2cab
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(New page: 200px<br /> <applet load="2cab" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cab, resolution 2.0Å" /> '''STRUCTURE, REFINEMEN...)
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Revision as of 10:40, 8 November 2007
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STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I
Overview
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.
About this Structure
2CAB is a Single protein structure of sequence from Homo sapiens with ZN as ligand. This structure superseeds the now removed PDB entry 1CAB. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
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
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