Database accession: MF7000821
Name: TM107
PDB ID: 1ilv
Experimental method: X-ray (2.00 Å)
Assembly: Homodimer
Source organism: Thermotoga maritima
Primary publication of the structure:
Zhang RG, Skarina T, Katz JE, Beasley S, Khachatryan A, Vyas S, Arrowsmith CH, Clarke S, Edwards A, Joachimiak A, Savchenko A
Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase.
(2001) Structure 9: 1095-106
PMID: 11709173
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
3'-nucleotidase activity 3'-nucleotidase activity
5'-nucleotidase activity 5'-nucleotidase activity
exopolyphosphatase activity exopolyphosphatase activity
metal ion binding metal ion binding
nucleotide binding nucleotide binding
XMP 5'-nucleosidase activity XMP 5'-nucleosidase activity
Biological process: not assigned
Cellular component:
cytoplasm cytoplasm
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, A-2
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: 5'-nucleotidase SurE
Source organism: Thermotoga maritima
Length: 247 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMRILVTNDDGIQSKGIIVLAELLSEEHEVFVVAPDKERSATGHSITIHVPLWMKKVFISERVVAYSTTGTPADCVKLAYNVVMDKRVDLIVSGVNRGPNMGMDILHSGTVSGAMEGAMMNIPSIAISSANYESPDFEGAARFLIDFLKEFDFSLLDPFTMLNINVPAGEIKGWRFTRQSRRRWNDYFEERVSPFGEKYYWMMGEVIEDDDRDDVDYKAVREGYVSITPIHPFLTNEQCLKKLREVYD
UniProtKB AC: P96112 (positions: 1-246)
Coverage: 99%
Name: 5'-nucleotidase SurE
Source organism: Thermotoga maritima
Length: 247 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMRILVTNDDGIQSKGIIVLAELLSEEHEVFVVAPDKERSATGHSITIHVPLWMKKVFISERVVAYSTTGTPADCVKLAYNVVMDKRVDLIVSGVNRGPNMGMDILHSGTVSGAMEGAMMNIPSIAISSANYESPDFEGAARFLIDFLKEFDFSLLDPFTMLNINVPAGEIKGWRFTRQSRRRWNDYFEERVSPFGEKYYWMMGEVIEDDDRDDVDYKAVREGYVSITPIHPFLTNEQCLKKLREVYD
UniProtKB AC: P96112 (positions: 1-247)
Coverage: 100%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Survival protein SurE
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
Two-state thermal unfolding (PMID:23409101). Domain-swapped dimer with extensive swap region and large dimer interface. Dimeric in solution (gel filtration, DLS).
Chain A:
N/A
Chain A-2:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
