› 3qmo

X-ray diffraction
3Å resolution

X-ray crystal structure of NS-398 bound to the cyclooxygenase channel of cyclooxygenase-2

Released:
DOI: 10.2210/pdb3qmo/pdb
PDB entry 3qmo coloured by chain, front view.
PDB entry 3qmo coloured by chain, side view.
PDB entry 3qmo coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The structure of NS-398 bound to cyclooxygenase-2.
Vecchio AJ, Malkowski MG
J Struct Biol 176 254-8 (2011)
PMID: 21843643

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Prostaglandin G/H synthase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 610 amino acids
Theoretical weight: 69.88 KDa
Source organism: Mus musculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q05769 (Residues: 1-19, 20-604; Coverage: 100%)
Gene names: Cox-2, Cox2, Pghs-b, Ptgs2, Tis10
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
Carbohydrate polymer : NEW Components: NAG, NDG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
5 bound ligands:
Ligand GOL 6 x GOL
Ligand NS4 2 x NS4
Ligand NAG 2 x NAG
Ligand BOG 1 x BOG
Ligand MAN 1 x MAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: I222
Unit cell:
a: 120.428Å b: 131.213Å c: 179.568Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.225
Expression system: Spodoptera frugiperda

Quick links

Citations

12 citation in other articles

The structure of ibuprofen bound to cyclooxygenase-2.
Orlando et al. (2015)
11 more

11 mentions without citation

Histone-modifying enzymes, histone modifications and histone chaperones in nucleosome assembly: Lessons learned from Rtt109 histone acetyltransferases.
Dahlin et al. (2015)
10 more