=Sso10a is a dimer of winged helix DNA-binding domains linked by an antiparallel coiled coil rod formed from the C-terminal α-helices of the monomers. The winged helix domains are at opposite ends of the extended coiled coil. Formation of stable dimers in solution is demonstrated by both AUC and DSC. With a T0 of 109 degrees C, Sso10a is one of the most stable two-stranded coiled coils known (PMID:15312764). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=MF7000978,MF7000979 [UniProt ID chain A]=Q5W1E8 [UniProt boundaries chain A]=4-93 [UniProt coverage chain A]=93% [Name chain A]=DNA-binding protein [UniProt sequence chain A]=MAKKKSKLEIIQAILEACKSGSPKTRIMYGANLSYALTGRYIKMLMDLEIIRQEGKQYMLTKKGEELLEDIRKFNEMRKNMDQLKEKINSVLSIRQ [Source organism chain A]=Saccharolobus solfataricus [UniProt ID chain A-2]=Q5W1E8 [UniProt boundaries chain A-2]=4-93 [UniProt coverage chain A-2]=93% [Name chain A-2]=DNA-binding protein [UniProt sequence chain A-2]=MAKKKSKLEIIQAILEACKSGSPKTRIMYGANLSYALTGRYIKMLMDLEIIRQEGKQYMLTKKGEELLEDIRKFNEMRKNMDQLKEKINSVLSIRQ [Source organism chain A-2]=Saccharolobus solfataricus [ExpTech]=X-ray [Resolution]=1.47 [Source organism]=Saccharolobus solfataricus [Accession]=MF7000978 [Entry] [Entry number]=1163 [Entry name]=Sso10a, a hyperthermophile DNA-binding protein [PDB ID]=1xsx [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=Winged helix DNA-binding domain (ArnR1-type) transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=Sso10a is a dimer of winged helix DNA-binding domains linked by an antiparallel coiled coil rod formed from the C-terminal α-helices of the monomers. The winged helix domains are at opposite ends of the extended coiled coil. Formation of stable dimers in solution is demonstrated by both AUC and DSC. With a T0 of 109 degrees C, Sso10a is one of the most stable two-stranded coiled coils known (PMID:15312764). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000978,MF7000979 [UniProt ID chain A]=Q5W1E8 [UniProt boundaries chain A]=2-96 [UniProt coverage chain A]=98% [Name chain A]=DNA-binding protein [UniProt sequence chain A]=MAKKKSKLEIIQAILEACKSGSPKTRIMYGANLSYALTGRYIKMLMDLEIIRQEGKQYMLTKKGEELLEDIRKFNEMRKNMDQLKEKINSVLSIRQ [Source organism chain A]=Saccharolobus solfataricus [UniProt ID chain B]=Q5W1E8 [UniProt boundaries chain B]=2-96 [UniProt coverage chain B]=98% [Name chain B]=DNA-binding protein [UniProt sequence chain B]=MAKKKSKLEIIQAILEACKSGSPKTRIMYGANLSYALTGRYIKMLMDLEIIRQEGKQYMLTKKGEELLEDIRKFNEMRKNMDQLKEKINSVLSIRQ [Source organism chain B]=Saccharolobus solfataricus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharolobus solfataricus [Accession]=MF7000979 [Entry] [Entry number]=1164 [Entry name]=Selenomethionine-labeled BPSL1038 (Burkholderia pseudomallei) [PDB ID]=7vxt [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=BPSL1038 modified ferredoxin fold [Evidence level]=No contradicting information [Evidence text]=The two monomers have a common beta sheet and a large total calculated buried interface area that involves mainly hydrophobic interactions in addition to 16 hydrogen bonds and one salt bridge. In total, 42% of the amino acids (37 residues) are associated with dimerization (PMID: 37684342). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000980,MF7000981 [UniProt ID chain A]=Q63W52 [UniProt boundaries chain A]=1-87 [UniProt coverage chain A]=98% [Name chain A]=Uncharacterized protein [UniProt sequence chain A]=MAGNLVIVCRDQDADAFDQLMQEYGSFQTRLSSTAWYLNMNIVPETLQEDILERVGKYTTLYIFEATSVTYNTIDSNAAETLSTLFGE [Source organism chain A]=Burkholderia pseudomallei [UniProt ID chain B]=Q63W52 [UniProt boundaries chain B]=2-87 [UniProt coverage chain B]=97% [Name chain B]=Uncharacterized protein [UniProt sequence chain B]=MAGNLVIVCRDQDADAFDQLMQEYGSFQTRLSSTAWYLNMNIVPETLQEDILERVGKYTTLYIFEATSVTYNTIDSNAAETLSTLFGE [Source organism chain B]=Burkholderia pseudomallei [ExpTech]=X-ray [Resolution]=1.88 [Source organism]=Burkholderia pseudomallei [Accession]=MF7000980 [Entry] [Entry number]=1165 [Entry name]=BPSL1038 (Burkholderia pseudomallei) [PDB ID]=7vxr [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=BPSL1038 modified ferredoxin fold [Evidence level]=No contradicting information [Evidence text]=The two monomers have a common beta sheet and a large total calculated buried interface area that involves mainly hydrophobic interactions in addition to 16 hydrogen bonds and one salt bridge. In total, 42% of the amino acids (37 residues) are associated with dimerization (PMID: 37684342). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000980,MF7000981 [UniProt ID chain A]=Q63W52 [UniProt boundaries chain A]=1-87 [UniProt coverage chain A]=98% [Name chain A]=Uncharacterized protein [UniProt sequence chain A]=MAGNLVIVCRDQDADAFDQLMQEYGSFQTRLSSTAWYLNMNIVPETLQEDILERVGKYTTLYIFEATSVTYNTIDSNAAETLSTLFGE [Source organism chain A]=Burkholderia pseudomallei [UniProt ID chain B]=Q63W52 [UniProt boundaries chain B]=2-87 [UniProt coverage chain B]=97% [Name chain B]=Uncharacterized protein [UniProt sequence chain B]=MAGNLVIVCRDQDADAFDQLMQEYGSFQTRLSSTAWYLNMNIVPETLQEDILERVGKYTTLYIFEATSVTYNTIDSNAAETLSTLFGE [Source organism chain B]=Burkholderia pseudomallei [ExpTech]=X-ray [Resolution]=1.55 [Source organism]=Burkholderia pseudomallei [Accession]=MF7000981 [Entry] [Entry number]=1166 [Entry name]=DNA-binding domain of NTRC, mutant (ALA substitutions) [PDB ID]=1ntc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=DNA-binding HTH domain and helical dimerization domain [Sequence domain]=Fis-type HTH domain transcriptional regulator [Evidence level]=Direct evidence [Evidence text]=FIS forms an intertwined homodimer. Helices A and B join of the two monomer to form an antiparallel four-helix bundle. Equilibrium and kinetic methods have shown that FIS follows a two-step folding reaction where the two unfolded monomers associate to a dimeric intermediate during a fast phase, which is followed by a slower, subsequent folding of the dimeric intermediate to the native dimer (PMID:14698300). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000982,MF2120020 [UniProt ID chain A]=P41789 [UniProt boundaries chain A]=380-469 [UniProt coverage chain A]=19% [Name chain A]=DNA-binding transcriptional regulator NtrC [UniProt sequence chain A]=MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLAALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIEVNGPTTDMIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLERRVQEGKFREDLFHRLNVIRIHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETETALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFEASTPDSPSHLPPDSWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME [Source organism chain A]=Salmonella typhimurium [UniProt ID chain B]=P41789 [UniProt boundaries chain B]=380-469 [UniProt coverage chain B]=19% [Name chain B]=DNA-binding transcriptional regulator NtrC [UniProt sequence chain B]=MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLAALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIEVNGPTTDMIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLERRVQEGKFREDLFHRLNVIRIHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETETALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFEASTPDSPSHLPPDSWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME [Source organism chain B]=Salmonella typhimurium [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella typhimurium [Accession]=MF7000982 [Entry] [Entry number]=1167 [Entry name]=C-terminal domain of Rv1828 (Mycobacterium tuberculosis) [PDB ID]=5ydd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=DNA-binding HTH domain and helical dimerization domain [Sequence domain]=HTH domain transcriptional regulator Rv1828 [Evidence level]=Indirect evidence [Evidence text]=M. tuberculosis Rv1828 is a MerR family transcription regulator. The structure of Rv1828-CTD showed that the dimerization is mediated by a4c and a5c helices from one monomer with a4'c, a5'c helices of other monomer. In the dimeric form of Rv1828-CTD, the a5c-helix of one monomer is extended into the other monomer and surrounded by a3'c, a4'c and a5'c helices to form a stable dimeric conformation. About 50% of the CTD residues are located at the extensive and tight dimeric interface largely formed through hydrophobic interactions. Accordingly, the hydrophobic core is contributed by both monomers (PMID:30306715). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000983,MF7000984 [UniProt ID chain A]=P9WME7 [UniProt boundaries chain A]=127-245 [UniProt coverage chain A]=48% [Name chain A]=Uncharacterized HTH-type transcriptional regulator Rv1828 [UniProt sequence chain A]=MSAPDSPALAGMSIGAVLDLLRPDFPDVTISKIRFLEAEGLVTPRRASSGYRRFTAYDCARLRFILTAQRDHYLPLKVIRAQLDAQPDGELPPFGSPYVLPRLVPVAGDSAGGVGSDTASVSLTGIRLSREDLLERSEVADELLTALLKAGVITTGPGGFFDEHAVVILQCARALAEYGVEPRHLRAFRSAADRQSDLIAQIAGPLVKAGKAGARDRADDLAREVAALAITLHTSLIKSAVRDVLHR [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WME7 [UniProt boundaries chain B]=127-246 [UniProt coverage chain B]=48% [Name chain B]=Uncharacterized HTH-type transcriptional regulator Rv1828 [UniProt sequence chain B]=MSAPDSPALAGMSIGAVLDLLRPDFPDVTISKIRFLEAEGLVTPRRASSGYRRFTAYDCARLRFILTAQRDHYLPLKVIRAQLDAQPDGELPPFGSPYVLPRLVPVAGDSAGGVGSDTASVSLTGIRLSREDLLERSEVADELLTALLKAGVITTGPGGFFDEHAVVILQCARALAEYGVEPRHLRAFRSAADRQSDLIAQIAGPLVKAGKAGARDRADDLAREVAALAITLHTSLIKSAVRDVLHR [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000983 [Entry] [Entry number]=1168 [Entry name]=C-terminal domain of Rv1828 (Mycobacterium tuberculosis) [PDB ID]=5ydc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=DNA-binding HTH domain and helical dimerization domain [Sequence domain]=HTH domain transcriptional regulator Rv1828 [Evidence level]=Indirect evidence [Evidence text]=M. tuberculosis Rv1828 is a MerR family transcription regulator. The structure of Rv1828-CTD showed that the dimerization is mediated by a4c and a5c helices from one monomer with a4'c, a5'c helices of other monomer. In the dimeric form of Rv1828-CTD, the a5c-helix of one monomer is extended into the other monomer and surrounded by a3'c, a4'c and a5'c helices to form a stable dimeric conformation. About 50% of the CTD residues are located at the extensive and tight dimeric interface largely formed through hydrophobic interactions. Accordingly, the hydrophobic core is contributed by both monomers (PMID:30306715). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000983,MF7000984 [UniProt ID chain A]=P9WME7 [UniProt boundaries chain A]=127-245 [UniProt coverage chain A]=48% [Name chain A]=Uncharacterized HTH-type transcriptional regulator Rv1828 [UniProt sequence chain A]=MSAPDSPALAGMSIGAVLDLLRPDFPDVTISKIRFLEAEGLVTPRRASSGYRRFTAYDCARLRFILTAQRDHYLPLKVIRAQLDAQPDGELPPFGSPYVLPRLVPVAGDSAGGVGSDTASVSLTGIRLSREDLLERSEVADELLTALLKAGVITTGPGGFFDEHAVVILQCARALAEYGVEPRHLRAFRSAADRQSDLIAQIAGPLVKAGKAGARDRADDLAREVAALAITLHTSLIKSAVRDVLHR [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain B]=P9WME7 [UniProt boundaries chain B]=127-246 [UniProt coverage chain B]=48% [Name chain B]=Uncharacterized HTH-type transcriptional regulator Rv1828 [UniProt sequence chain B]=MSAPDSPALAGMSIGAVLDLLRPDFPDVTISKIRFLEAEGLVTPRRASSGYRRFTAYDCARLRFILTAQRDHYLPLKVIRAQLDAQPDGELPPFGSPYVLPRLVPVAGDSAGGVGSDTASVSLTGIRLSREDLLERSEVADELLTALLKAGVITTGPGGFFDEHAVVILQCARALAEYGVEPRHLRAFRSAADRQSDLIAQIAGPLVKAGKAGARDRADDLAREVAALAITLHTSLIKSAVRDVLHR [Source organism chain B]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.91 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000984 [Entry] [Entry number]=1169 [Entry name]=Human MST2 with SAV1 SARAH domain [PDB ID]=6ao5 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=SARAH domain dimer [Sequence domain]=SARAH domain dimer [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:29519817). