Structure of PDB 2hsa Chain A

Receptor sequence
>2hsaA (length=376) Species: 4081 (Solanum lycopersicum) [Search protein sequence]
NPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGF
LITEGTMISPTSAGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWH
VGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYE
ISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGG
SLANRCKFITQVVQAVVSAIGADRVGVRVSPAIDHLDAMDSNPLSLGLAV
VERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLR
NAYQGTFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNA
PLNKYNRKTFYTQDPVVGYTDYPFLQ
3D structure
PDB2hsa Crystal structure of 12-oxophytodienoate reductase 3 from tomato: Self-inhibition by dimerization.
ChainA
Resolution1.5 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 H185 H188 Y190 R237 L245 Q289
Catalytic site (residue number reindexed from 1) T24 H176 H179 Y181 R228 L236 Q280
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 A Q289 E291 Q280 E282
BS02 FMN A P31 M32 T33 Q106 H185 H188 R237 S319 G320 G321 G342 R343 Y370 P22 M23 T24 Q97 H176 H179 R228 S310 G311 G312 G333 R334 Y361
Gene Ontology
Molecular Function
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016629 12-oxophytodienoate reductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0009695 jasmonic acid biosynthetic process
GO:0031408 oxylipin biosynthetic process
Cellular Component
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2hsa, PDBe:2hsa, PDBj:2hsa
PDBsum2hsa
PubMed16983071
UniProtQ9FEW9|OPR3_SOLLC 12-oxophytodienoate reductase 3 (Gene Name=OPR3)

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