1rzc

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[[Image:1rzc.jpg|left|200px]]<br /><applet load="1rzc" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rzc.jpg|left|200px]]
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caption="1rzc, resolution 1.9&Aring;" />
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'''X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES'''<br />
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{{Structure
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|PDB= 1rzc |SIZE=350|CAPTION= <scene name='initialview01'>1rzc</scene>, resolution 1.9&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=OXY:OXYGEN MOLECULE'>OXY</scene>
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|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]
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|GENE=
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}}
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'''X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RZC 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=CU:'>CU</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1RZC OCA].
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1RZC 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=1RZC OCA].
==Reference==
==Reference==
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X-ray analysis of metal-substituted human carbonic anhydrase II derivatives., Hakansson K, Wehnert A, Liljas A, Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):93-100. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299481 15299481]
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X-ray analysis of metal-substituted human carbonic anhydrase II derivatives., Hakansson K, Wehnert A, Liljas A, Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):93-100. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299481 15299481]
[[Category: Carbonate dehydratase]]
[[Category: Carbonate dehydratase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: lyase(oxo-acid)]]
[[Category: lyase(oxo-acid)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:58:20 2008''

Revision as of 11:58, 20 March 2008


PDB ID 1rzc

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: and
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Coordinates: save as pdb, mmCIF, xml



X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES


Contents

Overview

Metal-substituted crystals of human carbonic anhydrase II belonging to space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and beta = 104.6 degrees were analyzed crystallographically. The resolution limit ranged from 1.82 to 1.92 A with high completeness (86.2-90.7%). Cobalt(II)-substituted carbonic anhydrase has a tetrahedral coordination around the metal both at pH 6 and pH 7.8, similar to the native zinc enzyme. In contrast, the catalytically inactive copper(II), nickel(II) and manganese(II) derivatives showed increased coordination number around the metal ion. Whereas the copper is best described as penta-coordinated, the nickel and manganese are best described as hexa-coordinated. The results are briefly compared with spectroscopic observations and our current view on carbonic anhydrase catalysis.

Disease

Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]

About this Structure

1RZC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

X-ray analysis of metal-substituted human carbonic anhydrase II derivatives., Hakansson K, Wehnert A, Liljas A, Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):93-100. PMID:15299481

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