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7WH9

holo structure of emodin 1-OH O-methyltransferase complex with emodin and S-Adenosyl-L-homocysteine

Functional Information from GO Data
ChainGOidnamespacecontents
A0008168molecular_functionmethyltransferase activity
A0008171molecular_functionO-methyltransferase activity
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
A0044550biological_processsecondary metabolite biosynthetic process
A0046983molecular_functionprotein dimerization activity
B0008168molecular_functionmethyltransferase activity
B0008171molecular_functionO-methyltransferase activity
B0016740molecular_functiontransferase activity
B0032259biological_processmethylation
B0044550biological_processsecondary metabolite biosynthetic process
B0046983molecular_functionprotein dimerization activity
C0008168molecular_functionmethyltransferase activity
C0008171molecular_functionO-methyltransferase activity
C0016740molecular_functiontransferase activity
C0032259biological_processmethylation
C0044550biological_processsecondary metabolite biosynthetic process
C0046983molecular_functionprotein dimerization activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"35475366","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PubMed","id":"35475366","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35475366","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7WH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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PDB entries from 2026-03-11

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