1cah
From Proteopedia
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| - | [[Image:1cah.gif|left|200px]] | + | [[Image:1cah.gif|left|200px]] |
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| - | '''STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE''' | + | {{Structure |
| + | |PDB= 1cah |SIZE=350|CAPTION= <scene name='initialview01'>1cah</scene>, resolution 1.88Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> and <scene name='pdbligand=BCT:BICARBONATE ION'>BCT</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CAH is a [ | + | 1CAH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CAH OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of cobalt carbonic anhydrase complexed with bicarbonate., Hakansson K, Wehnert A, J Mol Biol. 1992 Dec 20;228(4):1212-8. PMID:[http:// | + | Structure of cobalt carbonic anhydrase complexed with bicarbonate., Hakansson K, Wehnert A, J Mol Biol. 1992 Dec 20;228(4):1212-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1474587 1474587] |
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: lyase(oxo-acid)]] | [[Category: lyase(oxo-acid)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:21:56 2008'' |
Revision as of 08:22, 20 March 2008
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| , resolution 1.88Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE
Contents |
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.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
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 Thu Mar 20 10:21:56 2008
