Publication Abstract from PubMed
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.
Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I.,Kannan KK, Ramanadham M, Jones TA Ann N Y Acad Sci. 1984;429:49-60. PMID:6430186[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
