2cab | pdb_00002cab

STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I

spinqualitylabelsall models 2cab, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cab is a 1 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 1cab. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Activity: Carbonate dehydratase, with EC number 4.2.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CAH1_HUMAN] Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carbonic anhydrase 3D structures

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