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3IV9

Structure of the B12-dependent Methionine Synthase (MetH) C-teminal half in a "His-On" conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0008705molecular_functionmethionine synthase activity
A0009086biological_processmethionine biosynthetic process
A0031419molecular_functioncobalamin binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE B12 A 1301
ChainResidue
AVAL758
ALEU806
AILE807
ATHR808
AGLY833
AGLY834
AALA835
ATHR836
AVAL857
AGLN858
AASN859
AHIS759
AALA860
AASP1093
AALA1136
APRO1137
AGLY1138
ATYR1139
AHIS1145
ALYS1148
AMET1171
AGLY1174
AASP760
AALA1175
ASER1176
AVAL1177
ASER1178
AHOH1400
AILE761
AGLY762
AILE765
AVAL766
AGLY802
ASER804

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues135
DetailsDomain: {"description":"B12-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00666","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues330
DetailsDomain: {"description":"AdoMet activation","evidences":[{"source":"PROSITE-ProRule","id":"PRU00346","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7992050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BMT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"7992050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BMT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8939751","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
ASER810
AASP757
AHIS759

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
ALEU770

site_idMCSA1
Number of Residues3
DetailsM-CSA 268
ChainResidueDetails
AASP757hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AHIS759hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, increase nucleophilicity, metal ligand, proton acceptor, proton donor
ASER810hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

247536

PDB entries from 2026-01-14

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