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

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 30% strand (DSSP).

Ligands and binding sites

• 6H0 · ~{N}-[[3-(4-formamidobutoxy)phenyl]methyl]-4-sulfamoyl-benzamide · ligand · 2 copies · chains A, B
• QOL · 8-azanyl-4-[2-(hydroxymethyl)-3-oxidanyl-propoxy]quinoline-2-carbaldehyde · ligand · 2 copies · chains B
• QVS · 8-azanyl-4-oxidanyl-quinoline-2-carboxylic acid · ligand · 2 copies · chains A, B
• QUK · 8-azanyl-4-(3-azanylpropoxy)quinoline-2-carboxylic acid · ligand · 2 copies · chains A, B
• QVE · 8-azanyl-4-(2-hydroxy-2-oxoethyloxy)quinoline-2-carboxylic acid · ligand · 2 copies · chains A, B
• ZN · Zinc ion · metal · 13 copies · chains A, B
• GOL · Glycerol · additive · 4 copies · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 364 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

• 5L70 · 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 A against A, TM-score 0.99

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 5L70 · PDBe 5L70 · UniProt P00918