1XEG

Crystal structure of human carbonic anhydrase II complexed with an acetate ion

Summary for 1XEG

• Entry DOI: 10.2210/pdb1xeg/pdb
• Related: 1AVN 1CAY 1CAZ
• Descriptor: Carbonic anhydrase II, ACETATE ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: human carbonic anhydrase ii, acetate ion complex, lyase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P00918
• Total number of polymer chains: 1
• Total formula weight: 29413.52

Authors

Mazumdar, P.A.,Kumaran, D.,Das, A.K.,Swaminathan, S. (deposition date: 2004-09-10, release date: 2005-09-27, Last modification date: 2024-02-14)

Primary citation

Mazumdar, P.A.,Kumaran, D.,Swaminathan, S.,Das, A.K.
A novel acetate-bound complex of human carbonic anhydrase II.
Acta Crystallogr.,Sect.F, 64:163-166, 2008

PubMed Abstract: 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-bonded solvent network required for activity of the enzyme. This mode of inhibitor binding is a novel one that has not been observed previously.

PubMed: 18323598
DOI: 10.1107/S1744309108002078

Experimental method

X-RAY DIFFRACTION (1.81 Å)