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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
A0018130biological_processobsolete heterocycle biosynthetic process
A0032259biological_processmethylation
A0044550biological_processsecondary metabolite biosynthetic process
A1901362biological_processorganic cyclic compound biosynthetic process
B0008168molecular_functionmethyltransferase activity
B0008171molecular_functionO-methyltransferase activity
B0018130biological_processobsolete heterocycle biosynthetic process
B0032259biological_processmethylation
B0044550biological_processsecondary metabolite biosynthetic process
B1901362biological_processorganic cyclic compound biosynthetic process
C0008168molecular_functionmethyltransferase activity
C0008171molecular_functionO-methyltransferase activity
C0018130biological_processobsolete heterocycle biosynthetic process
C0032259biological_processmethylation
C0044550biological_processsecondary metabolite biosynthetic process
C1901362biological_processorganic cyclic compound biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01020
ChainResidueDetails
AHIS373
BHIS373
CHIS373

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O04385
ChainResidueDetails
AGLY298
ASER353
AARG369
BGLY298
BSER353
BARG369
CGLY298
CSER353
CARG369

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01020
ChainResidueDetails
AASP321
BASP321
CASP321

221051

PDB entries from 2024-06-12

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