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1ICP

CRYSTAL STRUCTURE OF 12-OXOPHYTODIENOATE REDUCTASE 1 FROM TOMATO COMPLEXED WITH PEG400

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016629molecular_function12-oxophytodienoate reductase activity
A0031408biological_processoxylipin biosynthetic process
B0005737cellular_componentcytoplasm
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0016629molecular_function12-oxophytodienoate reductase activity
B0031408biological_processoxylipin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 505
ChainResidue
AARG205
ASER206
BARG156

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 506
ChainResidue
BALA244
BHIS245
BTYR246
BARG279

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 507
ChainResidue
ATYR246
AARG279
AHOH739
AALA244
AHIS245

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FMN A 501
ChainResidue
AALA34
APRO35
ALEU36
ATHR37
AALA68
AGLN110
AHIS187
AHIS190
AARG239
AGLY308
AGLY309
ATYR329
AGLY330
AARG331
APHE357
ATYR358
A2PE503
AHOH508
AHOH511
AHOH513
AHOH537

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FMN B 502
ChainResidue
BALA34
BPRO35
BLEU36
BTHR37
BALA68
BGLN110
BHIS187
BHIS190
BARG239
BGLY308
BGLY309
BTYR329
BGLY330
BARG331
BPHE357
BTYR358
B2PE504
BHOH522
BHOH525
BHOH536
BHOH722

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 2PE A 503
ChainResidue
ATHR37
AGLN39
AGLY77
ATYR78
AGLN140
AALA149
ATYR192
ATYR246
AARG279
AGLY309
AARG331
ATYR358
AFMN501
AHOH620
AHOH712
AHOH755

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 2PE B 504
ChainResidue
BTHR37
BGLN39
BGLY77
BTYR78
BPHE122
BGLN140
BILE141
BMET142
BALA149
BTYR192
BARG331
BTYR358
BFMN502
BHOH723
BHOH741

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19660473","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11377202","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1oya
ChainResidueDetails
ATYR192
AHIS187
AHIS190

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1oya
ChainResidueDetails
BTYR192
BHIS187
BHIS190

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1oya
ChainResidueDetails
ATYR192
APRO278

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1oya
ChainResidueDetails
BTYR192
BPRO278

246704

PDB entries from 2025-12-24

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