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2Q3O

Ensemble refinement of the protein crystal structure of 12-oxo-phytodienoate reductase isoform 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005777cellular_componentperoxisome
A0006633biological_processfatty acid biosynthetic process
A0009620biological_processresponse to fungus
A0009695biological_processjasmonic acid biosynthetic process
A0010181molecular_functionFMN binding
A0010193biological_processresponse to ozone
A0016491molecular_functionoxidoreductase activity
A0016629molecular_function12-oxophytodienoate reductase activity
A0031408biological_processoxylipin biosynthetic process
A0048443biological_processstamen development
B0005777cellular_componentperoxisome
B0006633biological_processfatty acid biosynthetic process
B0009620biological_processresponse to fungus
B0009695biological_processjasmonic acid biosynthetic process
B0010181molecular_functionFMN binding
B0010193biological_processresponse to ozone
B0016491molecular_functionoxidoreductase activity
B0016629molecular_function12-oxophytodienoate reductase activity
B0031408biological_processoxylipin biosynthetic process
B0048443biological_processstamen development
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FMN A 7401
ChainResidue
AALA30
AGLY321
AGLY322
APHE323
AGLY343
AARG344
APHE370
ATYR371
AHOH7438
AHOH7439
AHOH7460
APRO31
AHOH7461
AHOH7588
AMET32
ATHR33
AGLY64
AGLN106
AHIS186
AHIS189
AARG238

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN B 9401
ChainResidue
BALA30
BPRO31
BMET32
BTHR33
BGLY64
BGLN106
BHIS186
BHIS189
BARG238
BGLY322
BGLY343
BARG344
BPHE370
BTYR371
BHOH9417
BHOH9422
BHOH9452
BHOH9505
BHOH9547

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21915915
ChainResidueDetails
ATYR191
BTYR191

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:15468319, ECO:0000269|PubMed:17850744, ECO:0000269|PubMed:21915915, ECO:0007744|PDB:1Q45, ECO:0007744|PDB:2G5W, ECO:0007744|PDB:2Q3O
ChainResidueDetails
APRO31
BGLY343
AGLN106
AARG238
ASER320
AGLY343
BPRO31
BGLN106
BARG238
BSER320

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15468319, ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1Q45, ECO:0007744|PDB:2Q3O
ChainResidueDetails
AGLY64
BGLY64

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21915915, ECO:0007744|PDB:2G5W
ChainResidueDetails
AHIS186
AARG284
BHIS186
BARG284

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:Q8GYB8
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylthreonine; in 12-oxophytodienoate reductase 3, N-terminally processed => ECO:0007744|PubMed:22223895
ChainResidueDetails
ATHR2
BTHR2

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1oya
ChainResidueDetails
AHIS186
AHIS189
ATYR191

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1oya
ChainResidueDetails
BHIS186
BHIS189
BTYR191

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PDB entries from 2024-07-24

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