Ontology highlight
ABSTRACT:
SUBMITTER: Mazumdar PA
PROVIDER: S-EPMC2374158 | biostudies-literature | 2008 Mar
REPOSITORIES: biostudies-literature
Mazumdar Pooja Anjali PA Kumaran Desigan D Swaminathan Subramanyam S Das Amit Kumar AK
Acta crystallographica. Section F, Structural biology and crystallization communications 20080223 Pt 3
The enzyme human carbonic anhydrase II (hCAII) crystallized in an acetate-bound complex belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.3, b = 71.8, c = 74.0 A. 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-bon ...[more]