| Literature DB >> 6430186 |
K K Kannan, M Ramanadham, T A Jones.
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.Entities:
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Year: 1984 PMID： 6430186 DOI： 10.1111/j.1749-6632.1984.tb12314.x
Source DB: PubMed Journal: Ann N Y Acad Sci ISSN： 0077-8923 Impact factor: 5.691