Structure of aspirin acetylated cyclooxygenase-1 in complex with diclofenac

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 9% strand (DSSP).

Ligands and binding sites

• HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
• DIF · 2-[2,6-dichlorophenyl)amino]benzeneacetic acid · ligand · 2 copies · chains A, B
• SAL · 2-hydroxybenzoic acid · ligand · chains B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar · 7 copies · chains A, B
• NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 3 copies · chains A, B
• MAN · alpha-D-mannopyranose · sugar · 2 copies · chains B
• BOG · octyl beta-D-glucopyranoside · additive · 4 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2670 Ų buried · 33 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 5 glycan, 1 covalent, 1 modified (disulfide, N-glycosylation, covalent ligand, nonstandard).

Compared structures

• 3N8Y · Structure of Aspirin Acetylated Cyclooxygenase-1 in Complex with Diclofenac · 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 3N8Y · PDBe 3N8Y · UniProt P05979