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1cay

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[[Image:1cay.jpg|left|200px]]<br /><applet load="1cay" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1cay.jpg|left|200px]]
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caption="1cay, resolution 2.1&Aring;" />
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'''WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE'''<br />
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{{Structure
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|PDB= 1cay |SIZE=350|CAPTION= <scene name='initialview01'>1cay</scene>, resolution 2.1&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1CAY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CAY OCA].
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1CAY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CAY OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299482 15299482]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15299482 15299482]
[[Category: Carbonate dehydratase]]
[[Category: Carbonate dehydratase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: lyase(oxo-acid)]]
[[Category: lyase(oxo-acid)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:11 2008''

Revision as of 08:22, 20 March 2008

Image:1cay.jpg


PDB ID 1cay

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands: and
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Coordinates: save as pdb, mmCIF, xml



WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE


Contents

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.

Disease

Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]

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

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