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000985,MF7000389 [UniProt ID chain A]=Q13188 [UniProt boundaries chain A]=28-488 [UniProt coverage chain A]=93% [Name chain A]=Serine/threonine-protein kinase 3 [UniProt sequence chain A]=MEQPPAPKSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLIEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEEEENSDEDELDSHTMVKTSVESVGTMRATSTMSEGAQTMIEHNSTMLESDLGTMVINSEDEEEEDGTMKRNATSPQVQRPSFMDYFDKQDFKNKSHENCNQNMHEPFPMSKNVFPDNWKVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAKKRRQQNF [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9H4B6 [UniProt boundaries chain B]=291-376 [UniProt coverage chain B]=22% [Name chain B]=Protein salvador homolog 1 [UniProt sequence chain B]=MLSRKKTKNEVSKPAEVQGKYVKKETSPLLRNLMPSFIRHGPTIPRRTDICLPDSSPNAFSTSGDVVSRNQSFLRTPIQRTPHEIMRRESNRLSAPSYLARSLADVPREYGSSQSFVTEVSFAVENGDSGSRYYYSDNFFDGQRKRPLGDRAHEDYRYYEYNHDLFQRMPQNQGRHASGIGRVAATSLGNLTNHGSEDLPLPPGWSVDWTMRGRKYYIDHNTNTTHWSHPLEREGLPPGWERVESSEFGTYYVDHTNKKAQYRHPCAPSVPRYDQPPPVTYQPQQTERNQSLLVPANPYHTAEIPDWLQVYARAPVKYDHILKWELFQLADLDTYQGMLKLLFMKELEQIVKMYEAYRQALLTELENRKQRQQWYAQQHGKNF [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.96 [Source organism]=Homo sapiens [Accession]=MF7000985 [Entry] [Entry number]=1170 [Entry name]=SIV protease with inhibitor SB203386 [PDB ID]=1tcw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Retroviral aspartyl protease [Evidence level]=Direct evidence [Evidence text]=Retroviral aspartyl proteases follow a two-state unfolding behavior in which folded dimers were in equilibrium with unfolded monomers. This model conforms to cases in which protein unfolding and dimer dissociation are cooperative processes in which folded monomers do not exist (PMID:1390732). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000986,MF7000987 [UniProt ID chain A]=P05896 [UniProt boundaries chain A]=498-596 [UniProt coverage chain A]=6% [Name chain A]=Gag-Pol polyprotein [UniProt sequence chain A]=MGARNSVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVMETGTAETMPKTSRPTAPFSGRGGNYPVQQIGGNYTHLPLSPRTLNAWVKLIEEKKFGAEVVSGFQALSEGCLPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQQAPQQGQLREPSGSDIAGTTSTVEEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGTNPTLEEMLTACQGVGGPGQKARLMAEALKEALAPAPIPFAAAQQKGPRKPIKCWNCGKEGHSARQCRAPRRQGCWKCGKMDHVMAKCPNRQAGFFRPWPLGKEAPQFPHGSSASGADANCSPRRTSCGSAKELHALGQAAERKQREALQGGDRGFAAPQFSLWRRPVVTAHIEGQPVEVLLDTGADDSIVTGIELGPHYTPKIVGGIGGFINTKEYKNVEIEVLGKRIKGTIMTGDTPINIFGRNLLTALGMSLNLPIAKVEPVKSPLKPGKDGPKLKQWPLSKEKIVALREICEKMEKDGQLEEAPPTNPYNTPTFAIKKKDKNKWRMLIDFRELNRVTQDFTEVQLGIPHPAGLAKRKRITVLDIGDAYFSIPLDEEFRQYTAFTLPSVNNAEPGKRYIYKVLPQGWKGSPAIFQYTMRHVLEPFRKANPDVTLVQYMDDILIASDRTDLEHDRVVLQLKELLNSIGFSSPEEKFQKDPPFQWMGYELWPTKWKLQKIELPQRETWTVNDIQKLVGVLNWAAQIYPGIKTKHLCRLIRGKMTLTEEVQWTEMAEAEYEENKIILSQEQEGCYYQESKPLEATVIKSQDNQWSYKIHQEDKILKVGKFAKIKNTHTNGVRLLAHVIQKIGKEAIVIWGQVPKFHLPVEKDVWEQWWTDYWQVTWIPEWDFISTPPLVRLVFNLVKDPIEGEETYYVDGSCSKQSKEGKAGYITDRGKDKVKVLEQTTNQQAELEAFLMALTDSGPKANIIVDSQYVMGIITGCPTESESRLVNQIIEEMIKKTEIYVAWVPAHKGIGGNQEIDHLVSQGIRQVLFLEKIEPAQEEHSKYHSNIKELVFKFGLPRLVAKQIVDTCDKCHQKGEAIHGQVNSDLGTWQMDCTHLEGKIVIVAVHVASGFIEAEVIPQETGRQTALFLLKLASRWPITHLHTDNGANFASQEVKMVAWWAGIEHTFGVPYNPQSQGVVEAMNHHLKNQIDRIREQANSVETIVLMAVHCMNFKRRGGIGDMTPAERLINMITTEQEIQFQQSKNSKFKNFRVYYREGRDQLWKGPGELLWKGEGAVILKVGTDIKVVPRRKAKIIKDYGGGKEMDSSSHMEDTGEAREVA [Source organism chain A]=immunodeficiency virus rhesus monkey) [UniProt ID chain B]=P05896 [UniProt boundaries chain B]=498-596 [UniProt coverage chain B]=6% [Name chain B]=Gag-Pol polyprotein [UniProt sequence chain B]=MGARNSVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVMETGTAETMPKTSRPTAPFSGRGGNYPVQQIGGNYTHLPLSPRTLNAWVKLIEEKKFGAEVVSGFQALSEGCLPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQQAPQQGQLREPSGSDIAGTTSTVEEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGTNPTLEEMLTACQGVGGPGQKARLMAEALKEALAPAPIPFAAAQQKGPRKPIKCWNCGKEGHSARQCRAPRRQGCWKCGKMDHVMAKCPNRQAGFFRPWPLGKEAPQFPHGSSASGADANCSPRRTSCGSAKELHALGQAAERKQREALQGGDRGFAAPQFSLWRRPVVTAHIEGQPVEVLLDTGADDSIVTGIELGPHYTPKIVGGIGGFINTKEYKNVEIEVLGKRIKGTIMTGDTPINIFGRNLLTALGMSLNLPIAKVEPVKSPLKPGKDGPKLKQWPLSKEKIVALREICEKMEKDGQLEEAPPTNPYNTPTFAIKKKDKNKWRMLIDFRELNRVTQDFTEVQLGIPHPAGLAKRKRITVLDIGDAYFSIPLDEEFRQYTAFTLPSVNNAEPGKRYIYKVLPQGWKGSPAIFQYTMRHVLEPFRKANPDVTLVQYMDDILIASDRTDLEHDRVVLQLKELLNSIGFSSPEEKFQKDPPFQWMGYELWPTKWKLQKIELPQRETWTVNDIQKLVGVLNWAAQIYPGIKTKHLCRLIRGKMTLTEEVQWTEMAEAEYEENKIILSQEQEGCYYQESKPLEATVIKSQDNQWSYKIHQEDKILKVGKFAKIKNTHTNGVRLLAHVIQKIGKEAIVIWGQVPKFHLPVEKDVWEQWWTDYWQVTWIPEWDFISTPPLVRLVFNLVKDPIEGEETYYVDGSCSKQSKEGKAGYITDRGKDKVKVLEQTTNQQAELEAFLMALTDSGPKANIIVDSQYVMGIITGCPTESESRLVNQIIEEMIKKTEIYVAWVPAHKGIGGNQEIDHLVSQGIRQVLFLEKIEPAQEEHSKYHSNIKELVFKFGLPRLVAKQIVDTCDKCHQKGEAIHGQVNSDLGTWQMDCTHLEGKIVIVAVHVASGFIEAEVIPQETGRQTALFLLKLASRWPITHLHTDNGANFASQEVKMVAWWAGIEHTFGVPYNPQSQGVVEAMNHHLKNQIDRIREQANSVETIVLMAVHCMNFKRRGGIGDMTPAERLINMITTEQEIQFQQSKNSKFKNFRVYYREGRDQLWKGPGELLWKGEGAVILKVGTDIKVVPRRKAKIIKDYGGGKEMDSSSHMEDTGEAREVA [Source organism chain B]=immunodeficiency virus rhesus monkey) [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=immunodeficiency virus rhesus monkey) [Accession]=MF7000986 [Entry] [Entry number]=1171 [Entry name]=HIV-1 proteasw with macrocyclic peptidomimetic inhibitor 3 [PDB ID]=1z1h [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=Retroviral aspartyl protease [Evidence level]=Direct evidence [Evidence text]=Retroviral aspartyl proteases follow a two-state unfolding behavior in which folded dimers were in equilibrium with unfolded monomers. This model conforms to cases in which protein unfolding and dimer dissociation are cooperative processes in which folded monomers do not exist (PMID:1390732). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=MF7000986,MF7000987 [UniProt ID chain A]=P03369 [UniProt boundaries chain A]=491-589 [UniProt coverage chain A]=6% [Name chain A]=Gag-Pol polyprotein [UniProt sequence chain A]=MGARASVLSGGELDKWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIDVKDTKEALEKIEEEQNKSKKKAQQAAAAAGTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPANIMMQRGNFRNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWRCGREGHQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTRRELQVWGGENNSLSEAGADRQGTVSFNFPQITLWQRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPGKWKPKMIGGIGGFIKVRQYDQIPVEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDKDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQPIMLPEKDSWTVNDIQKLVGKLNWASQIYAGIKVKQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHEVYYDPSKDLVAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKVSTESIVIWGKIPKFKLPIQKETWEAWWMEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTDRGRQKVVSIADTTNQKTELQAIHLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVSQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVLFLNGIDKAQEEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKIILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTSTTVKAACWWAGIKQEFGIPYNPQSQGVVESMNNELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDNKDPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED [Source organism chain A]= [UniProt ID chain B]=P03369 [UniProt boundaries chain B]=491-589 [UniProt coverage chain B]=6% [Name chain B]=Gag-Pol polyprotein [UniProt sequence chain B]=MGARASVLSGGELDKWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIDVKDTKEALEKIEEEQNKSKKKAQQAAAAAGTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPANIMMQRGNFRNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWRCGREGHQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTRRELQVWGGENNSLSEAGADRQGTVSFNFPQITLWQRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPGKWKPKMIGGIGGFIKVRQYDQIPVEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDKDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQPIMLPEKDSWTVNDIQKLVGKLNWASQIYAGIKVKQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHEVYYDPSKDLVAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKVSTESIVIWGKIPKFKLPIQKETWEAWWMEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTDRGRQKVVSIADTTNQKTELQAIHLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVSQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVLFLNGIDKAQEEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKIILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTSTTVKAACWWAGIKQEFGIPYNPQSQGVVESMNNELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDNKDPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED [Source organism chain B]= [ExpTech]=X-ray [Resolution]=1.85 [Source organism]= [Accession]=MF7000987 [Entry] [Entry number]=1172 [Entry name]=Human N-terminus of GCP6 and Mozart1 [PDB ID]=6m33 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Recombinant Mozart1 (recMZT1) and recombinant GCP6-N terminal helical domain (recGCP6-NHD) were not soluble when expressed individually. A co-overexpression strategy was required to gain soluble recMZT1 and recGCP6-NHD that co-eluted as a single peak over a gel filtration column. The interface of the two proteins is surprisingly large and hydrophobic (PMID:32610146). MOZART1 is was found to be in equilibrium between different oligomeric states (tetramer to hexamer) and prone to aggregation (PMID:28851027). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q96RT7 [UniProt boundaries chain A]=1-118 [UniProt coverage chain A]=6% [Name chain A]=Gamma-tubulin complex component 6 [UniProt sequence chain A]=MASITQLFDDLCEALLPAAKTHLGQRSVNRKRAKRSLKKVAYNALFTNLFQDETQQLQPDMSKLPARNKILMLSFDLRVGGLGPKADRLEELVEELEAAPCCPLLEVGSVLDLLVQLAGSGPPQVLPRKRDYFLNNKHVGRNVPYSGYDCDDLSVFEMDVQSLISREECLCHSMIQETLQVMEAAPGTGLPTVGLFSFGDPCGDRFERDTRVSLFGALVHSRTYDMDVRLGLPPVPDNADLSGLAIKVPPSVDQWEDEGFQSASNLTPDSQSEPSVTPDVDLWEAALTYEASKRRCWERVGCPPGHREEPYLTEAGRDAFDKFCRLHQGELQLLAGGVLQAPQPVLVKECELVKDVLNVLIGVVSATFSLCQPAQAFVVKRGVHVSGASPESISSLLSEVAEYGTCYTRLSHFSLQPVLDSLYSKGLVFQAFTSGLRRYLQYYRACVLSTPPTLSLLTIGFLFKKLGRQLRYLAELCGVGAVLPGTCGGGPRAAFPTGVKLLSYLYQEALHNCSNEHYPVLLSLLKTSCEPYTRFIHDWVYSGVFRDAYGEFMIQVNHEYLSFRDKLYWTHGYVLISKEVEDCVPVFLKHIAHDIYVCGKTINLLKLCCPRHYLCWSDVPVPRISVIFSLEELKEIEKDCAVYVGRMERVARHSSVSKEEKELRMEIAKQELIAHAREAASRVLSALSDRQMSERMALDARKREQFQRLKEQFVKDQERRQAARQEELDDDFSYARELRDRERRLKSLEEELERKARQALVDHYSKLSAEAARREQKALWRIQRHRLESARLRFLLEDEKHIQEMLKAVSEAHQPQEPPDVLLSVHPQVTSPGPEHPEGGQGCDSGSAEQHSPAWDGWNRPGLLTPQPLKPLAVGAGGRGLQQAEGARPFSDSLSIGDFLPVGPGAEPSVQTGMVPLLEVALQTINLDLPPSAPGEAPAAASTQPSRPQEYDFSTVLRPAVATSPAPGPLQAAECSLGSSGLQLWEDSCGKMDACGSASRETLLPSHPPRRAALEEGSSQPTERLFGQVSGGGLPTGDYASEIAPTRPRWNTHGHVSDASIRVGENVSDVAPTQPRWNTHGHVSNASISLGESVSDVAPTRPRWNIHGHVSNASIRVGENVSDVAPTRPRWNTHGHVSNASIRVGENVSDVAPTRPRWNTHGHVSDASISLGESVSDMAPARPRWNTHGHVSDASISLGESVSDMAPTRPRWNTHGHVSDTSIRVGENVSDVAPIRSRCNTHGHVSDASISLGEPVSDVVSTRPRWNTHVPIPPPHMVLGALSPEAEPNTPRPQQSPPGHTSQSALSLGAQSTVLDCGPRLPVEVGPSLSSPSSGCGEGSISVGENVSDVAPTQPWWPNTPGDSVSEELGPGRSGDTEDLSPNWPLNSQEDTAAQSSPGRGEEAEASAAEAQGGEQAYLAGLAGQYHLERYPDSYESMSEPPIAHLLRPVLPRAFAFPVDPQVQSAADETAVQLSELLTLPVLMKRSITAPLAAHISLVNKAAVDYFFVELHLEAHYEALRHFLLMEDGEFAQSLSDLLFEKLGAGQTPGELLNPLVLNSVLSKALQCSLHGDTPHASNLSLALKYLPEVFAPNAPDVLSCLELRYKVDWPLNIVITEGCVSKYSGVFSFLLQLKLMMWALKDVCFHLKRTALLSHMAGSVQFRQLQLFKHEMQHFVKVIQGYIANQILHVTWCEFRARLATVGDLEEIQRAHAEYLHKAVFRGLLTEKAAPVMNVIHSIFSLVLKFRSQLISQAWGPPGGPRGAEHPNFALMQQSYNTFKYYSHFLFKVVTKLVNRGYQPHLEDFLLRINFNNYYQDA [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q08AG7 [UniProt boundaries chain B]=11-76 [UniProt coverage chain B]=80% [Name chain B]=Mitotic-spindle organizing protein 1 [UniProt sequence chain B]=MASSSGAGAAAAAAAANLNAVRETMDVLLEISRILNTGLDMETLSICVRLCEQGINPEALSSVIKELRKATEALKAAENMTS [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=3.29 [Source organism]=Homo sapiens [Accession]=MF7000988 [Entry] [Entry number]=1173 [Entry name]=foxM1 transcription factor [PDB ID]=6osw [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Two different segments of the same protein, which are independent modules, and both of them are told to be disordered in the unbound state. So, while both the FoxM1 NRD and TAD are primarily intrinsically disordered domains, they associate and adopt a structured conformation wherein both of them contribute essential residues to the hydrophobic core (PMID:31134895). