Structure of PDB 3hgo Chain A

Receptor sequence
>3hgoA (length=367) Species: 4081 (Solanum lycopersicum) [Search protein sequence]
DGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATA
GGFLITEGTMISPTSAGYPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQ
LWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIG
TYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDE
YGGSLANRCKFITQVVQAVVSAIGADRVGVRVSPAIDYLDAMDSNPLSLG
LAVVERLNKIQLHSGSKLAYLHVTQPRLGSEEEEARLMRTLRNAYQGTFI
CSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRK
TFYTQDPVVGYTDYPFL
3D structure
PDB3hgo Structural basis of substrate specificity of plant 12-oxophytodienoate reductases.
ChainA
Resolution2.3 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
Catalytic site (residue number reindexed from 1) T27 H179 H182 Y184 R231 L239
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 P31 M32 T33 Q106 H185 H188 R237 S319 G320 G321 G342 R343 F369 Y370 P25 M26 T27 Q100 H179 H182 R231 S302 G303 G304 G325 R326 F352 Y353
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:3hgo, PDBe:3hgo, PDBj:3hgo
PDBsum3hgo
PubMed19660473
UniProtQ9FEW9|OPR3_SOLLC 12-oxophytodienoate reductase 3 (Gene Name=OPR3)

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