PDBsum entry 1q45

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
Jmol PyMol
Protein chains
365 a.a. *
FMN ×2
Waters ×410
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: 12-0xo-phytodienoate reductase isoform 3
Structure: 12-oxophytodienoate-10,11-reductase. Chain: a, b. Synonym: 12-0xo-phytodienoate reductase isoform 3. 12- oxophytodienoate reductase. Opr3. Dde1. Engineered: yes
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: at2g06050. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.00Å     R-factor:   0.189     R-free:   0.236
Authors: G.N.Phillips Jr.,K.A.Johnson,C.A.Bingman,D.W.Smith,Center For Eukaryotic Structural Genomics (Cesg)
Key ref:
T.E.Malone et al. (2005). X-ray structure of Arabidopsis At2g06050, 12-oxophytodienoate reductase isoform 3. Proteins, 58, 243-245. PubMed id: 15468319 DOI: 10.1002/prot.20162
01-Aug-03     Release date:   25-Nov-03    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q9FUP0  (OPR3_ARATH) -  12-oxophytodienoate reductase 3
391 a.a.
365 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - 12-oxophytodienoate reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 8-((1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl)octanoate + NADP+ = (15Z)-12-oxophyto-10,15-dienoate + NADPH
+ NADP(+)
= (15Z)-12-oxophyto-10,15-dienoate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     peroxisome   1 term 
  Biological process     oxidation-reduction process   9 terms 
  Biochemical function     catalytic activity     4 terms  


DOI no: 10.1002/prot.20162 Proteins 58:243-245 (2005)
PubMed id: 15468319  
X-ray structure of Arabidopsis At2g06050, 12-oxophytodienoate reductase isoform 3.
T.E.Malone, S.E.Madson, R.L.Wrobel, W.B.Jeon, N.S.Rosenberg, K.A.Johnson, C.A.Bingman, D.W.Smith, G.N.Phillips, J.L.Markley, B.G.Fox.
No abstract given.

  Selected figure(s)  
Figure 1.
Figure 1. A stereo representation of the X-ray structure of Arabidopsis OPR3 (1Q45). The position of the substrate-binding loop of OPR1 was obtained from alignment of the backbone atoms of OPR1 and OPR3. The OPR1 loop is shown in orange (residues L137-F151), while the comparable OPR3 loop is shown in blue (residues I133-Y150).
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 58, 243-245) copyright 2005.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19416520 W.Li, B.Liu, L.Yu, D.Feng, H.Wang, and J.Wang (2009).
Phylogenetic analysis, structural evolution and functional divergence of the 12-oxo-phytodienoate acid reductase gene family in plants.
  BMC Evol Biol, 9, 90.  
18495659 Y.Zhang, K.H.Teoh, D.W.Reed, L.Maes, A.Goossens, D.J.Olson, A.R.Ross, and P.S.Covello (2008).
The molecular cloning of artemisinic aldehyde Delta11(13) reductase and its role in glandular trichome-dependent biosynthesis of artemisinin in Artemisia annua.
  J Biol Chem, 283, 21501-21508.  
16156787 H.Khan, T.Barna, N.C.Bruce, A.W.Munro, D.Leys, and N.S.Scrutton (2005).
Proton transfer in the oxidative half-reaction of pentaerythritol tetranitrate reductase. Structure of the reduced enzyme-progesterone complex and the roles of residues Tyr186, His181, His184.
  FEBS J, 272, 4660-4671.
PDB codes: 2aba 2abb
15905167 H.L.Messiha, N.C.Bruce, B.M.Sattelle, M.J.Sutcliffe, A.W.Munro, and N.S.Scrutton (2005).
Role of active site residues and solvent in proton transfer and the modulation of flavin reduction potential in bacterial morphinone reductase.
  J Biol Chem, 280, 27103-27110.  
15890652 K.Kitzing, T.B.Fitzpatrick, C.Wilken, J.Sawa, G.P.Bourenkov, P.Macheroux, and T.Clausen (2005).
The 1.3 A crystal structure of the flavoprotein YqjM reveals a novel class of Old Yellow Enzymes.
  J Biol Chem, 280, 27904-27913.
PDB codes: 1z41 1z42 1z44 1z48
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