5cac
From Proteopedia
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| - | [[Image:5cac.gif|left|200px]] | + | [[Image:5cac.gif|left|200px]] |
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| - | '''REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 5cac |SIZE=350|CAPTION= <scene name='initialview01'>5cac</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=SO3:SULFITE ION'>SO3</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= | ||
| + | }} | ||
| + | |||
| + | '''REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 5CAC is a [ | + | 5CAC 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=5CAC OCA]. |
==Reference== | ==Reference== | ||
| - | Refined structure of human carbonic anhydrase II at 2.0 A resolution., Eriksson AE, Jones TA, Liljas A, Proteins. 1988;4(4):274-82. PMID:[http:// | + | Refined structure of human carbonic anhydrase II at 2.0 A resolution., Eriksson AE, Jones TA, Liljas A, Proteins. 1988;4(4):274-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3151019 3151019] |
[[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 19:11:40 2008'' |
Revision as of 17:11, 20 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION
Contents |
Overview
The structure of human erythrocytic carbonic anhydrase II has been refined by constrained and restrained structure-factor least-squares refinement at 2.0 A resolution. The conventional crystallographic R value is 17.3%. Of 167 solvent molecules associated with the protein, four are buried and stabilize secondary structure elements. The zinc ion is ligated to three histidyl residues and one water molecule in a nearly tetrahedral geometry. In addition to the zinc-bound water, seven more water molecules are identified in the active site. Assuming that Glu-106 is deprotonated at pH 8.5, some of the hydrogen bond donor-acceptor relations in the active site can be assigned and are described here in detail. The O gamma 1 atom of Thr-199 donates its proton to the O epsilon 1 atom of Glu-106 and can function as a hydrogen bond acceptor only in additional hydrogen bonds.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
5CAC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Refined structure of human carbonic anhydrase II at 2.0 A resolution., Eriksson AE, Jones TA, Liljas A, Proteins. 1988;4(4):274-82. PMID:3151019
Page seeded by OCA on Thu Mar 20 19:11:40 2008
