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PDBsum entry 4e1g

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
4e1g
Jmol
Contents
Protein chains
551 a.a.
Ligands
LNL ×2
COH ×2
NAG-NAG ×3
NAG-NAG-MAN
NAG ×2
BOG
EDO ×7
AKR ×2
Waters ×746
PDB id:
4e1g
Name: Oxidoreductase
Title: X-ray crystal structure of alpha-linolenic acid bound to the cyclooxygenase channel of cyclooxygenase-2
Structure: Prostaglandin g/h synthase 2. Chain: a, b. Fragment: unp residues 1-604. Synonym: cyclooxygenase-2, cox-2, glucocorticoid-regulated inflammatory cyclooxygenase, gripghs, macrophage activation associated marker protein p71/73, pes-2, phs ii, prostaglan synthase 2, pgh synthase 2, pghs-2, prostaglandin-endoperox synthase 2, tis10 protein. Engineered: yes.
Source: Mus musculus. Mouse. Organism_taxid: 10090. Strain: wild type. Gene: cox-2, cox2, pghs-b, ptgs2, tis10. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Resolution:
2.10Å     R-factor:   0.161     R-free:   0.203
Authors: A.J.Vecchio,M.G.Malkowski
Key ref: A.J.Vecchio et al. (2012). Investigating substrate promiscuity in cyclooxygenase-2: the role of Arg-120 and residues lining the hydrophobic groove. J Biol Chem, 287, 24619-24630. PubMed id: 22637474 DOI: 10.1074/jbc.M112.372243
Date:
06-Mar-12     Release date:   25-Apr-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q05769  (PGH2_MOUSE) -  Prostaglandin G/H synthase 2
Seq:
Struc:
 
Seq:
Struc:
604 a.a.
551 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.1.14.99.1  - Prostaglandin-endoperoxide synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O
Arachidonate
Bound ligand (Het Group name = COH)
matches with 51.16% similarity
+ AH(2)
+
2 × O(2)
Bound ligand (Het Group name = EDO)
matches with 50.00% similarity
= prostaglandin H(2)
+
+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     protein complex   8 terms 
  Biological process     maintenance of blood-brain barrier   64 terms 
  Biochemical function     lipid binding     10 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M112.372243 J Biol Chem 287:24619-24630 (2012)
PubMed id: 22637474  
 
 
Investigating substrate promiscuity in cyclooxygenase-2: the role of Arg-120 and residues lining the hydrophobic groove.
A.J.Vecchio, B.J.Orlando, R.Nandagiri, M.G.Malkowski.
 
  ABSTRACT  
 
No abstract given.