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=The region(s) described in DP03377 covers 100% of the sequence present in the structure [Similar structures]=None [UniProt ID chain A]=Q7T2G3 [UniProt boundaries chain A]=50-103 [UniProt coverage chain A]=8% [Name chain A]=Forkhead box M1 [UniProt sequence chain A]=MRESPRRPIILKRRKLPFLKSESDLGCDEADGTRCKTTSTQSTARSFPDGIRVMDHPTMPDTQVVVIPKSADLQSVISVLTAKGKECGPQGRNKFILLSGDTSLEESKTLGCFSTELGSELGKVKKESECFPLDDSLTNIQWLGKMSSDGLGSEKCPNKDNPNDSQQQSKGPEKENDPHSERPPYSYMAMIQFAINSKNNRHMTLKEIYNWIEDHFPYFRDIAKPGWKNSIRHNLSLHDMFIRETSPDGKISYWTIRPEANRCLTLDQVYKPLGDPLTPTCPQIPQVAIHQQQKRGAPELKKAIPALGGTERKMKPLLPRTDSYLVPIQLPLGQSLFLPTSSPVSLSTPPQTQNSSTPSSSKRVRIAPKVSQSDLSSVLLCKPASQEIKEEPVFQPVTSSEAPPPKSRRTDNSSSRRKQRLVLPATEEPVLLYPDSTLFDSGVISDISTFQDTREADPKPELDSPNREYSFKTPIKSSHPSSSTPSKLPTVTLEPWRITPVGKGGVLDFSPIRTPTGPHVTPQRNQHTSLSFTSTPFKELPLFNSPRELLTCSRSSPKRSAPACSRELLQVGAANRSLTEGFVLDTMNDSLSKILVDISFSGLEDEDLGMGNISWSQFIPELK [Source organism chain A]=Danio rerio [UniProt ID chain B]=Q7T2G3 [UniProt boundaries chain B]=569-593 [UniProt coverage chain B]=4% [Name chain B]=Forkhead box M1 [UniProt sequence chain B]=MRESPRRPIILKRRKLPFLKSESDLGCDEADGTRCKTTSTQSTARSFPDGIRVMDHPTMPDTQVVVIPKSADLQSVISVLTAKGKECGPQGRNKFILLSGDTSLEESKTLGCFSTELGSELGKVKKESECFPLDDSLTNIQWLGKMSSDGLGSEKCPNKDNPNDSQQQSKGPEKENDPHSERPPYSYMAMIQFAINSKNNRHMTLKEIYNWIEDHFPYFRDIAKPGWKNSIRHNLSLHDMFIRETSPDGKISYWTIRPEANRCLTLDQVYKPLGDPLTPTCPQIPQVAIHQQQKRGAPELKKAIPALGGTERKMKPLLPRTDSYLVPIQLPLGQSLFLPTSSPVSLSTPPQTQNSSTPSSSKRVRIAPKVSQSDLSSVLLCKPASQEIKEEPVFQPVTSSEAPPPKSRRTDNSSSRRKQRLVLPATEEPVLLYPDSTLFDSGVISDISTFQDTREADPKPELDSPNREYSFKTPIKSSHPSSSTPSKLPTVTLEPWRITPVGKGGVLDFSPIRTPTGPHVTPQRNQHTSLSFTSTPFKELPLFNSPRELLTCSRSSPKRSAPACSRELLQVGAANRSLTEGFVLDTMNDSLSKILVDISFSGLEDEDLGMGNISWSQFIPELK [Source organism chain B]=Danio rerio [ExpTech]=NMR [Resolution]=N/A [Source organism]=Danio rerio [Accession]=MF7000989 [Entry] [Entry number]=1174 [Entry name]=ParB-like protein PadC [PDB ID]=6ryk [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=PadC forms a compact, domain-swapped dimer made of two interlocking polypeptide chains. There is a large relative dimer interface (PMID:31835030). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q1D3H3 [UniProt boundaries chain A]=289-421 [UniProt coverage chain A]=27% [Name chain A]=ParBC domain-containing protein [UniProt sequence chain A]=MRARGLFRGATMDAEHRVDGQDGTAGAGPEGGSQAPSGQDGGQGGAVSAELHASGGPSGPQGEHRREDASPESGGEHRAEGTPPAEGSEQRAEGTPAAEGSEQRAEGKPSEQGVAQRAEDTPSEQGEPQNAGSAQGQGGEPPVASGDTQGEGERPHNAGGEAPGSADASGSEGSKDQAGSQEGGLQAEGTTSQGQAEPPAKDASHAQGEHQAVSDSHGQDGSESGGRSVANEEARAEQSPSDGEARVTPGLDERPQGAFWTGEADGDKSGDSDEASREDVLPEPEQRLSGRVTTVLLPLEKLQDESAFKLRPEGDVSGLATDIARLGQLFPVDVRPAGEDRYQLVCGFRRVAALRFLKRDAVQARIHLRLSDEDALVMSLAEAIHATPVGPEVLEAKRDELEAQGRLSAAVRDMLEKALATEDTLAPEGVEEEIDADELAQEVAQRLGAINQDLSLLADVFAALDESRKAELLMQLRYSSELVTYLEGL [Source organism chain A]=Myxococcus xanthus [UniProt ID chain B]=Q1D3H3 [UniProt boundaries chain B]=289-420 [UniProt coverage chain B]=26% [Name chain B]=ParBC domain-containing protein [UniProt sequence chain B]=MRARGLFRGATMDAEHRVDGQDGTAGAGPEGGSQAPSGQDGGQGGAVSAELHASGGPSGPQGEHRREDASPESGGEHRAEGTPPAEGSEQRAEGTPAAEGSEQRAEGKPSEQGVAQRAEDTPSEQGEPQNAGSAQGQGGEPPVASGDTQGEGERPHNAGGEAPGSADASGSEGSKDQAGSQEGGLQAEGTTSQGQAEPPAKDASHAQGEHQAVSDSHGQDGSESGGRSVANEEARAEQSPSDGEARVTPGLDERPQGAFWTGEADGDKSGDSDEASREDVLPEPEQRLSGRVTTVLLPLEKLQDESAFKLRPEGDVSGLATDIARLGQLFPVDVRPAGEDRYQLVCGFRRVAALRFLKRDAVQARIHLRLSDEDALVMSLAEAIHATPVGPEVLEAKRDELEAQGRLSAAVRDMLEKALATEDTLAPEGVEEEIDADELAQEVAQRLGAINQDLSLLADVFAALDESRKAELLMQLRYSSELVTYLEGL [Source organism chain B]=Myxococcus xanthus [ExpTech]=X-ray [Resolution]=1.70 [Source organism]=Myxococcus xanthus [Accession]=MF7000990 [Entry] [Entry number]=1175 [Entry name]=Docking domain of Bam_5924 [PDB ID]=6tdd [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=Homodimer of chains with two α-helices and the first 12 residues being disordered (NMR). The highly stable homodimer showed no evidence for dilution-induced dissociation by CD or ITC (PMID:32717326). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q0B304 [UniProt boundaries chain A]=1-41 [UniProt coverage chain A]=1% [Name chain A]=Beta-ketoacyl synthase [UniProt sequence chain A]=MNKPTSSDGWKDDYLSRLSRLSKNQLMALALKLKQQQLEQGPAAEPIAIVGVGCRLPGGVAGPDDYWALLRSAGSGIVEMQDQRWNMAAYFDADPEAGGRIHTRSLGLVDEVDRFDADFFSISPREAESMDPQQRLLLEVAWEAIERSGHACASLDGRQVGVFVGMMNKDYLHLNAPDITGEAARHSPYYASGEAFSIAAGRLAYILGVHGPCMTIDTACSSSLVAVHLACRSLLEDECELALAGGTSLILSPEASIVSSNARMLSPTGQCWSFDHRADGYVRGEGCAVVVLKRLSRALADGDPVLAVIAGSAVNHDGRSQGLTAPNTAAQMALMREALRGAKLDAARIRYVEAHGTGTPLGDPIEMNSIQAVYGEARDEASPLVIGSVKTQIGHTEACAGVAGLIKLALCVAHDRVVPQRNFERLNPHITLRDGVRLALRDEPFGGEAGARYGAVNSFGFSGTNAHLIVRDLPPAAPVAPSLRGPGVLAVSATNAAALDALLLRYRDYLAPGRPEPDWDALAYTSQVGRNHFRERVALTADDIAGLRAALDAAIAARAAAAATAHDEWPPTARAGWVFGVFDMTPSELVAQLRRSSGAFARRFDALVARAAPELAARDDVLAYLTGCAIVETLHDAGLHADALAGADPLGRLVAATAAGLVSVDTVLAWLPLDAAARDVALADWPALPPEIALVDAGSGESRLDTWRDAARRRAWLAQPVEPVPAAHQGGDEAIRWLAIGDLNAAAGKSPAAAPFLFPREFASRSWDPAWAMLYRSGLSLDWSALYGTTRPPRLVLPTYAFQRRRYWPRNAKVEQLRAPARQASAEFRLVWQPAAAPVDISASGAAPARRRIVLAEPGAWSDAAELPAGLQWLPLPEGWRDAQVLAGLLASLEPGAAGAALDLLFWLSPSRVERDDAARRAADTTRGLCVIGQALLALGESAGMRIGFATEGVEQVVEADARQAPNVGDGVVAGFVKTLGFEQPQWRPWVVDLDARADGAAQIVLALDAADDENDVAIRDRQRHVRRLAAATADAADDTHTVDAIDAANAAEASNNATEAAREAPARGDRAYLITGGLGGIGLALARRLARDGAGELVLVSRRGPEDAEARAAHDMLAAAGVPLTWVRADVGDSEALRAGLAAVRLPLGGIYHAAGVLDDAPLQNLTDAHFARVMHAKVAGALNLDRIAREAGVERFVLFSSVAAVVGSAGQANYASANGFLAALGRARRAEGLGATVIHWGPWAEAGMAGPERVRQKIERAGFVLIEPEAALDALQAVLARDEAEAVIARFDWARIADYLADRGARPLFDQVSTAPARPAGASVEMRGEALADAVRELLQQGEAAAARQMQAHAEAIVRKVLAIDAGDAIDPARSLLELGMDSLLSVELRNRFAAQWGLSLPVSLMFDCPSVAAVSRRLLDELRSKEGTAAPRAAAIEMAAGAPRRDEARCDIAVIGMACRMPAGANDVGAFWDQLISGTDMVRPFDGTRWDVPRFYTPGSTEDGKMVANDGGQIADVHGFDNRFFGIGDREAEYMDPQQRIALEVAWETLESAAYTPEQLADGAGVFIGPGPSDFADLSQRHAGALVGLMGPGHHVSAIPGRIAHLFDWQGPCMAIDTACSSSLVAVHVAAQHLRERECRVALAGGVNVILSPANNIVLSKAGMLSPAGRCRTFDVGADGYVRSDGCGMVLLKRLDDALADGDAILGVIRGSAVNHNGRGQGLTAPSSRQQARLIEAALARAGTLPSEIRYVEAHGTGTPLGDPIEMAALKATYGAHRDAADPLYVGAVKSAIGHTESAAGVAGLIKVLLMMRHRMIPPTLHLNTLNPHLEIDPRTIRIPTAPQPLLAREDGTLSCAVSSFGFSGTNAHLIVAAPPGKPARPLARSGRGLFAVSARSLPALARLCERHAVHLARAGTAEPLADLCASTLLGRRRFEHVLCLYPDSHAELIAQLRASAARLRQAPAPAAPAAIDTLALRLVAGAALPAATLAGWHDEPRFAAALAAARDALSAAQAGEPAGEGAPASLDAAWFCVLHALSHCMAAFGVEPDRIDYRGRLWLAAAPIHQAGSLDEAARRFLAADPAPAPKRLGGIALRPADQCEGDEGEGGFLMLRDASGRATRHLDAAAGLDDEAWRRAFGALWEGGRRVDWLAGFAGSAYRRVALPAYPFEHRDCSRPARLPAGERSLELLLEDLQAE [Source organism chain A]=19182 / AMMD) [UniProt ID chain B]=Q0B304 [UniProt boundaries chain B]=1-41 [UniProt coverage chain B]=1% [Name chain B]=Beta-ketoacyl synthase [UniProt sequence chain B]=MNKPTSSDGWKDDYLSRLSRLSKNQLMALALKLKQQQLEQGPAAEPIAIVGVGCRLPGGVAGPDDYWALLRSAGSGIVEMQDQRWNMAAYFDADPEAGGRIHTRSLGLVDEVDRFDADFFSISPREAESMDPQQRLLLEVAWEAIERSGHACASLDGRQVGVFVGMMNKDYLHLNAPDITGEAARHSPYYASGEAFSIAAGRLAYILGVHGPCMTIDTACSSSLVAVHLACRSLLEDECELALAGGTSLILSPEASIVSSNARMLSPTGQCWSFDHRADGYVRGEGCAVVVLKRLSRALADGDPVLAVIAGSAVNHDGRSQGLTAPNTAAQMALMREALRGAKLDAARIRYVEAHGTGTPLGDPIEMNSIQAVYGEARDEASPLVIGSVKTQIGHTEACAGVAGLIKLALCVAHDRVVPQRNFERLNPHITLRDGVRLALRDEPFGGEAGARYGAVNSFGFSGTNAHLIVRDLPPAAPVAPSLRGPGVLAVSATNAAALDALLLRYRDYLAPGRPEPDWDALAYTSQVGRNHFRERVALTADDIAGLRAALDAAIAARAAAAATAHDEWPPTARAGWVFGVFDMTPSELVAQLRRSSGAFARRFDALVARAAPELAARDDVLAYLTGCAIVETLHDAGLHADALAGADPLGRLVAATAAGLVSVDTVLAWLPLDAAARDVALADWPALPPEIALVDAGSGESRLDTWRDAARRRAWLAQPVEPVPAAHQGGDEAIRWLAIGDLNAAAGKSPAAAPFLFPREFASRSWDPAWAMLYRSGLSLDWSALYGTTRPPRLVLPTYAFQRRRYWPRNAKVEQLRAPARQASAEFRLVWQPAAAPVDISASGAAPARRRIVLAEPGAWSDAAELPAGLQWLPLPEGWRDAQVLAGLLASLEPGAAGAALDLLFWLSPSRVERDDAARRAADTTRGLCVIGQALLALGESAGMRIGFATEGVEQVVEADARQAPNVGDGVVAGFVKTLGFEQPQWRPWVVDLDARADGAAQIVLALDAADDENDVAIRDRQRHVRRLAAATADAADDTHTVDAIDAANAAEASNNATEAAREAPARGDRAYLITGGLGGIGLALARRLARDGAGELVLVSRRGPEDAEARAAHDMLAAAGVPLTWVRADVGDSEALRAGLAAVRLPLGGIYHAAGVLDDAPLQNLTDAHFARVMHAKVAGALNLDRIAREAGVERFVLFSSVAAVVGSAGQANYASANGFLAALGRARRAEGLGATVIHWGPWAEAGMAGPERVRQKIERAGFVLIEPEAALDALQAVLARDEAEAVIARFDWARIADYLADRGARPLFDQVSTAPARPAGASVEMRGEALADAVRELLQQGEAAAARQMQAHAEAIVRKVLAIDAGDAIDPARSLLELGMDSLLSVELRNRFAAQWGLSLPVSLMFDCPSVAAVSRRLLDELRSKEGTAAPRAAAIEMAAGAPRRDEARCDIAVIGMACRMPAGANDVGAFWDQLISGTDMVRPFDGTRWDVPRFYTPGSTEDGKMVANDGGQIADVHGFDNRFFGIGDREAEYMDPQQRIALEVAWETLESAAYTPEQLADGAGVFIGPGPSDFADLSQRHAGALVGLMGPGHHVSAIPGRIAHLFDWQGPCMAIDTACSSSLVAVHVAAQHLRERECRVALAGGVNVILSPANNIVLSKAGMLSPAGRCRTFDVGADGYVRSDGCGMVLLKRLDDALADGDAILGVIRGSAVNHNGRGQGLTAPSSRQQARLIEAALARAGTLPSEIRYVEAHGTGTPLGDPIEMAALKATYGAHRDAADPLYVGAVKSAIGHTESAAGVAGLIKVLLMMRHRMIPPTLHLNTLNPHLEIDPRTIRIPTAPQPLLAREDGTLSCAVSSFGFSGTNAHLIVAAPPGKPARPLARSGRGLFAVSARSLPALARLCERHAVHLARAGTAEPLADLCASTLLGRRRFEHVLCLYPDSHAELIAQLRASAARLRQAPAPAAPAAIDTLALRLVAGAALPAATLAGWHDEPRFAAALAAARDALSAAQAGEPAGEGAPASLDAAWFCVLHALSHCMAAFGVEPDRIDYRGRLWLAAAPIHQAGSLDEAARRFLAADPAPAPKRLGGIALRPADQCEGDEGEGGFLMLRDASGRATRHLDAAAGLDDEAWRRAFGALWEGGRRVDWLAGFAGSAYRRVALPAYPFEHRDCSRPARLPAGERSLELLLEDLQAE [Source organism chain B]=19182 / AMMD) [ExpTech]=NMR [Resolution]=N/A [Source organism]=19182 / AMMD) [Accession]=MF7000991 [Entry] [Entry number]=1176 [Entry name]=Dimerization domain of b-TrCP [PDB ID]=2p64 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=All three helices of the D domain monomers self-associate in a right-handed superhelical manner to form a parallel dimer. There is a huge, tightly packed interface (PMID:17574027). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9Y297 [UniProt boundaries chain A]=128-177 [UniProt coverage chain A]=8% [Name chain A]=F-box/WD repeat-containing protein 1A [UniProt sequence chain A]=MDPAEAVLQEKALKFMCSMPRSLWLGCSSLADSMPSLRCLYNPGTGALTAFQNSSEREDCNNGEPPRKIIPEKNSLRQTYNSCARLCLNQETVCLASTAMKTENCVAKTKLANGTSSMIVPKQRKLSASYEKEKELCVKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVRTDSLWRGLAERRGWGQYLFKNKPPDGNAPPNSFYRALYPKIIQDIETIESNWRCGRHSLQRIHCRSETSKGVYCLQYDDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQYDERVIITGSSDSTVRVWDVNTGEMLNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMASPTDITLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLVAALDPRAPAGTLCLRTLVEHSGRVFRLQFDEFQIVSSSHDDTILIWDFLNDPAAQAEPPRSPSRTYTYISR [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9Y297 [UniProt boundaries chain B]=128-177 [UniProt coverage chain B]=8% [Name chain B]=F-box/WD repeat-containing protein 1A [UniProt sequence chain B]=MDPAEAVLQEKALKFMCSMPRSLWLGCSSLADSMPSLRCLYNPGTGALTAFQNSSEREDCNNGEPPRKIIPEKNSLRQTYNSCARLCLNQETVCLASTAMKTENCVAKTKLANGTSSMIVPKQRKLSASYEKEKELCVKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVRTDSLWRGLAERRGWGQYLFKNKPPDGNAPPNSFYRALYPKIIQDIETIESNWRCGRHSLQRIHCRSETSKGVYCLQYDDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQYDERVIITGSSDSTVRVWDVNTGEMLNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMASPTDITLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLVAALDPRAPAGTLCLRTLVEHSGRVFRLQFDEFQIVSSSHDDTILIWDFLNDPAAQAEPPRSPSRTYTYISR [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Homo sapiens [Accession]=MF7000992 [Entry] [Entry number]=1177 [Entry name]=Ttranscriptional regulator BswR [PDB ID]=4o8b [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=DNA-binding HTH domain and helical dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Transcriptional regulator with a Cro/C1-type helix-turn-helix DNA-binding domain and C-termimal helices (α6 and α7) mediating dimerization into an intertwined homodimer, which is the biological function unit (PMID:24497189). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q9I063 [UniProt boundaries chain A]=1-101 [UniProt coverage chain A]=88% [Name chain A]=HTH cro/C1-type domain-containing protein [UniProt sequence chain A]=MLGTRLKAARIRAGYSQKQLGMLVGMDEFSASARMNQYERERHSPNMRTSEQLAMVLQVPMAYLYCPEDELAELILKVSSLTPEFKKELTRFIEQLLAAQGSTSRQPVRTRSEL [Source organism chain A]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [UniProt ID chain A-2]=Q9I063 [UniProt boundaries chain A-2]=1-101 [UniProt coverage chain A-2]=88% [Name chain A-2]=HTH cro/C1-type domain-containing protein [UniProt sequence chain A-2]=MLGTRLKAARIRAGYSQKQLGMLVGMDEFSASARMNQYERERHSPNMRTSEQLAMVLQVPMAYLYCPEDELAELILKVSSLTPEFKKELTRFIEQLLAAQGSTSRQPVRTRSEL [Source organism chain A-2]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=14847 / LMG 12228 / 1C / PRS 101 / PAO1) [Accession]=MF7000993 [Entry] [Entry number]=1178 [Entry name]=Kinesin Neck Domain [PDB ID]=8tt7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The kinesin neck domain consists of a coiled coli homodimer with about five heptad repeats, preceded by a linker region that joins to the ATPase head. The subunits in the structure are bound via coiled coil interactions (PMID:37861970). