1ca2
From Proteopedia
(New page: 200px<br /> <applet load="1ca2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ca2, resolution 2.0Å" /> '''REFINED STRUCTURE OF...) |
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| - | [[Image:1ca2.gif|left|200px]]<br /> | + | [[Image:1ca2.gif|left|200px]]<br /><applet load="1ca2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ca2" size=" | + | |
caption="1ca2, resolution 2.0Å" /> | caption="1ca2, resolution 2.0Å" /> | ||
'''REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION'''<br /> | '''REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of human erythrocytic carbonic anhydrase II has been refined | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CA2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 1CA2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1CAC. The following page contains interesting information on the relation of 1CA2 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb49_1.html Carbonic Anhydrase]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CA2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Eriksson, A | + | [[Category: Eriksson, A E.]] |
| - | [[Category: Jones, T | + | [[Category: Jones, T A.]] |
[[Category: Liljas, A.]] | [[Category: Liljas, A.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: lyase(oxo-acid)]] | [[Category: lyase(oxo-acid)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:05 2008'' |
Revision as of 10:04, 21 February 2008
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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
1CA2 is a Single protein structure of sequence from Homo sapiens with as ligand. This structure supersedes the now removed PDB entry 1CAC. The following page contains interesting information on the relation of 1CA2 with [Carbonic Anhydrase]. Active as Carbonate dehydratase, with EC number 4.2.1.1 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
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