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5XOH

Crystal structure of bergaptol o-methyltransferase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008168molecular_functionmethyltransferase activity
A0008171molecular_functionO-methyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0009753biological_processresponse to jasmonic acid
A0009805biological_processcoumarin biosynthetic process
A0019438biological_processobsolete aromatic compound biosynthetic process
A0030752molecular_function5-hydroxyfuranocoumarin 5-O-methyltransferase activity
A0032259biological_processmethylation
A0046983molecular_functionprotein dimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue SAH A 401
ChainResidue
APHE158
AILE262
ATRP266
A8B6402
AHOH501
AHOH539
AHOH543
AMET175
ASER179
AGLY203
AASP226
ALEU227
AASP246
AMET247
ALYS260

site_idAC2
Number of Residues11
Detailsbinding site for residue 8B6 A 402
ChainResidue
ALEU122
AHIS126
AILE157
APHE158
AMET175
ATRP261
AHIS264
ASER265
ALEU312
AMET316
ASAH401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01020
ChainResidueDetails
AHIS264

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:31666994, ECO:0007744|PDB:5XOH
ChainResidueDetails
AHIS126
ASER179
AGLY203
AASP226
AASP246
ALYS260
AHIS264

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Determines the catalytic selectivity of hydroxyl groups in esculetin => ECO:0000250|UniProtKB:A0A4P8DY91
ChainResidueDetails
AHIS126

219140

PDB entries from 2024-05-01

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