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P56536 [UniProt boundaries chain A]=325-376 [UniProt coverage chain A]=5% [Name chain A]=Kinesin heavy chain isoform 5C [UniProt sequence chain A]=MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKALKSVIQHLEVELNRWRNGEAVPEDEQISAKDQKNLEPCDNTPIIDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQTDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAVRGGGGSSNSTHYQK [Source organism chain A]=Rattus norvegicus [UniProt ID chain B]=P56536 [UniProt boundaries chain B]=325-376 [UniProt coverage chain B]=5% [Name chain B]=Kinesin heavy chain isoform 5C [UniProt sequence chain B]=MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKALKSVIQHLEVELNRWRNGEAVPEDEQISAKDQKNLEPCDNTPIIDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQTDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAVRGGGGSSNSTHYQK [Source organism chain B]=Rattus norvegicus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Rattus norvegicus [Accession]=MF7000994 [Entry] [Entry number]=1179 [Entry name]=F420-gamma glutamyl ligase (Archaeoglobus fulgidus) [PDB ID]=2phn [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=The F420-gamma glutamyl ligase forms a tightly packed, highly intertwined, butterfly-like dimer formed by two-domain monomers. The dimer interface is very extensive and the putative active site lies in a large groove at the dimer interface. Also, the protein is a dimer in solution (SEC) which is in good agreement with its tight packing (PMID:17669425). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O28028 [UniProt boundaries chain A]=2-249 [UniProt coverage chain A]=99% [Name chain A]=Coenzyme F420:L-glutamate ligase [UniProt sequence chain A]=MRVEVFPVEGLPLIKEGDDLAELISSRVRFEDGDVLVVCSTVISKAEGRIRRLEEFNPSERAKEIAARIGKPAEFVQAVLEESEEVLLDFPFLLVKAKFGNVCVNAGIDASNVEEGSLLLPPLDPDGSAEKLRRRILELTGKRVGVIITDTNGRCFRRGVVGFAIGISGVKAMKDWIGRKDLYGRELEVTVECVADEIAAFANLLMGEGGDGIPAVVVRGLNVAGEGSMEEIYRSEEEDVIRRCLKRCL [Source organism chain A]=100126 / VC-16) [UniProt ID chain B]=O28028 [UniProt boundaries chain B]=1-249 [UniProt coverage chain B]=100% [Name chain B]=Coenzyme F420:L-glutamate ligase [UniProt sequence chain B]=MRVEVFPVEGLPLIKEGDDLAELISSRVRFEDGDVLVVCSTVISKAEGRIRRLEEFNPSERAKEIAARIGKPAEFVQAVLEESEEVLLDFPFLLVKAKFGNVCVNAGIDASNVEEGSLLLPPLDPDGSAEKLRRRILELTGKRVGVIITDTNGRCFRRGVVGFAIGISGVKAMKDWIGRKDLYGRELEVTVECVADEIAAFANLLMGEGGDGIPAVVVRGLNVAGEGSMEEIYRSEEEDVIRRCLKRCL [Source organism chain B]=100126 / VC-16) [ExpTech]=X-ray [Resolution]=1.35 [Source organism]=100126 / VC-16) [Accession]=MF7000995 [Entry] [Entry number]=1180 [Entry name]=Rpgrip1l CC2 [PDB ID]=7yfu [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:36915689). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q8CG73 [UniProt boundaries chain A]=104-143 [UniProt coverage chain A]=3% [Name chain A]=Protein fantom [UniProt sequence chain A]=MSGPSDETAGDLPVKDTGLNLFGVGGLQETSTARTVKTRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRFQNVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSERRVEELQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLRASGDKELVTFCTYAFYDFELQTTPIVRGLYPEYNFTSQYLVHVNDLFLQYIQKNTVTLELHQAHSTDYETIAACQLRFHEILEKSGRIFCTTSLVGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKKPEKMQLSSQQAATTAQISPAESTDGNLNELHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYMGKVNVPLISLAHDKCISGIFELMDKEKHAAGTIQVILKWKFTYLPPSGSITTEDLGKFVCREEPEAVQRLPPKSSDVTSVVAPKPKPRQRLTFVDKKVSFADTISHPSPETSPPPKDIKDSSPEVGPKPENGLSAVAYPSKESGVAKVEENVGEMQQGKEDDISFLSEGQLASGSVASSEDETEITEELEPEDEDRSASDSDDCIIPSSVSTNTKQPSEEIRIEIIALNLNDSQITREDTIQRLFIECRFYSLPAEETPMSLPKPQSGQWVYYNYSNVIYLDKENNPAVRDILKAILQRRELPHRSVRFTVVSDPPEDEQDLECEDIGVAHVDLADLFQKGRDIIEQDIDVLDARTDGGTIGKLKVTVEALHALRSVYEQNRKDLEA [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q8CG73 [UniProt boundaries chain B]=104-143 [UniProt coverage chain B]=3% [Name chain B]=Protein fantom [UniProt sequence chain B]=MSGPSDETAGDLPVKDTGLNLFGVGGLQETSTARTVKTRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRFQNVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSERRVEELQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLRASGDKELVTFCTYAFYDFELQTTPIVRGLYPEYNFTSQYLVHVNDLFLQYIQKNTVTLELHQAHSTDYETIAACQLRFHEILEKSGRIFCTTSLVGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKKPEKMQLSSQQAATTAQISPAESTDGNLNELHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYMGKVNVPLISLAHDKCISGIFELMDKEKHAAGTIQVILKWKFTYLPPSGSITTEDLGKFVCREEPEAVQRLPPKSSDVTSVVAPKPKPRQRLTFVDKKVSFADTISHPSPETSPPPKDIKDSSPEVGPKPENGLSAVAYPSKESGVAKVEENVGEMQQGKEDDISFLSEGQLASGSVASSEDETEITEELEPEDEDRSASDSDDCIIPSSVSTNTKQPSEEIRIEIIALNLNDSQITREDTIQRLFIECRFYSLPAEETPMSLPKPQSGQWVYYNYSNVIYLDKENNPAVRDILKAILQRRELPHRSVRFTVVSDPPEDEQDLECEDIGVAHVDLADLFQKGRDIIEQDIDVLDARTDGGTIGKLKVTVEALHALRSVYEQNRKDLEA [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Mus musculus [Accession]=MF7000996 [Entry] [Entry number]=1181 [Entry name]=Rv1738 (Mycobacterium tuberculosis) [PDB ID]=4wpy [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=There is no direct information on the stability of the monomeric form, but the Rv1738 polypeptides form an intimately associated homodimer with a three-stranded anti-parallel β-sheet packed against a long amphipathic α-helix in each monomer. The dimer is arranged in two layers. The antiparallel β-sheets are paired to form an extended six-stranded β-sheet which wraps around the two antiparallel C-terminal α-helices, which pack against the β-sheet and make intimate side chain–side chain interactions with each other (PMID:25831534). The homologous human SSM-‘RBD’5 homodimerizes in solution and in cells (PMID:23524536). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=P9WLS2 [UniProt boundaries chain A]=7-94 [UniProt coverage chain A]=93% [Name chain A]=Uncharacterized protein MT1780 [UniProt sequence chain A]=MCGDQSDHVLQHWTVDISIDEHEGLTRAKARLRWREKELVGVGLARLNPADRNVPEIGDELSVARALSDLGKRMLKVSTHDIEAVTHQPARLLY [Source organism chain A]=Mycobacterium tuberculosis [UniProt ID chain A-2]=P9WLS2 [UniProt boundaries chain A-2]=7-94 [UniProt coverage chain A-2]=93% [Name chain A-2]=Uncharacterized protein MT1780 [UniProt sequence chain A-2]=MCGDQSDHVLQHWTVDISIDEHEGLTRAKARLRWREKELVGVGLARLNPADRNVPEIGDELSVARALSDLGKRMLKVSTHDIEAVTHQPARLLY [Source organism chain A-2]=Mycobacterium tuberculosis [ExpTech]=X-ray [Resolution]=1.50 [Source organism]=Mycobacterium tuberculosis [Accession]=MF7000997 [Entry] [Entry number]=1182 [Entry name]=RNA-binding domain of Nodamura virus protein b2 [PDB ID]=3g80 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=4-helix bundle [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=NMV B2 forms an elongated dimer with the monomers arranged in a head-to-tail fashion, forming a four-helix bundle at the core. The dimer is primarily stabilized by hydrophobic interactions, involving approximately 50% of the amino acids. The RNA-binding site is contributed by both monomers of the dimer, suggesting that a minimal dimer is required for RNA binding by B2 proteins. The purified protein is in dimeric form according to gel filtration (PMID:19249868). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q9IMM3 [UniProt boundaries chain A]=5-77 [UniProt coverage chain A]=53% [Name chain A]=Protein B2 [UniProt sequence chain A]=MTNMSCAYELIKSLPAKLEQLAQETQATIQTLMIADPNVNKDLRAFCEFLTVQHQRAYRATNSLLIKPRVAAALRGEELDLGEADVAARVRQLKQQLAELEMEIKPGHQQVAQVSGRRKAAAAAPVAQLGRVGVVNE [Source organism chain A]=Nodamura virus [UniProt ID chain B]=Q9IMM3 [UniProt boundaries chain B]=6-78 [UniProt coverage chain B]=53% [Name chain B]=Protein B2 [UniProt sequence chain B]=MTNMSCAYELIKSLPAKLEQLAQETQATIQTLMIADPNVNKDLRAFCEFLTVQHQRAYRATNSLLIKPRVAAALRGEELDLGEADVAARVRQLKQQLAELEMEIKPGHQQVAQVSGRRKAAAAAPVAQLGRVGVVNE [Source organism chain B]=Nodamura virus [ExpTech]=X-ray [Resolution]=2.50 [Source organism]=Nodamura virus [Accession]=MF7000998 [Entry] [Entry number]=1183 [Entry name]=Dimerization domain of DGCR8 (frog) [PDB ID]=4e5r [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=SEC analyses indicated that the bat star HBD is a dimer in solution. The subunits are held together by an extensive interface mainly mediated by hydrophobic interactions. The WW motif folds into three β-strands (β1–β3) and a fourth β-strand (β4) interacts with the WW motif of the partner subunit, forming a continuous β-sheet and resulting in an apparently domain-swapped dimer (PMID:22768307). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q6IRB5 [UniProt boundaries chain A]=300-355 [UniProt coverage chain A]=7% [Name chain A]=MGC78846 protein [UniProt sequence chain A]=MEECEEVAPFPEVNGHDVTEMNPASPPPLPPEEEPPPPPLQTSSDAEVMDVGSGGDGQSQTPAGDLQQNNGLQLFTKGSTSYKSHRTVLDPFHSDQSPRTARHAPSNKRFTPDLKLLKDVKVSVSFTESCRSKDRHVLYTGLECEGSLHGGSNMNSVNGDMYVCPFAGSSNGNVTDSIEITLKKNYEPEIEQEKKVEYAVLDELEDFTENVMDVDEDGAEFVSESILQREKIDEEALIYSYEDEFDNDVDALLEESLHTPKKRRIDEKYDIDSDHQSDGESSVQPMVTKIKTVLKSRGRPPTEPLPDGWIMTFHNSGLPVYLHRETRVVTWSRPYFLGTGSIRKHDPPISSIPCLHYKKMKDNDIKEQSNDVTSALVSVSSSTKSSDTSHNSEEPDTTAADSFVSDERESVSEVAQGALGQVKAKVEVCKDESINLEDFRSYLEKRFDFEQVTVKKFRTWAERRQFNREMKRKQAECERPILPANQKLITLSVQDAPTKKEFVINPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVIINGVTYGTGTASSKKLAKNKAARATLEILIPDFVKQTCIEKPKDTDELEYFNHISIEDSRVYELTNKAGLLSPYQILHECLKRNHGMGDTSIKFEVIPGKNQKSEYVMTCGKHTVRGWCKNKRVGKQLASQKILQLLHPHVKNWGSLLRMYGRENSKIVKQETADKSVIELQQFAKKNKPNLHILNKLQEEMRRLAQEREETRKKPKMTIVESAQPGSEPLCTVDV [Source organism chain A]=Xenopus laevis [UniProt ID chain A-2]=Q6IRB5 [UniProt boundaries chain A-2]=300-355 [UniProt coverage chain A-2]=7% [Name chain A-2]=MGC78846 protein [UniProt sequence chain A-2]=MEECEEVAPFPEVNGHDVTEMNPASPPPLPPEEEPPPPPLQTSSDAEVMDVGSGGDGQSQTPAGDLQQNNGLQLFTKGSTSYKSHRTVLDPFHSDQSPRTARHAPSNKRFTPDLKLLKDVKVSVSFTESCRSKDRHVLYTGLECEGSLHGGSNMNSVNGDMYVCPFAGSSNGNVTDSIEITLKKNYEPEIEQEKKVEYAVLDELEDFTENVMDVDEDGAEFVSESILQREKIDEEALIYSYEDEFDNDVDALLEESLHTPKKRRIDEKYDIDSDHQSDGESSVQPMVTKIKTVLKSRGRPPTEPLPDGWIMTFHNSGLPVYLHRETRVVTWSRPYFLGTGSIRKHDPPISSIPCLHYKKMKDNDIKEQSNDVTSALVSVSSSTKSSDTSHNSEEPDTTAADSFVSDERESVSEVAQGALGQVKAKVEVCKDESINLEDFRSYLEKRFDFEQVTVKKFRTWAERRQFNREMKRKQAECERPILPANQKLITLSVQDAPTKKEFVINPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVIINGVTYGTGTASSKKLAKNKAARATLEILIPDFVKQTCIEKPKDTDELEYFNHISIEDSRVYELTNKAGLLSPYQILHECLKRNHGMGDTSIKFEVIPGKNQKSEYVMTCGKHTVRGWCKNKRVGKQLASQKILQLLHPHVKNWGSLLRMYGRENSKIVKQETADKSVIELQQFAKKNKPNLHILNKLQEEMRRLAQEREETRKKPKMTIVESAQPGSEPLCTVDV [Source organism chain A-2]=Xenopus laevis [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Xenopus laevis [Accession]=MF7000999 [Entry] [Entry number]=1184 [Entry name]=N-domain of FKBP22 (Shewanella sp. SIB1) [PDB ID]=3b09 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=There is a Val-Leu knot at the core of the dimer interface, contributing to the cohesion of the dimer structure in a hydrophobic zipper-like manner. It was also proved that dimerisation is required for the folding of the domain (PMID:21837652). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=Q765B0 [UniProt boundaries chain A]=3-67 [UniProt coverage chain A]=31% [Name chain A]=Peptidyl-prolyl cis-trans isomerase [UniProt sequence chain A]=MSDLFSTMEQHASYGVGRQMGEQLAANSFEGIDIPAVQAGLADAFAGKESAVSMEELQVAFTEISRRLQAAQEAAAEAAAAEGDTFLAENAKRDGITITESGLQYEVLVQGDGETPTYDSTVRTHYHGTFISGDVFDSSVARGQPAEFPVSGVIAGWTEALQLMPVGTKLKLYVPHHLAYGERGAGASIPPYSALVFEVELLEII [Source organism chain A]=Shewanella sp SIB1 [UniProt ID chain A-2]=Q765B0 [UniProt boundaries chain A-2]=3-67 [UniProt coverage chain A-2]=31% [Name chain A-2]=Peptidyl-prolyl cis-trans isomerase [UniProt sequence chain A-2]=MSDLFSTMEQHASYGVGRQMGEQLAANSFEGIDIPAVQAGLADAFAGKESAVSMEELQVAFTEISRRLQAAQEAAAEAAAAEGDTFLAENAKRDGITITESGLQYEVLVQGDGETPTYDSTVRTHYHGTFISGDVFDSSVARGQPAEFPVSGVIAGWTEALQLMPVGTKLKLYVPHHLAYGERGAGASIPPYSALVFEVELLEII [Source organism chain A-2]=Shewanella sp SIB1 [ExpTech]=X-ray [Resolution]=1.90 [Source organism]=Shewanella sp SIB1 [Accession]=MF7001000 [Entry] [Entry number]=1185 [Entry name]=Human interleukin-5 [PDB ID]=1hul [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Four-helical cytokine-like, core [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Interleukin 5 forms a very tight, S-S bond dimer, with extensive exchange of secondary structure elements and a large, hydrophobic interface. Authors suggest that the monomer would not be stable on its own due to high number of hydrophobic residues on the surface (PMID:8483502). