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1ZG3

Crystal structure of the isoflavanone 4'-O-methyltransferase complexed with SAH and 2,7,4'-trihydroxyisoflavanone

Functional Information from GO Data
ChainGOidnamespacecontents
A0008168molecular_functionmethyltransferase activity
A0008171molecular_functionO-methyltransferase activity
A0009701biological_processisoflavonoid phytoalexin biosynthetic process
A0016740molecular_functiontransferase activity
A0030746molecular_functionisoflavone 4'-O-methyltransferase activity
A0032259biological_processmethylation
A0046983molecular_functionprotein dimerization activity
A0102670molecular_function2,7,4'-trihydroxyisoflavanone-4'-O-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 2HI A 365
ChainResidue
ATYR25
ATYR318
AMET325
APHE326
AHOH4004
AHOH4039
AHOH4044
AILE122
AGLY125
AALA126
ASER131
AMET174
APHE175
AALA178
AMET179

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SAH A 3994
ChainResidue
AGLY207
AVAL213
AASP230
AGLN231
AVAL234
AASP250
AMET251
APHE252
ALYS264
AHOH4006

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01020","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01020","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kyw
ChainResidueDetails
AHIS268

238895

PDB entries from 2025-07-16

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