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1cay

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[[Image:1cay.jpg|left|200px]]
[[Image:1cay.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1cay |SIZE=350|CAPTION= <scene name='initialview01'>1cay</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1cay", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1cay| PDB=1cay | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cay OCA], [http://www.ebi.ac.uk/pdbsum/1cay PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cay RCSB]</span>
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}}
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'''WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE'''
'''WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE'''
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[[Category: Xue, Y.]]
[[Category: Xue, Y.]]
[[Category: Zaitsev, V.]]
[[Category: Zaitsev, V.]]
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[[Category: lyase(oxo-acid)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:32:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:18:10 2008''
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Revision as of 09:32, 2 May 2008

Image:1cay.jpg

Template:STRUCTURE 1cay

WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE


Overview

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.

About this Structure

1CAY 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 Page seeded by OCA on Fri May 2 12:32:15 2008

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