2cab

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{{STRUCTURE_2cab| PDB=2cab | SCENE= }}
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'''STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I'''
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===STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 6430186 is the PubMed ID number.
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{{ABSTRACT_PUBMED_6430186}}
==About this Structure==
==About this Structure==
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[[Category: Ramanadham, M.]]
[[Category: Ramanadham, M.]]
[[Category: Hydro-lyase]]
[[Category: Hydro-lyase]]
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Revision as of 11:01, 28 July 2008

Image:2cab.png

Template:STRUCTURE 2cab

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

Template:ABSTRACT PUBMED 6430186

About this Structure

2CAB is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1cab. 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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