| Literature DB >> 16870440 |
Claudia Temperini1, Andrea Scozzafava, Claudiu T Supuran.
Abstract
The X-ray crystallographic structure for the adduct of an activator with human carbonic anhydrase isozyme I (hCA I) is reported. L-Histidine binds deep within the enzyme active site, participating in a network of hydrogen bonds involving its carboxylate moiety and the zinc-bound water molecule, as well as the imidazole of His200, being in van der Waals contacts with Thr199, His200, His64, and His67. This binding is very different from that to the other major cytosolic isozyme hCA II.Entities:
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Year: 2006 PMID： 16870440 DOI： 10.1016/j.bmcl.2006.07.021
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823