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Title
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Refined structure of the acetazolamide complex of human carbonic anhydrase II at 1.9 A.
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Authors
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J.Vidgren,
A.Liljas,
N.P.Walker.
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Ref.
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Int J Biol Macromol, 1990,
12,
342-344.
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PubMed id
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Abstract
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The binding of acetazolamide to human carbonic anhydrase II (HCA II) has been
investigated by X-ray crystallography. The atomic positions of the enzyme
inhibitor complex have been refined at 1.9 A resolution using the least squares
refinement program package PROLSQ. The crystallographic R-factor is 17.6%. The
bound inhibitor is clearly resolved in the active site of the enzyme. The
acetazolamide amine group is bound as a fourth ligand to the zinc ion, the other
three are all histidine residues. In addition to van der Waals' interactions and
the previously described binding of the sulphonamide group, the inhibitor forms
a hydrogen bond from the carbonyl oxygen of the acetylamido group to the amino
group of Gln 92.
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