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

• QUK · 8-azanyl-4-(3-azanylpropoxy)quinoline-2-carboxylic acid · ligand · 4 copies · chains A, B
• QVS · 8-azanyl-4-oxidanyl-quinoline-2-carboxylic acid · ligand · 4 copies · chains A, B
• QVE · 8-azanyl-4-(2-hydroxy-2-oxoethyloxy)quinoline-2-carboxylic acid · ligand · 4 copies · chains A, B
• QUJ · 8-azanyl-4-(2-methylpropoxy)quinoline-2-carboxylic acid · ligand · 4 copies · chains A, B
• 6H0 · ~{N}-[[3-(4-formamidobutoxy)phenyl]methyl]-4-sulfamoyl-benzamide · ligand · 2 copies · chains A, B
• ZN · Zinc ion · metal · 2 copies · chains A, B
• NA · Sodium ion · metal · chains A
• GOL · Glycerol · additive · 4 copies · chains A, B
• PG4 · Tetraethylene glycol · additive · 2 copies
• DMS · Dimethyl sulfoxide · 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, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 225 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

• 5L6K · 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 5L6K · PDBe 5L6K · UniProt P00918