› 1ht5

X-ray diffraction
2.75Å resolution

THE 2.75 ANGSTROM RESOLUTION MODEL OF OVINE COX-1 COMPLEXED WITH METHYL ESTER FLURBIPROFEN

Released:
DOI: 10.2210/pdb1ht5/pdb
PDB entry 1ht5 coloured by chain, front view.
PDB entry 1ht5 coloured by chain, side view.
PDB entry 1ht5 coloured by chain, top view.
Source organism: Ovis aries
Primary publication:
Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations.
Selinsky BS, Gupta K, Sharkey CT, Loll PJ
Biochemistry 40 5172-80 (2001)
PMID: 11318639

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-138844 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostaglandin G/H synthase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 551 amino acids
Theoretical weight: 63.51 KDa
Source organism: Ovis aries
UniProt:
  • Canonical: P05979 (Residues: 33-583; Coverage: 96%)
Gene names: COX1, PTGS1
Sequence domains: Animal haem peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
3 bound ligands:
Ligand BOG 3 x BOG
Ligand NAG 10 x NAG
Ligand FL2 2 x FL2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: I222
Unit cell:
a: 98.888Å b: 209.45Å c: 223.013Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.223 0.252

Quick links

Citations

13 review citations

Enzymes of the cyclooxygenase pathways of prostanoid biosynthesis.
Smith et al. (2011)
12 more

8 mentions without citation

Structural and Chemical Biology of the Interaction of Cyclooxygenase with Substrates and Non-Steroidal Anti-Inflammatory Drugs.
Rouzer et al. (2020)
7 more