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3I5U

Crystal structure of an O-methyltransferase (NcsB1) from neocarzinostatin biosynthesis in complex with S-adenosylmethionine (SAM) and 2-hydroxy-5-methyl naphthoic acid (MNA)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008168molecular_functionmethyltransferase activity
A0008171molecular_functionO-methyltransferase activity
A0016740molecular_functiontransferase activity
A0017000biological_processantibiotic biosynthetic process
A0032259biological_processmethylation
A0046983molecular_functionprotein dimerization activity
B0003824molecular_functioncatalytic activity
B0008168molecular_functionmethyltransferase activity
B0008171molecular_functionO-methyltransferase activity
B0016740molecular_functiontransferase activity
B0017000biological_processantibiotic biosynthetic process
B0032259biological_processmethylation
B0046983molecular_functionprotein dimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAM A 401
ChainResidue
ATRP133
APHE228
APHE229
ASER242
AALA243
AASP247
A5NA402
AHOH523
AHOH538
AHOH581
AHOH582
APHE146
AHOH723
AMET150
AHIS153
AGLY177
AGLY179
AASP200
AGLY226
ASER227

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 5NA A 402
ChainResidue
ATRP96
AMET150
AHIS153
AMET286
AARG289
ATYR293
APHE294
ASAM401
AHOH593
BARG11

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
ALEU154
AGLU155
ATYR158
ATHR159
AGLY160
AHOH550

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAM B 401
ChainResidue
BTRP133
BMET150
BHIS153
BGLY177
BGLY179
BASP200
BPRO204
BGLY226
BSER227
BPHE228
BPHE229
BSER242
BALA243
BASP247
B5NA402
BHOH526
BHOH536
BHOH537
BHOH573
BHOH616
BHOH722

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 5NA B 402
ChainResidue
AARG11
BTRP96
BPHE146
BMET150
BHIS153
BMET286
BARG289
BTYR293
BSAM401

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 404
ChainResidue
BLEU154
BGLU155
BTYR158
BHOH636

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01020","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19702337","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19702337","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kyw
ChainResidueDetails
AHIS246

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kyw
ChainResidueDetails
BHIS246

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PDB entries from 2025-12-24

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