1h9q: Difference between revisions
New page: left|200px<br /> <applet load="1h9q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h9q, resolution 2.2Å" /> '''H119Q CARBONIC ANHYD... |
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==About this Structure== | ==About this Structure== | ||
1H9Q 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 ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H9Q OCA]]. | 1H9Q 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 ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Site: ZN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H9Q OCA]]. | ||
==Reference== | ==Reference== | ||
Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity., Lesburg CA, Huang C, Christianson DW, Fierke CA, Biochemistry. 1997 Dec 16;36(50):15780-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9398308 9398308] | Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity., Lesburg CA, Huang C, Christianson DW, Fierke CA, Biochemistry. 1997 Dec 16;36(50):15780-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9398308 9398308] | ||
[[Category: Carbonate dehydratase]] | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxo-acid]] | [[Category: oxo-acid]] | ||
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Revision as of 15:15, 30 October 2007
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H119Q CARBONIC ANHYDRASE II
OverviewOverview
The catalytic zinc ion of human carbonic anhydrase II (CAII) is, coordinated by three histidine ligands (H94, H96, and H119) and a, hydroxide ion with tetrahedral geometry. Structural and functional, analysis of variants in which the zinc ligands H94 and H119 are, substituted with asparagine and glutamine, and comparison with results, obtained with aspartate and glutamate substitutions indicate that the, neutral ligand field provided by the protein optimizes the electrostatic, environment for the catalytic function of the metal ion, including, stabilization of bound anions. This is demonstrated by catalytic activity, measurements for ester hydrolysis and CO2 hydration, as well as, sulfonamide inhibitor affinity assays. High-resolution X-ray crystal, structure determinations of H94N, ... [(full description)]
About this StructureAbout this Structure
1H9Q is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Active as [Carbonate dehydratase], with EC number [4.2.1.1]. Structure known Active Site: ZN. Full crystallographic information is available from [OCA].
ReferenceReference
Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity., Lesburg CA, Huang C, Christianson DW, Fierke CA, Biochemistry. 1997 Dec 16;36(50):15780-91. PMID:9398308
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