› 5cox

X-ray diffraction
3Å resolution

UNINHIBITED MOUSE CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2)

Released:
DOI: 10.2210/pdb5cox/pdb
PDB entry 5cox coloured by chain, front view.
PDB entry 5cox coloured by chain, side view.
PDB entry 5cox coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents.
Kurumbail RG, Stevens AM, Gierse JK, McDonald JJ, Stegeman RA, Pak JY, Gildehaus D, Miyashiro JM, Penning TD, Seibert K, Isakson PC, Stallings WC
Nature 384 644-8
PMID: 8967954

Function and Biology Details

Reaction catalysed: 
Arachidonate + AH(2) + 2 O(2) = prostaglandin H(2) + A + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostaglandin G/H synthase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 587 amino acids
Theoretical weight: 67.32 KDa
Source organism: Mus musculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q05769 (Residues: 18-604; Coverage: 100%)
Gene names: Cox-2, Cox2, Pghs-b, Ptgs2, Tis10
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
1 bound ligand:
Ligand NAG 12 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21212
Unit cell:
a: 180.46Å b: 134.42Å c: 119.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.321 0.321 0.308
Expression system: Spodoptera frugiperda

Quick links

Citations

164 review citations

Cyclooxygenases 1 and 2.
Vane et al. (1998)
163 more

9 mentions without citation

Lessons from Hot Spot Analysis for Fragment-Based Drug Discovery.
Hall et al. (2015)
8 more