Refined structure of the acetazolamide complex of human carbonic anhydrase II at 1.9 A.
The binding of acetazolamide to human carbonic anhydrase II (HCA II) has been investigated by X-ray crystallography. The atomic positions of the enzyme inhibitor complex have been refined at 1.9 A resolution using the least squares refinement program package PROLSQ. The crystallographic R-factor is 17.6%. The bound inhibitor is clearly resolved in the active site of the enzyme. The acetazolamide amine group is bound as a fourth ligand to the zinc ion, the other three are all histidine residues. In addition to van der Waals' interactions and the previously described binding of the sulphonamide group, the inhibitor forms a hydrogen bond from the carbonyl oxygen of the acetylamido group to the amino group of Gln 92.
Vidgren
J
J
Department of Molecular Biophysics, Chemical Center, University of Lund, Sweden.
Liljas
A
A
Walker
N P
NP
D000086:Acetazolamide / Q000737:chemistry* / Q000378:metabolism; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D014961:X-Ray Diffraction; D015032:Zinc
D002256:Carbonic Anhydrases; D015032:Zinc; D000086:Acetazolamide