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P05113 [UniProt boundaries chain A]=24-131 [UniProt coverage chain A]=80% [Name chain A]=Interleukin-5 [UniProt sequence chain A]=MRMLLHLSLLALGAAYVYAIPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWIIES [Source organism chain A]=Homo sapiens [UniProt ID chain B]=P05113 [UniProt boundaries chain B]=24-131 [UniProt coverage chain B]=80% [Name chain B]=Interleukin-5 [UniProt sequence chain B]=MRMLLHLSLLALGAAYVYAIPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWIIES [Source organism chain B]=Homo sapiens [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=Homo sapiens [Accession]=MF7001001 [Entry] [Entry number]=1186 [Entry name]=Ureidoglycolate hydrolase (AllA) (Escherichia coli O157:H7) [PDB ID]=1yqc [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=Domain-swapped dimer with beta sheet augmentation and an extensive interface. Face-to-face interactions of 5-stranded b-sheets of the two monomers. Both monomers contribute to the putative active site (PMID:16114032). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P63486 [UniProt boundaries chain A]=1-160 [UniProt coverage chain A]=100% [Name chain A]=Ureidoglycolate lyase [UniProt sequence chain A]=MKLQVLPLSQEAFSAYGDVIETQQRDFFHINNGLVERYHDLALVEILEQDRTLISINRAQPANLPLTIHELERHPLGTQAFIPMKGEVFVVVVALGDDKPDLSTLRAFITNGEQGVNYHRNVWHHPLFAWQRVTDFLTIDRGGSDNCDVESIPEQELCFA [Source organism chain A]=Escherichia coli O157:H7 [UniProt ID chain B]=P63486 [UniProt boundaries chain B]=1-160 [UniProt coverage chain B]=100% [Name chain B]=Ureidoglycolate lyase [UniProt sequence chain B]=MKLQVLPLSQEAFSAYGDVIETQQRDFFHINNGLVERYHDLALVEILEQDRTLISINRAQPANLPLTIHELERHPLGTQAFIPMKGEVFVVVVALGDDKPDLSTLRAFITNGEQGVNYHRNVWHHPLFAWQRVTDFLTIDRGGSDNCDVESIPEQELCFA [Source organism chain B]=Escherichia coli O157:H7 [ExpTech]=X-ray [Resolution]=1.71 [Source organism]=Escherichia coli O157:H7 [Accession]=MF7001002 [Entry] [Entry number]=1187 [Entry name]=Vps27/Hse1 complex [PDB ID]=2pjw [Chains]=H,V [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=All-helical dimerization domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The two GAT domains are connected by an antiparallel coiled coil, forming a 90 A-long barbell-like structure (PMID:17543868). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain H]=N/A [Evidence chain V]=N/A [Similar structures]=None [UniProt ID chain H]=P38753 [UniProt boundaries chain H]=288-375 [UniProt coverage chain H]=19% [Name chain H]=Class E vacuolar protein-sorting machinery protein HSE1 [UniProt sequence chain H]=MSSSAIKIRNALLKATDPKLRSDNWQYILDVCDLVKEDPEDNGQEVMSLIEKRLEQQDANVILRTLSLTVSLAENCGSRLRQEISSKNFTSLLYALIESHSVHITLKKAVTDVVKQLSDSFKDDPSLRAMGDLYDKIKRKAPYLVQPNVPEKHNMSTQADNSDDEELQKALKMSLFEYEKQKKLQEQEKESAEVLPQQQQQHQQQNQAPAHKIPAQTVVRRVRALYDLTTNEPDELSFRKGDVITVLEQVYRDWWKGALRGNMGIFPLNYVTPIVEPSKEEIEKEKNKEAIVFSQKTTIDQLHNSLNAASKTGNSNEVLQDPHIGDMYGSVTPLRPQVTRMLGKYAKEKEDMLSLRQVLANAERSYNQLMDRAANAHISPPVPGPALYAGMTHANNTPVMPPQRQSYQSNEYSPYPSNLPIQHPTNSANNTPQYGYDLGYSVVSQPPPGYEQ [Source organism chain H]=Saccharomyces cerevisiae [UniProt ID chain V]=P40343 [UniProt boundaries chain V]=348-438 [UniProt coverage chain V]=14% [Name chain V]=Vacuolar protein sorting-associated protein 27 [UniProt sequence chain V]=MSVSTPSELDALIEQATSESIPNGDLDLPIALEISDVLRSRRVNPKDSMRCIKKRILNTADNPNTQLSSWKLTNICVKNGGTPFIKEICSREFMDTMEHVILREDSNEELSELVKTILYELYVAFKNDSQLNYVAKVYDKLISRGIKFPEKLTLSNSPTAMFDSKTPADWIDSDACMICSKKFSLLNRKHHCRSCGGVFCQEHSSNSIPLPDLGIYEPVRVCDSCFEDYDLKRHDDSKKSKKHRHKRKKDRDYSTPEDEEELIRKAIELSLKESRNSASSEPIVPVVESKNEVKRQEIEEEEDPDLKAAIQESLREAEEAKLRSERQKASRQMQPQQPSPQPQPIHSVDLSDEEKDSIYMFASLVEKMKSRPLNEILEDSKLQNLAQRVFASKARLNYALNDKAQKYNTLIEMNGKISEIMNIYDRLLEQQLQSINLSQQYTLPQVPSDPYNYLTENVQNPAESYQTPPLQQLSSHQYKPQQDVSRQQSVKANSSPTTNIDHLKTIDVTPHAQQKPQSHVELAPSDPPYPKEEAEDEGTQAVQDEESSTQESRERPYPVETENGETSINKRPQGITRYDFPTVPARKFVQPESTVPLPASSSEIPIKEERPPSPQEELLIEL [Source organism chain V]=Saccharomyces cerevisiae [ExpTech]=X-ray [Resolution]=3.01 [Source organism]=Saccharomyces cerevisiae [Accession]=MF7001003 [Entry] [Entry number]=1188 [Entry name]=Lysinoalanine synthase, DurN [PDB ID]=6c0g [Chains]=A,B-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Homooligomeric enzymes [Subclass]=Homodimeric enzymes [Sequence domain]=- [Evidence level]=No contradicting information [Evidence text]=The overall structure of DurN consists of an interlaced homodimer where helix α1 is engaged with residues from helices α2–α6 in the adjacent monomer. An intermolecular, antiparallel β-strand is also formed between the monomers (PMID:30177849). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B-2]=N/A [Similar structures]=None [UniProt ID chain A]=A0A3F2YLX1 [UniProt boundaries chain A]=8-121 [UniProt coverage chain A]=94% [Name chain A]=Lysinoalanine synthase [UniProt sequence chain A]=SGMKSAKEPTIYQDVDIIRRIQELMVLCSLLPPDGKLREALELALALHEEPALARITPLTNLHPFATKAWLETLWLGEGVSSEEKELVAWQNKSENMGPAIRELKNAEQQSGITLVARLTS [Source organism chain A]=Streptomyces cinnamoneus [UniProt ID chain B-2]=A0A3F2YLX1 [UniProt boundaries chain B-2]=8-121 [UniProt coverage chain B-2]=94% [Name chain B-2]=Lysinoalanine synthase [UniProt sequence chain B-2]=SGMKSAKEPTIYQDVDIIRRIQELMVLCSLLPPDGKLREALELALALHEEPALARITPLTNLHPFATKAWLETLWLGEGVSSEEKELVAWQNKSENMGPAIRELKNAEQQSGITLVARLTS [Source organism chain B-2]=Streptomyces cinnamoneus [ExpTech]=X-ray [Resolution]=2.15 [Source organism]=Streptomyces cinnamoneus [Accession]=MF7001004 [Entry] [Entry number]=1189 [Entry name]=PALB2 homodimer (Escherichia coli) [PDB ID]=6e4h [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Leucine zipper (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The PALB2cc homodimer is a classical antiparallel coiled-coil leucine zipper. Backbone amide circular dichroism (CD) analysis demonstrates that PALB2cc exhibits a highly-cooperative thermal folding/unfolding equilibrium (PMID:30289697). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q3U0P1 [UniProt boundaries chain A]=1-60 [UniProt coverage chain A]=5% [Name chain A]=Partner and localizer of BRCA2 [UniProt sequence chain A]=MEELSGKPLSYAEKEKLKEKLAFLKKEYSRTLARLQRAKRAEKAKNSKKAIEDGVPQPEASSQLSHSESINKGFPCDTLQSNHLDEETGENISQILDVEPQSFNCKQGKEVLHTPRAGDIQGQLLHSTSSPDGKKEQNTLPGTTKTPWEKSSVSQEKEDYFDTNSLALLGKHRKGQESISRKNSRTPVSEKTHLLSLRSQIPDPPALVTGIGEGILIPPSGKSERGIDTLVRGNTVSAEAAVPSCTASNSNHSQHLEHTPPKSGCKITTQGPASSTNLVAQDQKMTIFTVNSVVYKAVRAHGQLPGSPNSCSVNDLTHSNLPANSTPNSKSLKSPSNTVDERNEPLQEDEILGPSKNFNLAAVSPPSTESQIHSCTMLEGLLFPAEYYVRTTRRMSDCQRKIALEAVIQSHLGVKKKELKKKTKATKAVVLSSEDTDQSESGMLDTSTGQSSSGSLSQKLLSPAEVSSPPGPAGKATTPPPGRGHRGKRKSARTSTLGHCQLLFPPCAALAVNRSKGKFTKHKCQNRGVVIHDFELPDEDFGLLKLEKLKSCSEKLIESPDSKNCGERLPREGNHAALEELQRDSETEGLEEELTVPPGEAYRPGPTLRRQPGSKDLSSSIVLFTPADTAAPNDSGRPPPSLCSPAFPILGMTPALGSQAAGETLSTEAAQPCSTSQPPLLGDTNSLVNNSKQCNSSACSPKPDTNLQASGRQGQPACDSDSGPQATPLPVESFTFRENQLCGNACLELHEHSTEQTETADRPACDNLNPGNLQLVSELKNPSSSCSVDVSAMWWERAGAKEPCIVTACEDVVSLWKPLNSLQWEKVHTWHFTEVPVLQIVPVPDVYNLICVALGSLEIREIRALLCSSGDDSEKQVLLKSGDIKAMLGLTKRRLVSSTGTFCNQQIQIMTFADDGSSKDEQLLMPPDETVLTFAEVQGTQEALLGTTTVNSIVIWNLKTGQLLKKMHIDDSYQASVCHGAYSEKGLLFVVVSQPCAKESQALGSPVFQLLVINPKTAQSVGVLLCSLPQGQAGRFLEGDVKDHVAAAVLTSGTIAIWDLLLGHCTALLPPVSDQSWSLVKWSGTDSHLLAGQKDGNIFIYRYF [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q3U0P1 [UniProt boundaries chain B]=1-60 [UniProt coverage chain B]=5% [Name chain B]=Partner and localizer of BRCA2 [UniProt sequence chain B]=MEELSGKPLSYAEKEKLKEKLAFLKKEYSRTLARLQRAKRAEKAKNSKKAIEDGVPQPEASSQLSHSESINKGFPCDTLQSNHLDEETGENISQILDVEPQSFNCKQGKEVLHTPRAGDIQGQLLHSTSSPDGKKEQNTLPGTTKTPWEKSSVSQEKEDYFDTNSLALLGKHRKGQESISRKNSRTPVSEKTHLLSLRSQIPDPPALVTGIGEGILIPPSGKSERGIDTLVRGNTVSAEAAVPSCTASNSNHSQHLEHTPPKSGCKITTQGPASSTNLVAQDQKMTIFTVNSVVYKAVRAHGQLPGSPNSCSVNDLTHSNLPANSTPNSKSLKSPSNTVDERNEPLQEDEILGPSKNFNLAAVSPPSTESQIHSCTMLEGLLFPAEYYVRTTRRMSDCQRKIALEAVIQSHLGVKKKELKKKTKATKAVVLSSEDTDQSESGMLDTSTGQSSSGSLSQKLLSPAEVSSPPGPAGKATTPPPGRGHRGKRKSARTSTLGHCQLLFPPCAALAVNRSKGKFTKHKCQNRGVVIHDFELPDEDFGLLKLEKLKSCSEKLIESPDSKNCGERLPREGNHAALEELQRDSETEGLEEELTVPPGEAYRPGPTLRRQPGSKDLSSSIVLFTPADTAAPNDSGRPPPSLCSPAFPILGMTPALGSQAAGETLSTEAAQPCSTSQPPLLGDTNSLVNNSKQCNSSACSPKPDTNLQASGRQGQPACDSDSGPQATPLPVESFTFRENQLCGNACLELHEHSTEQTETADRPACDNLNPGNLQLVSELKNPSSSCSVDVSAMWWERAGAKEPCIVTACEDVVSLWKPLNSLQWEKVHTWHFTEVPVLQIVPVPDVYNLICVALGSLEIREIRALLCSSGDDSEKQVLLKSGDIKAMLGLTKRRLVSSTGTFCNQQIQIMTFADDGSSKDEQLLMPPDETVLTFAEVQGTQEALLGTTTVNSIVIWNLKTGQLLKKMHIDDSYQASVCHGAYSEKGLLFVVVSQPCAKESQALGSPVFQLLVINPKTAQSVGVLLCSLPQGQAGRFLEGDVKDHVAAAVLTSGTIAIWDLLLGHCTALLPPVSDQSWSLVKWSGTDSHLLAGQKDGNIFIYRYF [Source organism chain B]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus [Accession]=MF7001005 [Entry] [Entry number]=1190 [Entry name]=N-terminal dimer domain of DsbC (Escherichia coli) [PDB ID]=2iyj [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=No contradicting information [Evidence text]=Tight dimer with beta sheet augmentation, there is no information on the stability of the monomers (PMID:17372350). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q14F36 [UniProt boundaries chain A]=5-74 [UniProt coverage chain A]=40% [Name chain A]=Thiol:disulfide interchange protein [UniProt sequence chain A]=FAQADDAAIQQTLAKMGIKSSDIQPAPVAGMKTVLTNSGVLYITDDGKHIIQGPMYDVSGTAPVNVTNKMLLKQLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMADYNALGITVRYLAFPRQGLDSDAEKEMKAIWCAKDKNKAFDDVMAGKSVAPASCDVDIA [Source organism chain A]=Escherichia coli [UniProt ID chain B]=Q14F36 [UniProt boundaries chain B]=3-75 [UniProt coverage chain B]=42% [Name chain B]=Thiol:disulfide interchange protein [UniProt sequence chain B]=FAQADDAAIQQTLAKMGIKSSDIQPAPVAGMKTVLTNSGVLYITDDGKHIIQGPMYDVSGTAPVNVTNKMLLKQLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMADYNALGITVRYLAFPRQGLDSDAEKEMKAIWCAKDKNKAFDDVMAGKSVAPASCDVDIA [Source organism chain B]=Escherichia coli [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Escherichia coli [Accession]=MF7001006 [Entry] [Entry number]=1191 [Entry name]=ArsR As(III)-responsive repressor [PDB ID]=6j05 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=Dimer with five α-helices and two β-strands per monomer, forming a winged helix-like DNA binding domain (ArsR-type) and a helical dimerization subdomain formed by the α1 and α5 helices from both monomers (PMID:31136796). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=B7J952 [UniProt boundaries chain A]=5-105 [UniProt coverage chain A]=85% [Name chain A]=Transcriptional regulator, ArsR [UniProt sequence chain A]=MEPLQDPAQIVARLEALASPVRLEIFRLLVEQEPTGLVSGDIAEHLGQPHNGISFHLKNLQHAGLVTVQREGRYQRYRAAMPVVRALVAYLTENCCHGTRDCALSGETRSPSVQEGNQ [Source organism chain A]=/ NCIMB 8455) [UniProt ID chain B]=B7J952 [UniProt boundaries chain B]=4-93 [UniProt coverage chain B]=76% [Name chain B]=Transcriptional regulator, ArsR [UniProt sequence chain B]=MEPLQDPAQIVARLEALASPVRLEIFRLLVEQEPTGLVSGDIAEHLGQPHNGISFHLKNLQHAGLVTVQREGRYQRYRAAMPVVRALVAYLTENCCHGTRDCALSGETRSPSVQEGNQ [Source organism chain B]=/ NCIMB 8455) [ExpTech]=X-ray [Resolution]=1.86 [Source organism]=/ NCIMB 8455) [Accession]=MF7001007 [Entry] [Entry number]=1192 [Entry name]=GPS2 53-90 and SMRT 167-207 [PDB ID]=2l5g [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:21240272). