1v9e: Difference between revisions
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'''Crystal Structure Analysis of Bovine Carbonic Anhydrase II''' | {{Structure | ||
|PDB= 1v9e |SIZE=350|CAPTION= <scene name='initialview01'>1v9e</scene>, resolution 1.95Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|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] | |||
|GENE= | |||
}} | |||
'''Crystal Structure Analysis of Bovine Carbonic Anhydrase II''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1V9E is a [ | 1V9E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9E OCA]. | ||
==Reference== | ==Reference== | ||
Structure of bovine carbonic anhydrase II at 1.95 A resolution., Saito R, Sato T, Ikai A, Tanaka N, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):792-5. Epub 2004, Mar 23. PMID:[http:// | Structure of bovine carbonic anhydrase II at 1.95 A resolution., Saito R, Sato T, Ikai A, Tanaka N, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):792-5. Epub 2004, Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15039588 15039588] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
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[[Category: zinc metalloenzyme]] | [[Category: zinc metalloenzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:42:32 2008'' | ||
Revision as of 12:42, 20 March 2008
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| 1v9e, resolution 1.95Å | |||||||||||||
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| Ligands: | ZN | ||||||||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure Analysis of Bovine Carbonic Anhydrase II
Overview
Carbonic anhydrase (CA) is a zinc-containing enzyme that catalyzes the reversible hydration of CO2 to HCO3-. In eukaryotes, the enzyme plays a role in various physiological functions, including interconversion between CO2 and HCO3- in intermediary metabolism, facilitated diffusion of CO2, pH homeostasis and ion transport. The structure of bovine carbonic anhydrase II (BCA II) has been determined by molecular replacement and refined to 1.95 A resolution by simulated-annealing and individual B-factor refinement. The final R factor for the BCA II structure was 19.4%. BCA II has a C-terminal knot structure similar to that observed in human CA II. It contains one zinc ion in the active site coordinated to three histidines and one putative water molecule in a tetrahedral geometry. The structure of BCA II reveals a probable alternative proton-wire pathway that differs from that of HCA II.
About this Structure
1V9E is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structure of bovine carbonic anhydrase II at 1.95 A resolution., Saito R, Sato T, Ikai A, Tanaka N, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):792-5. Epub 2004, Mar 23. PMID:15039588
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