1h4n
From Proteopedia
(New page: 200px<br /> <applet load="1h4n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4n, resolution 2.0Å" /> '''H94N CARBONIC ANHYDR...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1H4N 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 and TRS as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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=1H4N OCA]]. | + | 1H4N 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 and TRS 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]]. Structure known Active Site: ZN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4N 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]] | ||
| Line 22: | Line 23: | ||
[[Category: oxo-acid]] | [[Category: oxo-acid]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:42:08 2007'' |
Revision as of 10:37, 30 October 2007
|
H94N CARBONIC ANHYDRASE II COMPLEXED WITH TRIS
Overview
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 Structure
1H4N is a [Single protein] structure of sequence from [Homo sapiens] with ZN and TRS as [ligands]. Active as [Carbonate dehydratase], with EC number [4.2.1.1]. Structure known Active Site: ZN. Full crystallographic information is available from [OCA].
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:9398308
Page seeded by OCA on Tue Oct 30 12:42:08 2007
