Sandbox1029: Difference between revisions
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== Carbonic Anhydrase == | == Carbonic Anhydrase == | ||
This is a | 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 | ||
<scene name='Sandbox1029/Alpha_helix/1'>alpha helices</scene> and <scene name='Sandbox1029/Betabeta2/1'>beta sheets.</scene> | |||
<scene name='Sandbox1029/Hydrophobicity/1'>hydrophobic regions</scene> | |||
{{STRUCTURE_1ca2 | PDB=1ca2 | SCENE= }} | {{STRUCTURE_1ca2 | PDB=1ca2 | SCENE= }} | ||
Latest revision as of 23:16, 19 May 2009
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Carbonic AnhydraseCarbonic 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
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1ca2, resolution 2.00Å () | |||||||||
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Ligands: | |||||||||
Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
Coordinates: | save as pdb, mmCIF, xml |