Open AccessA novel acetate‐bound complex of human carbonic anhydrase II
Author(s) -
Mazumdar Pooja Anjali,
Kumaran Desigan,
Swaminathan Subramanyam,
Das Amit Kumar
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108002078
Subject(s) - carbonic anhydrase ii , carbonic anhydrase , enzyme , molecule , zinc , chemistry , solvent , bound water , stereochemistry , binding site , crystallography , biochemistry , organic chemistry
The enzyme human carbonic anhydrase II (hCAII) crystallized in an acetate‐bound complex belonging to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 42.3, b = 71.8, c = 74.0 Å. The structure was solved by the molecular‐replacement method and refined to an R value of 0.18 and an R free of 0.21. The acetate molecule replaced the zinc‐bound water molecule in the structure, differing from previous reports regarding the site of acetate binding. This mode of binding disrupts the hydrogen‐bonded solvent network required for activity of the enzyme. This mode of inhibitor binding is a novel one that has not been observed previously.