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q13227 [UniProt boundaries chain A]=53-90 [UniProt coverage chain A]=11% [Name chain A]=G protein pathway suppressor 2 [UniProt sequence chain A]=MPALLERPKLSNAMARALHRHIMMERERKRQEEEEVDKMMEQKMKEEQERRKKKEMEERMSLEETKEQILKLEEKLLALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTSAAYQQSLTVHTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTRHYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTGFLQPGGALSLQKQMEHANQQTGFSDSSSLRPMHPQALHPAPGLLASPQLPVQMQPAGKSGFAATSQPGPRLPFIQHSQNPRFYHK [Source organism chain A]=Homo sapiens [UniProt ID chain B]=Q9Y618 [UniProt boundaries chain B]=167-207 [UniProt coverage chain B]=1% [Name chain B]=Nuclear receptor corepressor 2 [UniProt sequence chain B]=MSGSTQPVAQTWRATEPRYPPHSLSYPVQIARTHTDVGLLEYQHHSRDYASHLSPGSIIQPQRRRPSLLSEFQPGNERSQELHLRPESHSYLPELGKSEMEFIESKRPRLELLPDPLLRPSPLLATGQPAGSEDLTKDRSLTGKLEPVSPPSPPHTDPELELVPPRLSKEELIQNMDRVDREITMVEQQISKLKKKQQQLEEEAAKPPEPEKPVSPPPIESKHRSLVQIIYDENRKKAEAAHRILEGLGPQVELPLYNQPSDTRQYHENIKINQAMRKKLILYFKRRNHARKQWEQKFCQRYDQLMEAWEKKVERIENNPRRRAKESKVREYYEKQFPEIRKQRELQERMQSRVGQRGSGLSMSAARSEHEVSEIIDGLSEQENLEKQMRQLAVIPPMLYDADQQRIKFINMNGLMADPMKVYKDRQVMNMWSEQEKETFREKFMQHPKNFGLIASFLERKTVAECVLYYYLTKKNENYKSLVRRSYRRRGKSQQQQQQQQQQQQQQQQQPMPRSSQEEKDEKEKEKEAEKEEEKPEVENDKEDLLKEKTDDTSGEDNDEKEAVASKGRKTANSQGRRKGRITRSMANEANSEEAITPQQSAELASMELNESSRWTEEEMETAKKGLLEHGRNWSAIARMVGSKTVSQCKNFYFNYKKRQNLDEILQQHKLKMEKERNARRKKKKAPAAASEEAAFPPVVEDEEMEASGVSGNEEEMVEEAEALHASGNEVPRGECSGPATVNNSSDTESIPSPHTEAAKDTGQNGPKPPATLGADGPPPGPPTPPPEDIPAPTEPTPASEATGAPTPPPAPPSPSAPPPVVPKEEKEEETAAAPPVEEGEEQKPPAAEELAVDTGKAEEPVKSECTEEAEEGPAKGKDAEAAEATAEGALKAEKKEGGSGRATTAKSSGAPQDSDSSATCSADEVDEAEGGDKNRLLSPRPSLLTPTGDPRANASPQKPLDLKQLKQRAAAIPPIQVTKVHEPPREDAAPTKPAPPAPPPPQNLQPESDAPQQPGSSPRGKSRSPAPPADKEAFAAEAQKLPGDPPCWTSGLPFPVPPREVIKASPHAPDPSAFSYAPPGHPLPLGLHDTARPVLPRPPTISNPPPLISSAKHPSVLERQIGAISQGMSVQLHVPYSEHAKAPVGPVTMGLPLPMDPKKLAPFSGVKQEQLSPRGQAGPPESLGVPTAQEASVLRGTALGSVPGGSITKGIPSTRVPSDSAITYRGSITHGTPADVLYKGTITRIIGEDSPSRLDRGREDSLPKGHVIYEGKKGHVLSYEGGMSVTQCSKEDGRSSSGPPHETAAPKRTYDMMEGRVGRAISSASIEGLMGRAIPPERHSPHHLKEQHHIRGSITQGIPRSYVEAQEDYLRREAKLLKREGTPPPPPPSRDLTEAYKTQALGPLKLKPAHEGLVATVKEAGRSIHEIPREELRHTPELPLAPRPLKEGSITQGTPLKYDTGASTTGSKKHDVRSLIGSPGRTFPPVHPLDVMADARALERACYEESLKSRPGTASSSGGSIARGAPVIVPELGKPRQSPLTYEDHGAPFAGHLPRGSPVTTREPTPRLQEGSLSSSKASQDRKLTSTPREIAKSPHSTVPEHHPHPISPYEHLLRGVSGVDLYRSHIPLAFDPTSIPRGIPLDAAAAYYLPRHLAPNPTYPHLYPPYLIRGYPDTAALENRQTIINDYITSQQMHHNAATAMAQRADMLRGLSPRESSLALNYAAGPRGIIDLSQVPHLPVLVPPTPGTPATAMDRLAYLPTAPQPFSSRHSSSPLSPGGPTHLTKPTTTSSSERERDRDRERDRDREREKSILTSTTTVEHAPIWRPGTEQSSGSSGGGGGSSSRPASHSHAHQHSPISPRTQDALQQRPSVLHNTGMKGIITAVEPSTPTVLRSTSTSSPVRPAATFPPATHCPLGGTLDGVYPTLMEPVLLPKEAPRVARPERPRADTGHAFLAKPPARSGLEPASSPSKGSEPRPLVPPVSGHATIARTPAKNLAPHHASPDPPAPPASASDPHREKTQSKPFSIQELELRSLGYHGSSYSPEGVEPVSPVSSPSLTHDKGLPKHLEELDKSHLEGELRPKQPGPVKLGGEAAHLPHLRPLPESQPSSSPLLQTAPGVKGHQRVVTLAQHISEVITQDYTRHHPQQLSAPLPAPLYSFPGASCPVLDLRRPPSDLYLPPPDHGAPARGSPHSEGGKRSPEPNKTSVLGGGEDGIEPVSPPEGMTEPGHSRSAVYPLLYRDGEQTEPSRMGSKSPGNTSQPPAFFSKLTESNSAMVKSKKQEINKKLNTHNRNEPEYNISQPGTEIFNMPAITGTGLMTYRSQAVQEHASTNMGLEAIIRKALMGKYDQWEESPPLSANAFNPLNASASLPAAMPITAADGRSDHTLTSPGGGGKAKVSGRPSSRKAKSPAPGLASGDRPPSVSSVHSEGDCNRRTPLTNRVWEDRPSSAGSTPFPYNPLIMRLQAGVMASPPPPGLPAGSGPLAGPHHAWDEEPKPLLCSQYETLSDSE [Source organism chain B]=Homo sapiens [ExpTech]=NMR [Resolution]=N/A [Source organism]=Homo sapiens [Accession]=MF7001008 [Entry] [Entry number]=1193 [Entry name]=Pathogenicity island 1 protein gp6 (Staphylococcus aureus) [PDB ID]=2l8t [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=4-helix bundle [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=Full-length, His6-tagged SaPI1 gp6 protein was found to exist as a stable dimer by AUC. The gp6 dimer consists of a four-helix bundle, to which each monomer contributes by two amphipathic α-helices, forming a hydrophobic core. The dimer is stabilized by extensive intermolecular contacts, consistent with the observed tight dimer in solution (PMID:21821042). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O54465 [UniProt boundaries chain A]=2-72 [UniProt coverage chain A]=98% [Name chain A]=Hypothetical mobile element-associated protein [UniProt sequence chain A]=METKYELNNTKKVANAFGLNEEDTNLLINAVDLDIKNNMQEISSELQQSEQSKQKQYGTTLQNLAKQNRIIK [Source organism chain A]=Staphylococcus aureus [UniProt ID chain B]=O54465 [UniProt boundaries chain B]=2-72 [UniProt coverage chain B]=98% [Name chain B]=Hypothetical mobile element-associated protein [UniProt sequence chain B]=METKYELNNTKKVANAFGLNEEDTNLLINAVDLDIKNNMQEISSELQQSEQSKQKQYGTTLQNLAKQNRIIK [Source organism chain B]=Staphylococcus aureus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Staphylococcus aureus [Accession]=MF7001009 [Entry] [Entry number]=1194 [Entry name]=Yeast Rna14p monkeytail domain and Rna15p hinge domain heterodimer [PDB ID]=2l9b [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The C-terminal monkeytail domain from Rna14p and the hinge region from Rna15p display a coupled binding and folding mechanism, where both peptides are initially disordered (as evidenced by CD spectroscopy). NMR spectroscopy confirms that the peptides that are either unfolded or in a heterogeneous molten-globule state (PMID:21481776). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=The region(s) described in DP02761 covers 100% of the sequence present in the structure [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P25299 [UniProt boundaries chain A]=138-228 [UniProt coverage chain A]=30% [Name chain A]=mRNA 3'-end-processing protein RNA15 [UniProt sequence chain A]=MNRQSGVNAGVQNNPPSRVVYLGSIPYDQTEEQILDLCSNVGPVINLKMMFDPQTGRSKGYAFIEFRDLESSASAVRNLNGYQLGSRFLKCGYSSNSDISGVSQQQQQQYNNINGNNNNNGNNNNNSNGPDFQNSGNANFLSQKFPELPSGIDVNINMTTPAMMISSELAKKPKEVQLKFLQKFQEWTRAHPEDAVSLLELCPQLSFVTAELLLTNGICKVDDLIPLASRPQEEASATNNNSVNEVVDPAVLNKQKELLKQVLQLNDSQISILPDDERMAIWDLKQKALRGEFGAF [Source organism chain A]=Saccharomyces cerevisiae [UniProt ID chain B]=P25298 [UniProt boundaries chain B]=630-669 [UniProt coverage chain B]=5% [Name chain B]=mRNA 3'-end-processing protein RNA14 [UniProt sequence chain B]=MSSSTTPDLLYPSADKVAEPSDNIHGDELRLRERIKDNPTNILSYFQLIQYLETQESYAKVREVYEQFHNTFPFYSPAWTLQLKGELARDEFETVEKILAQCLSGKLENNDLSLWSTYLDYIRRKNNLITGGQEARAVIVKAFQLVMQKCAIFEPKSSSFWNEYLNFLEQWKPFNKWEEQQRIDMLREFYKKMLCVPFDNLEKMWNRYTQWEQEINSLTARKFIGELSAEYMKARSLYQEWLNVTNGLKRASPINLRTANKKNIPQPGTSDSNIQQLQIWLNWIKWERENKLMLSEDMLSQRISYVYKQGIQYMIFSAEMWYDYSMYISENSDRQNILYTALLANPDSPSLTFKLSECYELDNDSESVSNCFDKCTQTLLSQYKKIASDVNSGEDNNTEYEQELLYKQREKLTFVFCVYMNTMKRISGLSAARTVFGKCRKLKRILTHDVYVENAYLEFQNQNDYKTAFKVLELGLKYFQNDGVYINKYLDFLIFLNKDSQIKTLFETSVEKVQDLTQLKEIYKKMISYESKFGNLNNVYSLEKRFFERFPQENLIEVFTSRYQIQNSNLIKKLELTYMYNEEEDSYFSSGNGDGHHGSYNMSSSDRKRLMEETGNNGNFSNKKFKRDSELPTEVLDLLSVIPKRQYFNTNLLDAQKLVNFLNDQVEIPTVESTKSG [Source organism chain B]=Saccharomyces cerevisiae [ExpTech]=NMR [Resolution]=N/A [Source organism]=Saccharomyces cerevisiae [Accession]=MF7001010 [Entry] [Entry number]=1195 [Entry name]=mSin3A PAH3-SAP30 SID complex [PDB ID]=2ld7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=The authors claim that the complex has a large hydrophobic interface, strong interaction, and the isolated proteins are not well-behaved, not completely soluble, which could be due to instability (PMID:21676866). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=O88574 [UniProt boundaries chain A]=130-220 [UniProt coverage chain A]=41% [Name chain A]=Histone deacetylase complex subunit SAP30 [UniProt sequence chain A]=MNGFTPEEMSRGGDAAAAVAAVVAAAAAAASAGNGNAAGGGAEVPGAGAVSASGPPGAAGPGPGQLCCLREDGERCGRAAGNASFSKRIQKSISQKKVKIELDKSARHLYICDYHKNLIQSVRNRRKRKGSDDDGGDSPVQDIDTPEVDLYQLQVNTLRRYKRHFKLPTRPGLNKAQLVEIVGCHFKSIPVNEKDTLTCFIYSVRNDKNKSDLKADSGVH [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q60520 [UniProt boundaries chain B]=456-528 [UniProt coverage chain B]=5% [Name chain B]=Paired amphipathic helix protein Sin3a [UniProt sequence chain B]=MKRRLDDQESPVYAAQQRRIPGSTEAFSHQHRVLAPAPPVYEAVSETMQSATGIQYSVAPNYQVSAVPQSSGSHGPAIAAVHSSHHHPTAVQPHGGQVVQSHAHPAPPVAPVQGQQQFQRLKVEDALSYLDQVKLQFGSQPQVYNDFLDIMKEFKSQSIDTPGVISRVSQLFKGHPDLIMGFNTFLPPGYKIEVQTNDMVNVTTPGQVHQIPTHGIQPQPQPPPQHPSQPSSQSAPTPAQPAPQPTAAKVSKPSQLQAHTPASQQTPPLPPYASPRSPPVQPHTPVTISLGTAPSLQNNQPVEFNHAINYVNKIKNRFQGQPDIYKAFLEILHTYQKEQRNAKEAGGNYTPALTEQEVYAQVARLFKNQEDLLSEFGQFLPDANSSVLLSKTTAEKVDSVRNDHGGTVKKPQLNNKPQRPSQNGCQIRRHSGTGATPPVKKKPKLMSLKESSMADASKHGVGTESLFFDKVRKALRSAEAYENFLRCLVIFNQEVISRAELVQLVSPFLGKFPELFNWFKNFLGYKESVHLESFPKERATEGIAMEIDYASCKRLGSSYRALPKSYQQPKCTGRTPLCKEVLNDTWVSFPSWSEDSTFVSSKKTQYEEHIYRCEDERFELDVVLETNLATIRVLEAIQKKLSRLSAEEQAKFRLDNTLGGTSEVIHRKALQRIYADKAADIIDGLRKNPSIAVPIVLKRLKMKEEEWREAQRGFNKVWREQNEKYYLKSLDHQGINFKQNDTKVLRSKSLLNEIESIYDERQEQATEENAGVPVGPHLSLAYEDKQILEDAAALIIHHVKRQTGIQKEDKYKIKQIMHHFIPDLLFAQRGDLSDVEEEEEEEMDVDEATGAPKKHNGVGGSPPKSKLLFSNTAAQKLRGMDEVYNLFYVNNNWYIFMRLHQILCLRLLRICSQAERQIEEENREREWEREVLGIKRDKSDSPAIQLRLKEPMDVDVEDYYPAFLDMVRSLLDGNIDSSQYEDSLREMFTIHAYIAFTMDKLIQSIVRQLQHIVSDEVCVQVTDLYLAENNNGATGGQLNSQTSRSLLESAYQRKAEQLMSDENCFKLMFIQSQGQVQLTVELLDTEEENSDDPVEAERWSDYVERYMSSDTTSPELREHLAQKPVFLPRNLRRIRKCQRGREQQEKEGKEGNSKKTMENVESLDKLECRFKLNSYKMVYVIKSEDYMYRRTALLRAHQSHERVSKRLHQRFQAWVDKWTKEHVPREMAAETSKWLMGEGLEGLVPCTTTCDTETLHFVSINKYRVKYGTVFKAP [Source organism chain B]=Mus musculus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Mus musculus [Accession]=MF7001011 [Entry] [Entry number]=1196 [Entry name]=Dimerization domain of ZEN-4 [PDB ID]=7eqb [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Coils and zippers [Subclass]=Coiled coil (dimeric) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The subunits in the structure are bound via coiled coil interactions (PMID:34588311). Coiled coils are highly versatile folding units (PMID:11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID:9811815) and trimers (PMID:10933510) up to heptamers (PMID:17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID:8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID:17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure. Leucine zippers, phenylalanine zippers and alanine zippers are subclasses of coiled coils where the hydrophobic interactions between subunits are predominantly formed by leucine, phenylalanine or alanine residues, respectively. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q8MQ03 [UniProt boundaries chain A]=534-601 [UniProt coverage chain A]=8% [Name chain A]=Kinesin-like protein [UniProt sequence chain A]=MSSRKRGITPSRDQVRRKKLSIEETDSIEVVCRLCPYTGSTPSLIAIDEGSIQTVLPPAQFRRENAPQVEKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGKPTETGTGLLPRTLDVIFNSINNRVEKCIFYPSALNTFEIRATLDAHLKRHQMAADRLSTSREITDRYCEAIKLSGYNDDMVCSVFVTYVEIYNNYCYDLLEDARNGSRVLTKREIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRAYETKSVYPTMDSSQIIVSQLCLVDLAGSERAKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSQNLEQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTIEVKKQVERMPSERIPHSFFTQWNSELDGSVRMEDDGSREIPCPPTFCLTDCNDKDTVDSMYKYARKLSSLQNSSEEGPSSTLLTMIRQYMMEADYQRVEIARLKDSLNDKDEEIKKLRGFCSRYKRENASMKERIASCEQGEQENALVMEKLMEQKMEDRKIIQSQKKAMRNVRGIIDNPSPSVASLRSRFDQENVAHPTAPIQTPPPPYQTPGRAPVFKKRLEATTSTTVMSGSSSGGSGQQGYVNPKYQRRSKSASRLLDHQPLHRVPTGTVLQSRTPANAIRTTKPEMHQLNKSGEYRLTHQEVDDEGNISTNIVKAPSKPPELQLEDSQSSSYSPCTDVKSITIYSNHDVEEEDE [Source organism chain A]=Caenorhabditis elegans [UniProt ID chain B]=Q8MQ03 [UniProt boundaries chain B]=536-603 [UniProt coverage chain B]=8% [Name chain B]=Kinesin-like protein [UniProt sequence chain B]=MSSRKRGITPSRDQVRRKKLSIEETDSIEVVCRLCPYTGSTPSLIAIDEGSIQTVLPPAQFRRENAPQVEKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGKPTETGTGLLPRTLDVIFNSINNRVEKCIFYPSALNTFEIRATLDAHLKRHQMAADRLSTSREITDRYCEAIKLSGYNDDMVCSVFVTYVEIYNNYCYDLLEDARNGSRVLTKREIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRAYETKSVYPTMDSSQIIVSQLCLVDLAGSERAKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSQNLEQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTIEVKKQVERMPSERIPHSFFTQWNSELDGSVRMEDDGSREIPCPPTFCLTDCNDKDTVDSMYKYARKLSSLQNSSEEGPSSTLLTMIRQYMMEADYQRVEIARLKDSLNDKDEEIKKLRGFCSRYKRENASMKERIASCEQGEQENALVMEKLMEQKMEDRKIIQSQKKAMRNVRGIIDNPSPSVASLRSRFDQENVAHPTAPIQTPPPPYQTPGRAPVFKKRLEATTSTTVMSGSSSGGSGQQGYVNPKYQRRSKSASRLLDHQPLHRVPTGTVLQSRTPANAIRTTKPEMHQLNKSGEYRLTHQEVDDEGNISTNIVKAPSKPPELQLEDSQSSSYSPCTDVKSITIYSNHDVEEEDE [Source organism chain B]=Caenorhabditis elegans [ExpTech]=X-ray [Resolution]=2.10 [Source organism]=Caenorhabditis elegans [Accession]=MF7001012 [Entry] [Entry number]=1197 [Entry name]=AF2331 protein (Archaeoglobus fulgidus DSM 4304) [PDB ID]=2fdo [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=Unusually tight and interdigitated a+b homodimer. Extremely large dimerization interface for a protein of its size. The percentage of the total surface area buried in the interface (41.1%) is extreme (PMID:19768810). