Database accession: MF7000647
Name: Methyltransferase CalO6
PDB ID: 4z2y
Experimental method: X-ray (3.40 Å)
Assembly: Homodimer
Source organism: Micromonospora echinospora
Primary publication of the structure:
Tsodikov OV, Hou C, Walsh CT, Garneau-Tsodikova S
Crystal structure of O-methyltransferase CalO6 from the calicheamicin biosynthetic pathway: a case of challenging structure determination at low resolution.
(2015) BMC Struct. Biol. 15: 13
PMID: 26170207
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
O-methyltransferase activity O-methyltransferase activity
Biological process: not assigned
Cellular component: not assigned
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: CalO6
Source organism: Micromonospora echinospora
Length: 356 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMELTTTAARPGLRHRMQQLIYGFFTAQTLHVAVRLRIPDLLADGARDVGDLASATGADAPSLRRLLRALVFLEVLDEPAPGTFALTEQGEVLRADVTGSMRELVLLLSGPESWAAWGQLEHSVRTGEVAWEHVHGRSCFDHLMADPQRQAAFNAAMAEGSRAFVPTLLSAYDFGDLRTVVDVGGGSGALLAGVLAAHPHLRGTVFDTPDGVADAARTVAEQGVADRCGVETGDFFVSVPPGADAYVLKSVLHDWDDEQCVEVLRTVRRAVRPDSRVILVESLMPTTVTTAPSVAQVVMNDLNMMVCHGGRERTVAEFRELLRVAGFRLESVTPCPAPSVVGILEAAPAPATGPDGS
UniProtKB AC: Q8KND2 (positions: 11-346)
Coverage: 94%
Name: CalO6
Source organism: Micromonospora echinospora
Length: 356 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMELTTTAARPGLRHRMQQLIYGFFTAQTLHVAVRLRIPDLLADGARDVGDLASATGADAPSLRRLLRALVFLEVLDEPAPGTFALTEQGEVLRADVTGSMRELVLLLSGPESWAAWGQLEHSVRTGEVAWEHVHGRSCFDHLMADPQRQAAFNAAMAEGSRAFVPTLLSAYDFGDLRTVVDVGGGSGALLAGVLAAHPHLRGTVFDTPDGVADAARTVAEQGVADRCGVETGDFFVSVPPGADAYVLKSVLHDWDDEQCVEVLRTVRRAVRPDSRVILVESLMPTTVTTAPSVAQVVMNDLNMMVCHGGRERTVAEFRELLRVAGFRLESVTPCPAPSVVGILEAAPAPATGPDGS
UniProtKB AC: Q8KND2 (positions: 11-346)
Coverage: 94%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Dimeric O-methyltransferase
Evidence level: Indirect evidence
Evidence coverage: Only some parts of the structure participates in mutual synergistic folding.
Complex Evidence:
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).
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)
