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1cah

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[[Image:1cah.gif|left|200px]]
[[Image:1cah.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1cah |SIZE=350|CAPTION= <scene name='initialview01'>1cah</scene>, resolution 1.88&Aring;
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The line below this paragraph, containing "STRUCTURE_1cah", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1cah| PDB=1cah | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cah OCA], [http://www.ebi.ac.uk/pdbsum/1cah PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cah RCSB]</span>
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}}
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'''STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE'''
'''STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE'''
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[[Category: Hakansson, K.]]
[[Category: Hakansson, K.]]
[[Category: Wehnert, A.]]
[[Category: Wehnert, A.]]
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[[Category: lyase(oxo-acid)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:31:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:17:52 2008''
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Revision as of 09:31, 2 May 2008

Image:1cah.gif

Template:STRUCTURE 1cah

STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE


Overview

The three-dimensional structure of a complex between catalytically active cobalt(II) substituted human carbonic anhydrase II and its substrate bicarbonate was determined by X-ray crystallography (1.9 A). One water molecule and two bicarbonate oxygen atoms are found at distances between 2.3 and 2.5 A from the cobalt ion in addition to the three histidyl ligands contributed by the peptide chain. The tetrahedral geometry around the metal ion in the native enzyme with a single water molecule 2.0 A from the metal is therefore lost. The geometry is difficult to classify but might best be described as distorted octahedral. The structure is suggested to represent a water-bicarbonate exchange state relevant also for native carbonic anhydrase, where the two unprotonized oxygen atoms of the substrate are bound in a carboxylate binding site and the hydroxyl group is free to move closer to the metal thereby replacing the metal-bound water molecule. A reaction mechanism based on crystallographically determined enzyme-ligand complexes is represented.

About this Structure

1CAH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of cobalt carbonic anhydrase complexed with bicarbonate., Hakansson K, Wehnert A, J Mol Biol. 1992 Dec 20;228(4):1212-8. PMID:1474587 Page seeded by OCA on Fri May 2 12:31:28 2008

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