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain B]=N/A [Evidence chain A]=N/A [Similar structures]=None [UniProt ID chain B]=O27953 [UniProt boundaries chain B]=1-92 [UniProt coverage chain B]=100% [Name chain B]=Uncharacterized protein AF_2331 [UniProt sequence chain B]=MPAYVFSKESFLKFLEGHLEDDVVVVVSSDVTDFCKKLSESMVGEKEYCFAEFAFPADIFDADEDEIDEMMKYAIVFVEKEKLSEAGRNAIR [Source organism chain B]=100126 / VC-16) [UniProt ID chain A]=O27953 [UniProt boundaries chain A]=1-92 [UniProt coverage chain A]=100% [Name chain A]=Uncharacterized protein AF_2331 [UniProt sequence chain A]=MPAYVFSKESFLKFLEGHLEDDVVVVVSSDVTDFCKKLSESMVGEKEYCFAEFAFPADIFDADEDEIDEMMKYAIVFVEKEKLSEAGRNAIR [Source organism chain A]=100126 / VC-16) [ExpTech]=X-ray [Resolution]=2.40 [Source organism]=100126 / VC-16) [Accession]=MF7001013 [Entry] [Entry number]=1198 [Entry name]=Type III secretion system pilotin-secretin complex: InvH-InvG [PDB ID]=6xfl [Chains]=A,B [Total number of chains]=2 [Assembly]=Heterodimer [Number of unique proteins]=2 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Both proteins were fully or partially disodered by NMR when separated, but formed a well-folded complex together. [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P0CL43 [UniProt boundaries chain A]=70-147 [UniProt coverage chain A]=53% [Name chain A]=SPI-1 type 3 secretion system pilotin [UniProt sequence chain A]=MKKFYSCLPVFLLIGCAQVPLPSSVSKPVQQPGAQKEQLANANSIDECQSLPYVPSDLAKNKSLSNHNADNSASKNSAISSSIFCEKYKQTKEQALTFFQEHPQYMRSKEDEEQLMTEFKKVLLEPGSKNLSIYQTLLAAHERLQAL [Source organism chain A]=Salmonella typhimurium [UniProt ID chain B]=P35672 [UniProt boundaries chain B]=520-562 [UniProt coverage chain B]=7% [Name chain B]=SPI-1 type 3 secretion system secretin [UniProt sequence chain B]=MKTHILLARVLACAALVLVTPGYSSEKIPVTGSGFVAKDDSLRTFFDAMALQLKEPVIVSKMAARKKITGNFEFHDPNALLEKLSLQLGLIWYFDGQAIYIYDASEMRNAVVSLRNVSLNEFNNFLKRSGLYNKNYPLRGDNRKGTFYVSGPPVYVDMVVNAATMMDKQNDGIELGRQKIGVMRLNNTFVGDRTYNLRDQKMVIPGIATAIERLLQGEEQPLGNIVSSEPPAMPAFSANGEKGKAANYAGGMSLQEALKQNAAAGNIKIVAYPDTNSLLVKGTAEQVHFIEMLVKALDVAKRHVELSLWIVDLNKSDLERLGTSWSGSITIGDKLGVSLNQSSISTLDGSRFIAAVNALEEKKQATVVSRPVLLTQENVPAIFDNNRTFYTKLIGERNVALEHVTYGTMIRVLPRFSADGQIEMSLDIEDGNDKTPQSDTTTSVDALPEVGRTLISTIARVPHGKSLLVGGYTRDANTDTVQSIPFLGKLPLIGSLFRYSSKNKSNVVRVFMIEPKEIVDPLTPDASESVNNILKQSGAWSGDDKLQKWVRVYLDRGQEAIK [Source organism chain B]=Salmonella typhimurium [ExpTech]=NMR [Resolution]=N/A [Source organism]=Salmonella typhimurium [Accession]=MF7001014 [Entry] [Entry number]=1199 [Entry name]=V66L CzrA with Zn [PDB ID]=6cdb [Chains]=A-3,A [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=ArsR-type HTH winged helix DBD transcriptional regulator (PMID:29953213) that, similar to other similar proteins, has a dimerization subdomain that represents the hydrophobic core of the protein and is made up of two long a-helices from each monomer forming a 4-helix bundle-like structure. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-3]=N/A [Similar structures]=None [UniProt ID chain A]=O85142 [UniProt boundaries chain A]=6-102 [UniProt coverage chain A]=91% [Name chain A]=Transcriptional regulator [UniProt sequence chain A]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A]=Staphylococcus aureus [UniProt ID chain A-3]=O85142 [UniProt boundaries chain A-3]=8-102 [UniProt coverage chain A-3]=89% [Name chain A-3]=Transcriptional regulator [UniProt sequence chain A-3]=MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL [Source organism chain A-3]=Staphylococcus aureus [ExpTech]=X-ray [Resolution]=1.99 [Source organism]=Staphylococcus aureus [Accession]=MF7001015 [Entry] [Entry number]=1200 [Entry name]=Transcriptional regulator homologue protein (Pyrococcus horikoshii OT3) [PDB ID]=1ub9 [Chains]=A,A-2 [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=ArsR-type HTH winged helix DBD transcriptional regulator (PMID:16506234) that, similar to other similar proteins, has a dimerization subdomain that represents the hydrophobic core of the protein and is made up of two long a-helices from each monomer forming a 4-helix bundle-like structure. [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-2]=N/A [Similar structures]=None [UniProt ID chain A]=O58788 [UniProt boundaries chain A]=1-100 [UniProt coverage chain A]=100% [Name chain A]=HTH arsR-type domain-containing protein [UniProt sequence chain A]=MEELKEIMKSHILGNPVRLGIMIFLLPRRKAPFSQIQKVLDLTPGNLDSHIRVLERNGLVKTYKVIADRPRTVVEITDFGMEEAKRFLSSLKAVIDGLDL [Source organism chain A]=100139 / OT-3) [UniProt ID chain A-2]=O58788 [UniProt boundaries chain A-2]=1-100 [UniProt coverage chain A-2]=100% [Name chain A-2]=HTH arsR-type domain-containing protein [UniProt sequence chain A-2]=MEELKEIMKSHILGNPVRLGIMIFLLPRRKAPFSQIQKVLDLTPGNLDSHIRVLERNGLVKTYKVIADRPRTVVEITDFGMEEAKRFLSSLKAVIDGLDL [Source organism chain A-2]=100139 / OT-3) [ExpTech]=X-ray [Resolution]=2.05 [Source organism]=100139 / OT-3) [Accession]=MF7001016 [Entry] [Entry number]=1201 [Entry name]=Thermostable protein (Hyperthermophilic Virus SSV-RH) [PDB ID]=4aai [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Similarity to ribbon-helix-helix (RHH) domains is present in numerous proteins involved in transcriptional regulation. The RHH motif is elaborated upon by the insertion of a third helix that is tightly integrated into the structural domain. Thermal stability data were analyzed assuming a two-state transition of a folded dimer to two unfolded monomers without intermediates. SEC, AUC, DLS and NMR spectroscopy all indicated that E73 is a homodimer in solution (PMID:22409376). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q6TRU9 [UniProt boundaries chain A]=1-73 [UniProt coverage chain A]=100% [Name chain A]=ORF E73 [UniProt sequence chain A]=MVESKKIAKKKTTLAFDEDVYHTLKLVSVYLNRDMTEIIEEAVVMWLIQNKEKLPNELKPKIDEISKRFFPAK [Source organism chain A]=Sulfolobus virus Ragged Hills [UniProt ID chain B]=Q6TRU9 [UniProt boundaries chain B]=1-73 [UniProt coverage chain B]=100% [Name chain B]=ORF E73 [UniProt sequence chain B]=MVESKKIAKKKTTLAFDEDVYHTLKLVSVYLNRDMTEIIEEAVVMWLIQNKEKLPNELKPKIDEISKRFFPAK [Source organism chain B]=Sulfolobus virus Ragged Hills [ExpTech]=NMR [Resolution]=N/A [Source organism]=Sulfolobus virus Ragged Hills [Accession]=MF7001017 [Entry] [Entry number]=1202 [Entry name]=Mouse Sak Polo domain [PDB ID]=1mby [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Based on limited proteolysis and mass spectrometry, the dimeric polo box motif comprises an autonomously folding unit, the polo domain. It behaves as a dimer in solution, as indicated by SEC and static light scattering (SLS).The dimer has a relatively large interface. Overall, the dimeric structure is clam-like, β-strands 6, 1, 2 and 3 from one monomer form a contiguous antiparallel β-sheet with β-strands 4 and 5 from the other monomer (PMID:12352953). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q64702 [UniProt boundaries chain A]=845-919 [UniProt coverage chain A]=8% [Name chain A]=Serine/threonine-protein kinase PLK4 [UniProt sequence chain A]=MAACIGERIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSVLELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRMKPFSEREARHFMHQIITGMLYLHSHGILHRDLTLSNILLTRNMNIKIADFGLATQLNMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRRNPADRLSLSSVLDHPFMSRNPSPKSKDVGTVEDSMDSGHATLSTTITASSGTSLSGSLLDRRLLVGQPLPNKITVFQKNKNSSDFSSGDGSNFCTQWGNPEQEANSRGRGRVIEDAEERPHSRYLRRAHSSDRASPSNQSRAKTYSVERCHSVEMLSKPRRSLDENQHSSNHHCLGKTPFPFADQTPQMEMVQQWFGNLQMNAHLGETNEHHTVSPNRDFQDYPDLQDTLRNAWTDTRASKNADTSANVHAVKQLSAMKYMSAHHHKPEVMPQEPGLHPHSEQSKNRSMESTLGYQKPTLRSITSPLIAHRLKPIRQKTKKAVVSILDSEEVCVELLRECASEGYVKEVLQISSDGTMITVYYPNDGRGFPLADRPPLPTDNISRYSFDNLPEKYWRKYQYASRFIQLVRSKTPKITYFTRYAKCILMENSPGADFEVWFYDGAKIHKTENLIHIIEKTGISYNLKNENEVTSLKEEVKVYMDHANEGHRICLSLESVISEEEKRSRGSSFFPIIVGRKPGNTSSPKALSAPPVDPSCCKGEQASASRLSVNSAAFPTQSPGLSPSTVTVEGLGHTATATGTGVSSSLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPDGQTTRYGENEKLPEYIKQKLQCLSSILLMFSNPTPNFQ [Source organism chain A]=Mus musculus [UniProt ID chain B]=Q64702 [UniProt boundaries chain B]=845-919 [UniProt coverage chain B]=8% [Name chain B]=Serine/threonine-protein kinase PLK4 [UniProt sequence chain B]=MAACIGERIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSVLELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRMKPFSEREARHFMHQIITGMLYLHSHGILHRDLTLSNILLTRNMNIKIADFGLATQLNMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRRNPADRLSLSSVLDHPFMSRNPSPKSKDVGTVEDSMDSGHATLSTTITASSGTSLSGSLLDRRLLVGQPLPNKITVFQKNKNSSDFSSGDGSNFCTQWGNPEQEANSRGRGRVIEDAEERPHSRYLRRAHSSDRASPSNQSRAKTYSVERCHSVEMLSKPRRSLDENQHSSNHHCLGKTPFPFADQTPQMEMVQQWFGNLQMNAHLGETNEHHTVSPNRDFQDYPDLQDTLRNAWTDTRASKNADTSANVHAVKQLSAMKYMSAHHHKPEVMPQEPGLHPHSEQSKNRSMESTLGYQKPTLRSITSPLIAHRLKPIRQKTKKAVVSILDSEEVCVELLRECASEGYVKEVLQISSDGTMITVYYPNDGRGFPLADRPPLPTDNISRYSFDNLPEKYWRKYQYASRFIQLVRSKTPKITYFTRYAKCILMENSPGADFEVWFYDGAKIHKTENLIHIIEKTGISYNLKNENEVTSLKEEVKVYMDHANEGHRICLSLESVISEEEKRSRGSSFFPIIVGRKPGNTSSPKALSAPPVDPSCCKGEQASASRLSVNSAAFPTQSPGLSPSTVTVEGLGHTATATGTGVSSSLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPDGQTTRYGENEKLPEYIKQKLQCLSSILLMFSNPTPNFQ [Source organism chain B]=Mus musculus [ExpTech]=X-ray [Resolution]=2.00 [Source organism]=Mus musculus [Accession]=MF7001018 [Entry] [Entry number]=1203 [Entry name]=ParB (plasmid pCXC100) [PDB ID]=3no7 [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Ribbon-helix-helix (RHH) [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=The interacting chains form a ribbon-helix-helix (RHH) structure (PMID:21123191). These structures in general have been described with the two monomers adopting a stable conformation upon the interaction (PMID:17676053). The hydrophobic core stabilizing the complex is formed by both interactors and is thus absent prior to the interaction (PMID:25713077). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=Q6EEF9 [UniProt boundaries chain A]=69-128 [UniProt coverage chain A]=43% [Name chain A]=Putative plasmid related protein [UniProt sequence chain A]=MADRTVAPPPSRPGAGSLIRSQREASAAPSMVAPAFVPESPSVADSVAPTVPVPVPGGSSEPRGARSEVKMTVTVGEERRARLRTAYTLTHLQEGHRTFSGFIAAALDAEVQRLEQRYNEGRRFENAERGVTRGRPLGS [Source organism chain A]=Leifsonia xyli subsp cynodontis [UniProt ID chain B]=Q6EEF9 [UniProt boundaries chain B]=70-128 [UniProt coverage chain B]=42% [Name chain B]=Putative plasmid related protein [UniProt sequence chain B]=MADRTVAPPPSRPGAGSLIRSQREASAAPSMVAPAFVPESPSVADSVAPTVPVPVPGGSSEPRGARSEVKMTVTVGEERRARLRTAYTLTHLQEGHRTFSGFIAAALDAEVQRLEQRYNEGRRFENAERGVTRGRPLGS [Source organism chain B]=Leifsonia xyli subsp cynodontis [ExpTech]=X-ray [Resolution]=1.40 [Source organism]=Leifsonia xyli subsp cynodontis [Accession]=MF7001019 [Entry] [Entry number]=1204 [Entry name]=PadR (Bacillus subtilis (space group H32)) [PDB ID]=7cbv [Chains]=A-3,A [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Multidomain structures [Subclass]=Winged helix DNA-binding domain and helical dimerization domain [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=PadR-type transcriptional regulators form homodimers wherein the two Winged helix DNA-binding domains are linked together by a helical dimerization domain that forms dimeric coiled-coil structures. The homologous AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748). [Evidence coverage]=Only some parts of the structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain A-3]=N/A [Similar structures]=None [UniProt ID chain A]=P94443 [UniProt boundaries chain A]=2-180 [UniProt coverage chain A]=98% [Name chain A]=Negative transcription regulator PadR [UniProt sequence chain A]=MRVLKYAILGLLRKGELSGYDITSYFKEELGQFWSAKHSQIYPELKKLTDEGFITFRTTIQGTKLEKKMYTLTDSGKQELHDWLIRHQPIPETVKDEFMLKAYFISCLSRQEASDLFKDQLQKRQAKLSDLQGSYEKLMASAEPMSFSSPDFGHYLVLTKALEREKNYVSWLESILAMIDKD [Source organism chain A]=Bacillus subtilis [UniProt ID chain A-3]=P94443 [UniProt boundaries chain A-3]=2-180 [UniProt coverage chain A-3]=98% [Name chain A-3]=Negative transcription regulator PadR [UniProt sequence chain A-3]=MRVLKYAILGLLRKGELSGYDITSYFKEELGQFWSAKHSQIYPELKKLTDEGFITFRTTIQGTKLEKKMYTLTDSGKQELHDWLIRHQPIPETVKDEFMLKAYFISCLSRQEASDLFKDQLQKRQAKLSDLQGSYEKLMASAEPMSFSSPDFGHYLVLTKALEREKNYVSWLESILAMIDKD [Source organism chain A-3]=Bacillus subtilis [ExpTech]=X-ray [Resolution]=2.30 [Source organism]=Bacillus subtilis [Accession]=MF7001020 [Entry] [Entry number]=1205 [Entry name]=C-terminal of AbrB [PDB ID]=2mjg [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=The AbrBC homodimer is connected by a domain-swapped anti-parallel beta-sheet with significant interactions between them forming the core of the structure. A planar helical structure is set underneath the two sets of β-sheets. HPLC shows that AbrBC (residues 52–94) exists as a dimer in solution (PMID: 25308864). