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6IV7

The crystal structure of a SAM-dependent enzyme from aspergillus flavus

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
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue SAH A 401
ChainResidue
AGLY227
AARG291
AHOH501
AHOH542
AHOH558
AHOH560
AGLY229
AASP252
ALEU253
AVAL256
AHIS274
AASN275
APHE276
AHIS277

site_idAC2
Number of Residues13
Detailsbinding site for residue SAH B 401
ChainResidue
BGLY227
BGLY229
BASP252
BVAL256
BHIS274
BASN275
BPHE276
BHIS277
BARG291
BHOH533
BHOH540
BHOH548
BHOH555

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsRegion: {"description":"Substrate binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues26
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O04385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01020","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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