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1ICQ

CRYSTAL STRUCTURE OF 12-OXOPHYTODIENOATE REDUCTASE 1 FROM TOMATO COMPLEXED WITH 9R,13R-OPDA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006633biological_processfatty acid biosynthetic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016629molecular_function12-oxophytodienoate reductase activity
A0031408biological_processoxylipin biosynthetic process
B0005737cellular_componentcytoplasm
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 Residues21
DetailsBINDING SITE FOR RESIDUE FMN A 501
ChainResidue
AALA34
AGLY308
AGLY309
AGLY330
AARG331
APHE357
ATYR358
AOPD503
AHOH507
AHOH512
AHOH520
APRO35
AHOH535
AHOH622
ALEU36
ATHR37
AALA68
AGLN110
AHIS187
AHIS190
AARG239

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FMN B 502
ChainResidue
BALA34
BPRO35
BLEU36
BTHR37
BALA68
BGLN110
BHIS187
BHIS190
BARG239
BGLY308
BGLY309
BGLY330
BARG331
BTYR358
BOPD504
BHOH524
BHOH528
BHOH541

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OPD A 503
ChainResidue
ATHR37
AGLN39
ATYR78
AMET142
ASER143
AHIS187
AHIS190
ATYR192
ATYR246
ATYR358
AFMN501
AHOH540

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE OPD B 504
ChainResidue
BTHR37
BGLN39
BTYR78
BTRP112
BMET142
BSER143
BHIS187
BHIS190
BTYR192
BTYR246
BTYR358
BFMN502
BHOH553
BHOH620

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
ATYR192
BTYR192

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:19660473
ChainResidueDetails
APRO35
BARG239
BGLY309
BGLY330
AALA68
AGLN110
AARG239
AGLY309
AGLY330
BPRO35
BALA68
BGLN110

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11377202
ChainResidueDetails
ASER143
BSER143

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AHIS187
BHIS187

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG279
BARG279

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

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PDB entries from 2024-08-07

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