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1ICS

CRYSTAL STRUCTURE OF 12-OXOPHYTODIENOATE REDUCTASE 1 FROM TOMATO

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 Residues18
DetailsBINDING SITE FOR RESIDUE FMN A 501
ChainResidue
AALA34
AGLY308
AGLY309
AGLY330
AARG331
APHE357
ATYR358
AHOH518
AHOH539
AHOH615
APRO35
ALEU36
ATHR37
AALA68
AGLN110
AHIS187
AHIS190
AARG239

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN B 502
ChainResidue
BALA34
BPRO35
BLEU36
BTHR37
BALA68
BGLN110
BHIS187
BHIS190
BARG239
BGLY308
BGLY309
BTYR329
BGLY330
BARG331
BTYR358
BHOH503
BHOH511
BHOH552
BHOH575

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

246031

PDB entries from 2025-12-10

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