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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]] 2.95Å' scene=''> | <StructureSection load='1v9i' size='340' side='right'caption='[[1v9i]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1v9i]] is a 1 chain structure with sequence from [ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</td></tr> | ||
<tr id=' | <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='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'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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/ | </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: | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ikai | [[Category: Ikai A]] | ||
[[Category: Saito | [[Category: Saito R]] | ||
[[Category: Sato | [[Category: Sato T]] | ||
[[Category: Tanaka | [[Category: Tanaka N]] | ||
Latest revision as of 03:00, 28 December 2023
Crystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase IICrystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase II
Structural highlights
FunctionCAH2_BOVIN Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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