2cab
From Proteopedia
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|PDB= 2cab |SIZE=350|CAPTION= <scene name='initialview01'>2cab</scene>, resolution 2.0Å | |PDB= 2cab |SIZE=350|CAPTION= <scene name='initialview01'>2cab</scene>, resolution 2.0Å | ||
|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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cab OCA], [http://www.ebi.ac.uk/pdbsum/2cab PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cab RCSB]</span> | ||
}} | }} | ||
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[[Category: Kannan, K K.]] | [[Category: Kannan, K K.]] | ||
[[Category: Ramanadham, M.]] | [[Category: Ramanadham, M.]] | ||
| - | [[Category: ZN]] | ||
[[Category: hydro-lyase]] | [[Category: hydro-lyase]] | ||
| - | ''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 02:18:42 2008'' |
Revision as of 23:18, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I
Overview
The structure of human erythrocyte carbonic anhydrase I has been refined to a final R value of 19% to 2-A resolution by a combination of least squares refinement and model fitting in a three-dimensional graphics display. About 300 solvent atoms have been located bound to the protein molecule. An interesting hydrogen bond network involving Zn2+, the liganded solvent, side chain groups of Thr-199, Glu-106, Thr-7, and His-64 through two solvent molecules have been found that may be important for the catalytic mechanism of the carbonic anhydrase.
About this Structure
2CAB is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1CAB. Full crystallographic information is available from OCA.
Reference
Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I., Kannan KK, Ramanadham M, Jones TA, Ann N Y Acad Sci. 1984;429:49-60. PMID:6430186
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