Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I.
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Kannan KK, Ramanadham M, Jones TA
Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I.
Ann N Y Acad Sci. 1984;429:49-60.
- PubMed ID
- 6430186 [ View in PubMed]
- 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.