Ann N Y Acad Sci. 1984;429:49-60.

Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I.

Abstract

The structure of human erythrocyte carbonic anhydrase I has been refined to a final R value of 19% to 2-A resolution by a combination of least squares refinement and model fitting in a three-dimensional graphics display. About 300 solvent atoms have been located bound to the protein molecule. An interesting hydrogen bond network involving Zn2+, the liganded solvent, side chain groups of Thr-199, Glu-106, Thr-7, and His-64 through two solvent molecules have been found that may be important for the catalytic mechanism of the carbonic anhydrase.

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Cited by 15 PubMed Central articles

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Structures reported by this article

Structure, Refinement And Function Of Carbonic Anhydrase Isozymes. Refinement Of Human Carbonic Anhydrase I

PDB: 2CAB

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 2 Å

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