1can

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[[Image:1can.gif|left|200px]]<br /><applet load="1can" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1can.gif|left|200px]]
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caption="1can, resolution 1.9&Aring;" />
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'''CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS'''<br />
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{{Structure
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|PDB= 1can |SIZE=350|CAPTION= <scene name='initialview01'>1can</scene>, resolution 1.9&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</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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'''CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1CAN 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=HG:'>HG</scene>, <scene name='pdbligand=NO3:'>NO3</scene> and <scene name='pdbligand=ACE:'>ACE</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=1CAN OCA].
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1CAN 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=1CAN OCA].
==Reference==
==Reference==
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Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions., Mangani S, Hakansson K, Eur J Biochem. 1992 Dec 15;210(3):867-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1336460 1336460]
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Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions., Mangani S, Hakansson K, Eur J Biochem. 1992 Dec 15;210(3):867-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1336460 1336460]
[[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 12:04:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:21:59 2008''

Revision as of 08:22, 20 March 2008

Image:1can.gif


PDB ID 1can

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



CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS


Contents

Overview

The structures of human carbonic-anhydrase-II complexes with the anionic inhibitors hydrogen sulphide (HS-) and nitrate (NO3-) have been determined by X-ray diffraction at 0.19-nm resolution from crystals soaked at pH 7.8 and 6.0, respectively. The modes of binding of these two anions differ markedly from each other. The strong inhibitor HS- replaces the native zinc-bound water/hydroxide (Wat263) leaving the tetrahedral metal geometry unaltered and acts as a hydrogen-bonding donor towards Thr199 gamma. The weak NO3- inhibitor does not displace Wat263 from the metal coordination but occupies a fifth binding site changing the zinc coordination polyhedron into a slightly distorted trigonal bipyramid. The interaction of NO3- with the metal is weak; the nearest of its oxygen atoms being at a distance of 0.28 nm from the zinc ion. The binding of nitrate to the enzyme is completed by a hydrogen bond to the metal coordinated Wat263 and a second one to a water molecule of the active-site cavity. The structures of the two complexes help to rationalize the binding of anionic inhibitors to carbonic anhydrase and the binding mode displayed by NO39 may be relevant to the catalytic mechanism.

Disease

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

About this Structure

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

Reference

Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions., Mangani S, Hakansson K, Eur J Biochem. 1992 Dec 15;210(3):867-71. PMID:1336460

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