Crystal structure of cyclooxygenase-1 in complex with celecoxib

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 9% strand (DSSP).

Ligands and binding sites

• HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
• CEL · 4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide · ligand · 2 copies · chains A, B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, B
• MAN · alpha-D-mannopyranose · sugar · 3 copies · chains B
• NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 3 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar · 2 copies · chains B
• BOG · octyl beta-D-glucopyranoside · additive · 4 copies · chains A, B
• FLC · Citrate anion · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2700 Ų buried · 35 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

• 3KK6 · Crystal Structure of Cyclooxygenase-1 in complex with celecoxib · the same entry in another collection · chain A against A, TM-score 1.00
• P05979 · AlphaFold monomer V2.0 prediction for prostaglandin G/H synthase 1 (P05979) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P05979
• Elsewhere: RCSB PDB 3KK6 · PDBe 3KK6 · UniProt P05979