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==Crystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase II==
==Crystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase II==
<StructureSection load='1v9i' size='340' side='right' caption='[[1v9i]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
<StructureSection load='1v9i' size='340' side='right'caption='[[1v9i]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1v9i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V9I FirstGlance]. <br>
<table><tr><td colspan='2'>[[1v9i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V9I FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v9e|1v9e]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9i OCA], [https://pdbe.org/1v9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v9i RCSB], [https://www.ebi.ac.uk/pdbsum/1v9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v9i ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v9i RCSB], [http://www.ebi.ac.uk/pdbsum/1v9i PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CAH2_BOVIN CAH2_BOVIN]] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide.  
[https://www.uniprot.org/uniprot/CAH2_BOVIN CAH2_BOVIN] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v9/1v9i_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v9/1v9i_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v9i ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Carbonic anhydrase|Carbonic anhydrase]]
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Carbonate dehydratase]]
[[Category: Large Structures]]
[[Category: Ikai, A]]
[[Category: Ikai A]]
[[Category: Saito, R]]
[[Category: Saito R]]
[[Category: Sato, T]]
[[Category: Sato T]]
[[Category: Tanaka, N]]
[[Category: Tanaka N]]
[[Category: Beta sheet]]
[[Category: Lyase]]
[[Category: Zinc metalloenzyme]]

Latest revision as of 00:00, 28 December 2023

Crystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase II

1v9i, resolution 2.95Å

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