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P08874 [UniProt boundaries chain A]=54-96 [UniProt coverage chain A]=44% [Name chain A]=Transition state regulatory protein AbrB [UniProt sequence chain A]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain A]=Bacillus subtilis [UniProt ID chain B]=P08874 [UniProt boundaries chain B]=54-96 [UniProt coverage chain B]=44% [Name chain B]=Transition state regulatory protein AbrB [UniProt sequence chain B]=MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK [Source organism chain B]=Bacillus subtilis [ExpTech]=NMR [Resolution]=N/A [Source organism]=Bacillus subtilis [Accession]=MF7001021 [Entry] [Entry number]=1206 [Entry name]=N-terminal dimerization domain of EBNA-2 (Epstein-barr virus) [PDB ID]=2n2j [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Other [Sequence domain]=- [Evidence level]=Indirect evidence [Evidence text]=The EBNA-2 N-terminal dimerization (END) domain monomer comprises a small fold of four β-strands and an α-helix which form a parallel dimer by interaction of two β-strands from each protomer. A structure-guided mutational analysis showed that hydrophobic residues in the dimer interface are required for self-association in vitro. Importantly, these interface mutants also displayed severely impaired self-association and transactivation in vivo. The L16A mutant exists in equilibrium between an unfolded monomeric and folded dimeric state (PMID:26024477). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P12978 [UniProt boundaries chain A]=1-58 [UniProt coverage chain A]=11% [Name chain A]=Epstein-Barr nuclear antigen 2 [UniProt sequence chain A]=MPTFYLALHGGQTYHLIVDTDSLGNPSLSVIPSNPYQEQLSDTPLIPLTIFVGENTGVPPPLPPPPPPPPPPPPPPPPPPPPPPPPPPSPPPPPPPPPPPQRRDAWTQEPSPLDRDPLGYDVGHGPLASAMRMLWMANYIVRQSRGDRGLILPQGPQTAPQARLVQPHVPPLRPTAPTILSPLSQPRLTPPQPLMMPPRPTPPTPLPPATLTVPPRPTRPTTLPPTPLLTVLQRPTELQPTPSPPRMHLPVLHVPDQSMHPLTHQSTPNDPDSPEPRSPTVFYNIPPMPLPPSQLPPPAAPAQPPPGVINDQQLHHLPSGPPWWPPICDPPQPSKTQGQSRGQSRGRGRGRGRGRGKGKSRDKQRKPGGPWRPEPNTSSPSMPELSPVLGLHQGQGAGDSPTPGPSNAAPVCRNSHTATPNVSPIHEPESHNSPEAPILFPDDWYPPSIDPADLDESWDYIFETTESPSSDEDYVEGPSKRPRPSIQ [Source organism chain A]=Epstein-Barr virus [UniProt ID chain B]=P12978 [UniProt boundaries chain B]=1-58 [UniProt coverage chain B]=11% [Name chain B]=Epstein-Barr nuclear antigen 2 [UniProt sequence chain B]=MPTFYLALHGGQTYHLIVDTDSLGNPSLSVIPSNPYQEQLSDTPLIPLTIFVGENTGVPPPLPPPPPPPPPPPPPPPPPPPPPPPPPPSPPPPPPPPPPPQRRDAWTQEPSPLDRDPLGYDVGHGPLASAMRMLWMANYIVRQSRGDRGLILPQGPQTAPQARLVQPHVPPLRPTAPTILSPLSQPRLTPPQPLMMPPRPTPPTPLPPATLTVPPRPTRPTTLPPTPLLTVLQRPTELQPTPSPPRMHLPVLHVPDQSMHPLTHQSTPNDPDSPEPRSPTVFYNIPPMPLPPSQLPPPAAPAQPPPGVINDQQLHHLPSGPPWWPPICDPPQPSKTQGQSRGQSRGRGRGRGRGRGKGKSRDKQRKPGGPWRPEPNTSSPSMPELSPVLGLHQGQGAGDSPTPGPSNAAPVCRNSHTATPNVSPIHEPESHNSPEAPILFPDDWYPPSIDPADLDESWDYIFETTESPSSDEDYVEGPSKRPRPSIQ [Source organism chain B]=Epstein-Barr virus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Epstein-Barr virus [Accession]=MF7001022 [Entry] [Entry number]=1207 [Entry name]=Synthetic two-site CA-binding homodimer [PDB ID]=1cta [Chains]=A,B [Total number of chains]=2 [Assembly]=Homodimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=EF hand dimers [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Two-dimensional 'H NMR data showed no evidence of the existence of a Ca2+-free folded monomer. This implies a transient existence of a Ca2+- bound monomer and that the dimerization process involves a concerted folding mechanism (PMID1304377). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Similar structures]=None [UniProt ID chain A]=P02588 [UniProt boundaries chain A]=94-127 [UniProt coverage chain A]=20% [Name chain A]=Troponin C, skeletal muscle [UniProt sequence chain A]=MASMTDQQAEARAFLSEEMIAEFKAAFDMFDADGGGDISTKELGTVMRMLGQNPTKEELDAIIEEVDEDGSGTIDFEEFLVMMVRQMKEDAKGKSEEELANCFRIFDKNADGFIDIEELGEILRATGEHVTEEDIEDLMKDSDKNNDGRIDFDEFLKMMEGVQ [Source organism chain A]=Gallus gallus [UniProt ID chain B]=P02588 [UniProt boundaries chain B]=94-127 [UniProt coverage chain B]=20% [Name chain B]=Troponin C, skeletal muscle [UniProt sequence chain B]=MASMTDQQAEARAFLSEEMIAEFKAAFDMFDADGGGDISTKELGTVMRMLGQNPTKEELDAIIEEVDEDGSGTIDFEEFLVMMVRQMKEDAKGKSEEELANCFRIFDKNADGFIDIEELGEILRATGEHVTEEDIEDLMKDSDKNNDGRIDFDEFLKMMEGVQ [Source organism chain B]=Gallus gallus [ExpTech]=NMR [Resolution]=N/A [Source organism]=Gallus gallus [Accession]=MF7001023 [Entry] [Entry number]=1208 [Entry name]=Eye lens beta/gamma-crystallin [PDB ID]=1hdf [Chains]=A,A-2,B,B-2 [Total number of chains]=4 [Assembly]=Tetramer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Crystallin [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Spherulin 3a is a tight homodimer, which is consistent with ultracentrifugation studies (PMID:11250196). The equilibrium unfolding transitions obey the two-state model according to N2-->2 U (PMID:10518950). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain A-2]=N/A [Evidence chain B-2]=N/A [Similar structures]=None [UniProt ID chain A]=P09353 [UniProt boundaries chain A]=2-101 [UniProt coverage chain A]=97% [Name chain A]=Spherulin-3A [UniProt sequence chain A]=MSVCKGVSGNPAKGEVFLYKHVNFQGDSWKVTGNVYDFRSVSGLNDVVSSVKVGPNTKAFIFKDDRFNGNFIRLEESSQVTDLTTRNLNDAISSIIVATFESA [Source organism chain A]=Physarum polycephalum [UniProt ID chain B]=P09353 [UniProt boundaries chain B]=2-101 [UniProt coverage chain B]=97% [Name chain B]=Spherulin-3A [UniProt sequence chain B]=MSVCKGVSGNPAKGEVFLYKHVNFQGDSWKVTGNVYDFRSVSGLNDVVSSVKVGPNTKAFIFKDDRFNGNFIRLEESSQVTDLTTRNLNDAISSIIVATFESA [Source organism chain B]=Physarum polycephalum [UniProt ID chain A-2]=P09353 [UniProt boundaries chain A-2]=2-101 [UniProt coverage chain A-2]=97% [Name chain A-2]=Spherulin-3A [UniProt sequence chain A-2]=MSVCKGVSGNPAKGEVFLYKHVNFQGDSWKVTGNVYDFRSVSGLNDVVSSVKVGPNTKAFIFKDDRFNGNFIRLEESSQVTDLTTRNLNDAISSIIVATFESA [Source organism chain A-2]=Physarum polycephalum [UniProt ID chain B-2]=P09353 [UniProt boundaries chain B-2]=2-101 [UniProt coverage chain B-2]=97% [Name chain B-2]=Spherulin-3A [UniProt sequence chain B-2]=MSVCKGVSGNPAKGEVFLYKHVNFQGDSWKVTGNVYDFRSVSGLNDVVSSVKVGPNTKAFIFKDDRFNGNFIRLEESSQVTDLTTRNLNDAISSIIVATFESA [Source organism chain B-2]=Physarum polycephalum [ExpTech]=X-ray [Resolution]=2.35 [Source organism]=Physarum polycephalum [Accession]=MF7001024 [Entry] [Entry number]=1209 [Entry name]=Cpn10 (Thermus thermophilus HB8) [PDB ID]=1wnr [Chains]=A,D,B,G,E,F,C [Total number of chains]=7 [Assembly]=Heptamer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=GroES [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=For the GroES heptamer, DSC and CD measuremetns were in agreement, suggesting that the two-state folding/unfolding oligomerization model accounts well for the overall thermodynamic parameters and cooperativity of GroES folding/unfolding, and for its concentration dependence. Attempts to include intermediate forms in the fitting equations did not improve the goodness of the fit, indicating that folded monomers are not measurably populated during (PMID:9368656). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Evidence chain D]=N/A [Evidence chain E]=N/A [Evidence chain F]=N/A [Evidence chain G]=N/A [Similar structures]=None [UniProt ID chain A]=P61493 [UniProt boundaries chain A]=8-101 [UniProt coverage chain A]=93% [Name chain A]=Co-chaperonin GroES [UniProt sequence chain A]=MAAEVKTVIKPLGDRVVVKRIEEEPKTKGGIVLPDTAKEKPQKGKVIAVGTGRVLENGQRVPLEVKEGDIVVFAKYGGTEIEIDGEEYVILSERDLLAVLQ [Source organism chain A]=Thermus thermophilus [UniProt ID chain B]=P61493 [UniProt boundaries chain B]=8-101 [UniProt coverage chain B]=93% [Name chain B]=Co-chaperonin GroES [UniProt sequence chain B]=MAAEVKTVIKPLGDRVVVKRIEEEPKTKGGIVLPDTAKEKPQKGKVIAVGTGRVLENGQRVPLEVKEGDIVVFAKYGGTEIEIDGEEYVILSERDLLAVLQ [Source organism chain B]=Thermus thermophilus [UniProt ID chain C]=P61493 [UniProt boundaries chain C]=8-101 [UniProt coverage chain C]=93% [Name chain C]=Co-chaperonin GroES [UniProt sequence chain C]=MAAEVKTVIKPLGDRVVVKRIEEEPKTKGGIVLPDTAKEKPQKGKVIAVGTGRVLENGQRVPLEVKEGDIVVFAKYGGTEIEIDGEEYVILSERDLLAVLQ [Source organism chain C]=Thermus thermophilus [UniProt ID chain D]=P61493 [UniProt boundaries chain D]=8-101 [UniProt coverage chain D]=93% [Name chain D]=Co-chaperonin GroES [UniProt sequence chain D]=MAAEVKTVIKPLGDRVVVKRIEEEPKTKGGIVLPDTAKEKPQKGKVIAVGTGRVLENGQRVPLEVKEGDIVVFAKYGGTEIEIDGEEYVILSERDLLAVLQ [Source organism chain D]=Thermus thermophilus [UniProt ID chain E]=P61493 [UniProt boundaries chain E]=8-101 [UniProt coverage chain E]=93% [Name chain E]=Co-chaperonin GroES [UniProt sequence chain E]=MAAEVKTVIKPLGDRVVVKRIEEEPKTKGGIVLPDTAKEKPQKGKVIAVGTGRVLENGQRVPLEVKEGDIVVFAKYGGTEIEIDGEEYVILSERDLLAVLQ [Source organism chain E]=Thermus thermophilus [UniProt ID chain F]=P61493 [UniProt boundaries chain F]=8-101 [UniProt coverage chain F]=93% [Name chain F]=Co-chaperonin GroES [UniProt sequence chain F]=MAAEVKTVIKPLGDRVVVKRIEEEPKTKGGIVLPDTAKEKPQKGKVIAVGTGRVLENGQRVPLEVKEGDIVVFAKYGGTEIEIDGEEYVILSERDLLAVLQ [Source organism chain F]=Thermus thermophilus [UniProt ID chain G]=P61493 [UniProt boundaries chain G]=8-101 [UniProt coverage chain G]=93% [Name chain G]=Co-chaperonin GroES [UniProt sequence chain G]=MAAEVKTVIKPLGDRVVVKRIEEEPKTKGGIVLPDTAKEKPQKGKVIAVGTGRVLENGQRVPLEVKEGDIVVFAKYGGTEIEIDGEEYVILSERDLLAVLQ [Source organism chain G]=Thermus thermophilus [ExpTech]=X-ray [Resolution]=2.90 [Source organism]=Thermus thermophilus [Accession]=MF7001025 [Entry] [Entry number]=1210 [Entry name]=T4 phagehead fibritin trimer [PDB ID]=1rfo [Chains]=C,A,B [Total number of chains]=3 [Assembly]=Trimer [Number of unique proteins]=1 [PDB note]=All chains according to the most probable oligomerization state stored in PDBe were considered. [Class]=Other [Subclass]=Coiled coil/foldon domain [Sequence domain]=- [Evidence level]=Direct evidence [Evidence text]=Two-state folding from folded trimer to unfolded monomers was observed for the homotrimer (PMID:15033360). [Evidence coverage]=The full structure participates in mutual synergistic folding. [Evidence chain A]=N/A [Evidence chain B]=N/A [Evidence chain C]=N/A [Similar structures]=None [UniProt ID chain A]=P10104 [UniProt boundaries chain A]=458-484 [UniProt coverage chain A]=5% [Name chain A]=Fibritin [UniProt sequence chain A]=MTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA [Source organism chain A]=Enterobacteria phage T4 [UniProt ID chain B]=P10104 [UniProt boundaries chain B]=458-484 [UniProt coverage chain B]=5% [Name chain B]=Fibritin [UniProt sequence chain B]=MTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA [Source organism chain B]=Enterobacteria phage T4 [UniProt ID chain C]=P10104 [UniProt boundaries chain C]=458-484 [UniProt coverage chain C]=5% [Name chain C]=Fibritin [UniProt sequence chain C]=MTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA [Source organism chain C]=Enterobacteria phage T4 [ExpTech]=NMR [Resolution]=N/A [Source organism]=Enterobacteria phage T4 [Accession]=MF7001026