1v9e
From Proteopedia
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|PDB= 1v9e |SIZE=350|CAPTION= <scene name='initialview01'>1v9e</scene>, resolution 1.95Å | |PDB= 1v9e |SIZE=350|CAPTION= <scene name='initialview01'>1v9e</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1v9i|1V9I]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9e OCA], [http://www.ebi.ac.uk/pdbsum/1v9e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v9e RCSB]</span> | ||
}} | }} | ||
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[[Category: Sato, T.]] | [[Category: Sato, T.]] | ||
[[Category: Tanaka, N.]] | [[Category: Tanaka, N.]] | ||
| - | [[Category: ZN]] | ||
[[Category: high-resolution]] | [[Category: high-resolution]] | ||
[[Category: twisted beta sheet]] | [[Category: twisted beta sheet]] | ||
[[Category: zinc metalloenzyme]] | [[Category: zinc metalloenzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:21:15 2008'' |
Revision as of 21:21, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
| Related: | 1V9I
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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