The structure of meclofenamic acid bound to human cyclooxygenase-2

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 9% strand (DSSP).

Ligands and binding sites

• AKR · Acrylic acid · ligand · 3 copies · chains A, B
• JMS · 2-[(2,6-dichloro-3-methyl-phenyl)amino]benzoic acid · ligand · 2 copies · chains A, B
• COH · Protoporphyrin IX containing co · ligand · 2 copies · chains A, B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
• MAN · alpha-D-mannopyranose · sugar · 4 copies · chains B, A
• BOG · octyl beta-D-glucopyranoside · additive · chains A

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

Pockets

11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2537 Ų buried · 44 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 6 glycan, 2 covalent (disulfide, N-glycosylation, covalent ligand).

Compared structures

• 5IKQ · The Structure of Meclofenamic Acid Bound to Human Cyclooxygenase-2 · the same entry in another collection · chain A against A, TM-score 1.00
• P35354 · AlphaFold monomer V2.0 prediction for prostaglandin G/H synthase 2 (P35354) · 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 P35354
• Elsewhere: RCSB PDB 5IKQ · PDBe 5IKQ · UniProt P35354