Sandbox1029

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== Carbonic Anhydrase ==
== Carbonic Anhydrase ==
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This is a placeholder text to help you get started in
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The alpha form of this enzyme, located mainly in red blood cells of animals, catalyzes the interconversion of carbon dioxide and carbonic acid. It is important for transportation and release of carbon dioxide in the blood. This enzyme's <scene name='Sandbox1029/Histidine_residues/1'>active site</scene> contains a zinc cofactor that is held in place by three histidine side chains (His94, His96, His119). The reaction has a two-step mechanism in which there is a zinc-bound hydroxide ion that nucleophilically attacks the carbon dioxide. Following the first step, is the regeneration of the active site by removing a proton and re-ionizing the zinc-bound water molecule. The enzyme also consists of
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placing a Jmol applet on your page. At any time, click
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<scene name='Sandbox1029/Alpha_helix/1'>alpha helices</scene> and <scene name='Sandbox1029/Betabeta2/1'>beta sheets.</scene>
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"Show Preview" at the bottom of this page to see how it goes.
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Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
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<scene name='Sandbox1029/Hydrophobicity/1'>hydrophobic regions</scene>
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and display another structure.
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{{STRUCTURE_1ca2 | PDB=1ca2 | SCENE= }}
{{STRUCTURE_1ca2 | PDB=1ca2 | SCENE= }}
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<scene name='Sandbox1029/Alpha_helix/1'>alpha helices</scene>
 
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<scene name='Sandbox1029/Zinc_ion/1'>zinc ion</scene>
 
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<scene name='Sandbox1029/Betabeta2/1'>beta sheets</scene>
 
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<scene name='Sandbox1029/Hydrophobicity/1'>hydrophobic region</scene>
 
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<scene name='Sandbox1029/Histidine_residues/1'>His 94, 96, 119 and active site</scene>
 

Current revision

This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!

Carbonic Anhydrase

The alpha form of this enzyme, located mainly in red blood cells of animals, catalyzes the interconversion of carbon dioxide and carbonic acid. It is important for transportation and release of carbon dioxide in the blood. This enzyme's contains a zinc cofactor that is held in place by three histidine side chains (His94, His96, His119). The reaction has a two-step mechanism in which there is a zinc-bound hydroxide ion that nucleophilically attacks the carbon dioxide. Following the first step, is the regeneration of the active site by removing a proton and re-ionizing the zinc-bound water molecule. The enzyme also consists of and


PDB ID 1ca2

Drag the structure with the mouse to rotate
1ca2, resolution 2.00Å ()
Ligands:
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


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