Structure of PDB 2hs8 Chain A

Receptor sequence

>2hs8A (length=367) Species: 4081 (Solanum lycopersicum)

DGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATA
GGFLITEGTMISPTSAGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQ
LWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIG
TYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDE
YGGSLANRCKFITQVVQAVVSAIGADRVGVRVSPAIDHLDAMDSNPLSLG
LAVVERLNKIQLHSGSKLAYLHVTQPRLGSEEEEARLMRTLRNAYQGTFI
CSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKFNRK
TFYTQDPVVGYTDYPFL

3D structure

• PDB: 2hs8 Crystal structure of 12-oxophytodienoate reductase 3 from tomato: Self-inhibition by dimerization.
• Chain: A
• Resolution: 1.9 Å

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

External links

• PDB: RCSB:2hs8, PDBe:2hs8, PDBj:2hs8
• PDBsum: 2hs8
• PubMed: 16983071
• UniProt: Q9FEW9|OPR3_SOLLC 12-oxophytodienoate reductase 3 (Gene Name=OPR3)