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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 Å resolution, respectively. Both wild-type and mutant enzyme crystallize in space group P21 with cell dimensions a = 42.7, b = 41.7, c = 73.0 Å and β = 104.6°. 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 Oγ1. 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.

Supporting information

PDB references: 1cay; 1caz

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