1CAZ

WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE

Summary for 1CAZ

• Entry DOI: 10.2210/pdb1caz/pdb
• Descriptor: CARBONIC ANHYDRASE II, ZINC ION, ACETIC ACID, ... (4 entities in total)
• Functional Keywords: lyase(oxo-acid)
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P00918
• Total number of polymer chains: 1
• Total formula weight: 29347.75

Authors

Hakansson, K.,Briand, C.,Zaitsev, V.,Xue, Y.,Liljas, A. (deposition date: 1993-02-26, release date: 1993-10-31, Last modification date: 2024-02-07)

Primary citation

Hakansson, K.,Briand, C.,Zaitsev, V.,Xue, Y.,Liljas, A.
Wild-type and E106Q mutant carbonic anhydrase complexed with acetate.
Acta Crystallogr.,Sect.D, 50:101-104, 1994

PubMed Abstract: The molecular structures of the acetate complexes of wild-type human carbonic anhydrase II (HCAII) and of E106Q mutant human carbonic anhydrase II were solved with high completeness (89-91%) to 2.1 and 1.9 A resolution, respectively. Both wild-type and mutant enzyme crystallize in space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and beta = 104.6 degrees. The altered active-site hydrogen-bond network caused by the mutation results in a different binding of the inhibitor in the two complexes. In the mutant, but not in the wild-type complex, a carboxylate O atom is within hydrogen-bond distance of Thr199 Ogamma1. In the wild-type enzyme ligand hydrogen bonding to this atom is normally only found for hydrogen-bond donors. The importance of this discrimination on catalysis by the enzyme is discussed briefly.

PubMed: 15299482
DOI: 10.1107/S0907444993009667

Experimental method

X-RAY DIFFRACTION (1.9 Å)