Crystal structure of human carbonic anhydrase II in complex with a quinoline oligoamide foldamer

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 30% strand (DSSP).

Ligands and binding sites

• Q4I · 8-({[4-(3-aminopropoxy)-8-({[4-hydroxy-8-({[4-(2-methylpropoxy)-8-({[4-(3-{[(4-sulfamoylbenzoyl)amino]methyl}phenoxy)butyl]carbamoyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)quinolin-2-yl]carbonyl}amino)-4-(carboxymethoxy)quinoline-2-carboxylic acid · ligand · 2 copies · chains A, B
• ZN · Zinc ion · metal · 13 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 241 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

• 4LP6 · Crystal Structure of Human Carbonic Anhydrase II in complex with a quinoline oligoamide… · the same entry in another collection · chain A against A, TM-score 1.00
• P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · a predicted model of the same protein · chain B 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 P00918
• Elsewhere: RCSB PDB 4LP6 · PDBe 4LP6 · UniProt P00918