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PDBsum entry 3rde

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase/oxidoreductase inhibitor PDB id
3rde
Jmol
Contents
Protein chains
552 a.a.
Ligands
OYP ×4
Metals
__K ×2
FE2 ×4
Waters ×1274
PDB id:
3rde
Name: Oxidoreductase/oxidoreductase inhibitor
Title: Crystal structure of the catalytic domain of porcine leukocy lipoxygenase
Structure: Arachidonate 12-lipoxygenase, 12s-type. Chain: a, b, c, d. Fragment: unp residues 112-663. Synonym: 12s-lox, 12s-lipoxygenase. Engineered: yes. Mutation: yes
Source: Sus scrofa. Pigs,swine,wild boar. Organism_taxid: 9823. Gene: alox12. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.89Å     R-factor:   0.173     R-free:   0.214
Authors: M.O.Funk,S.Xu,L.J.Marnett,T.C.Mueser
Key ref: S.Xu et al. (2012). Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis. Structure, 20, 1490-1497. PubMed id: 22795085 DOI: 10.1016/j.str.2012.06.003
Date:
01-Apr-11     Release date:   18-Apr-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P16469  (LOX12_PIG) -  Arachidonate 15-lipoxygenase
Seq:
Struc:
 
Seq:
Struc:
663 a.a.
552 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: E.C.1.13.11.31  - Arachidonate 12-lipoxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa- 5,8,10,14-tetraenoate
Arachidonate
Bound ligand (Het Group name = OYP)
matches with 41.18% similarity
+ O(2)
= (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa- 5,8,10,14-tetraenoate
      Cofactor: Fe cation
   Enzyme class 3: E.C.1.13.11.33  - Arachidonate 15-lipoxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa- 5,8,11,13-tetraenoate
Arachidonate
+ O(2)
= (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa- 5,8,11,13-tetraenoate
      Cofactor: Fe cation
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen     3 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.str.2012.06.003 Structure 20:1490-1497 (2012)
PubMed id: 22795085  
 
 
Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis.
S.Xu, T.C.Mueser, L.J.Marnett, M.O.Funk.
 
  ABSTRACT  
 
No abstract given.