Structure of PDB 1q45 Chain B

Receptor sequence
>1q45B (length=367) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
NETLFSSYKMGRFDLSHRVVLAPMTRCRALNGVPNAALAEYYAQRTTPGG
FLISEGTMVSPGSAGFPHVPGIYSDEQVEAWKQVVEAVHAKGGFIFCQLW
HVGRASHAVYQPNGGSPISSTNKPISENRWRVLLPDGSHVKYPKPRALEA
SEIPRVVEDYCLSALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDQY
GGSIANRCRFLKQVVEGVVSAIGASKVGVRVSPAIDHLDATDSDPLSLGL
AVVGMLNKLQGVNGSKLAYLHVTQPRYHAYDEEEAKLMKSLRMAYNGTFM
SSGGFNKELGMQAVQQGDADLVSYGRLFIANPDLVSRFKIDGELNKYNRK
TFYTQDPVVGYTDYPFL
3D structure
PDB1q45 X-ray structure of Arabidopsis At2g06050, 12-oxophytodienoate reductase isoform 3
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T33 H186 H189 Y191 R238 L246
Catalytic site (residue number reindexed from 1) T25 H178 H181 Y183 R230 L238
Enzyme Commision number 1.3.1.42: 12-oxophytodienoate reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FMN B A30 P31 M32 T33 G64 Q106 H186 H189 R238 S320 G321 G322 Y342 G343 R344 F370 Y371 A22 P23 M24 T25 G56 Q98 H178 H181 R230 S302 G303 G304 Y324 G325 R326 F352 Y353
Gene Ontology
Molecular Function
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016629 12-oxophytodienoate reductase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0009620 response to fungus
GO:0009695 jasmonic acid biosynthetic process
GO:0010193 response to ozone
GO:0031408 oxylipin biosynthetic process
GO:0048443 stamen development
Cellular Component
GO:0005777 peroxisome

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Cellular Component
External links
PDB RCSB:1q45, PDBe:1q45, PDBj:1q45
PDBsum1q45
PubMed15468319
UniProtQ9FUP0|OPR3_ARATH 12-oxophytodienoate reductase 3 (Gene Name=OPR3)

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