2cab: Difference between revisions

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[[Image:2cab.gif|left|200px]]
{{Seed}}
[[Image:2cab.png|left|200px]]


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{{STRUCTURE_2cab|  PDB=2cab  |  SCENE=  }}  
{{STRUCTURE_2cab|  PDB=2cab  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_6430186}}, adds the Publication Abstract to the page
(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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:34:06 2008''
 
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