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1caz

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[[Image:1caz.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1caz| PDB=1caz | SCENE= }}
{{STRUCTURE_1caz| PDB=1caz | SCENE= }}
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'''WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE'''
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===WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE===
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==Overview==
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The molecular structures of the acetate complexes of wild-type human carbonic anhydrase II (HCAII) and of E106Q mutant human carbonic anhydrase II were solved with high completeness (89-91%) to 2.1 and 1.9 A resolution, respectively. Both wild-type and mutant enzyme crystallize in space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and beta = 104.6 degrees. The altered active-site hydrogen-bond network caused by the mutation results in a different binding of the inhibitor in the two complexes. In the mutant, but not in the wild-type complex, a carboxylate O atom is within hydrogen-bond distance of Thr199 Ogamma1. In the wild-type enzyme ligand hydrogen bonding to this atom is normally only found for hydrogen-bond donors. The importance of this discrimination on catalysis by the enzyme is discussed briefly.
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The line below this paragraph, {{ABSTRACT_PUBMED_15299482}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15299482 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15299482}}
==About this Structure==
==About this Structure==
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[[Category: Xue, Y.]]
[[Category: Xue, Y.]]
[[Category: Zaitsev, V.]]
[[Category: Zaitsev, V.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:32:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:29:41 2008''

Revision as of 17:29, 30 June 2008

Template:STRUCTURE 1caz

WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE

Template:ABSTRACT PUBMED 15299482

About this Structure

1CAZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Wild-type and E106Q mutant carbonic anhydrase complexed with acetate., Hakansson K, Briand C, Zaitsev V, Xue Y, Liljas A, Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):101-4. PMID:15299482

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