2vhs

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(New page: 200px<br /><applet load="2vhs" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vhs, resolution 1.50&Aring;" /> '''CATHSILICATEIN, A CH...)
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[[Image:2vhs.jpg|left|200px]]<br /><applet load="2vhs" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2vhs, resolution 1.50&Aring;" />
 
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'''CATHSILICATEIN, A CHIMERA'''<br />
 
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==About this Structure==
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==Cathsilicatein, a chimera==
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2VHS 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Chain+D'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Chain+D'>AC5</scene>, <scene name='pdbsite=AC6:So4+Binding+Site+For+Chain+C'>AC6</scene>, <scene name='pdbsite=AC7:So4+Binding+Site+For+Chain+A'>AC7</scene> and <scene name='pdbsite=AC8:So4+Binding+Site+For+Chain+B'>AC8</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHS OCA].
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<StructureSection load='2vhs' size='340' side='right'caption='[[2vhs]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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[[Category: Homo sapiens]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[2vhs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VHS FirstGlance]. <br>
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[[Category: Naismith, J H.]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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[[Category: SO4]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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[[Category: glycoprotein]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vhs OCA], [https://pdbe.org/2vhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vhs RCSB], [https://www.ebi.ac.uk/pdbsum/2vhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vhs ProSAT]</span></td></tr>
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[[Category: hydrolase]]
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</table>
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[[Category: lysosome]]
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== Function ==
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[[Category: protease]]
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[https://www.uniprot.org/uniprot/CATL1_HUMAN CATL1_HUMAN] Important for the overall degradation of proteins in lysosomes.
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[[Category: silica condensation]]
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== Evolutionary Conservation ==
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[[Category: thiol protease]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: zymogen]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vh/2vhs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2vhs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cathepsin L mutants with the ability to condense silica from solution have been generated and a 1.5 A crystal structure of one of these chimeras allows us to rationalise the catalytic mechanism of silicic acid condensation.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Mar 14 09:35:48 2008''
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Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras.,Fairhead M, Johnson KA, Kowatz T, McMahon SA, Carter LG, Oke M, Liu H, Naismith JH, van der Walle CF Chem Commun (Camb). 2008 Apr 21;(15):1765-7. Epub 2008 Feb 11. PMID:18379686<ref>PMID:18379686</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2vhs" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Carter LG]]
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[[Category: Fairhead M]]
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[[Category: Johnson KA]]
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[[Category: Kowatz T]]
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[[Category: Liu H]]
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[[Category: McMahon SA]]
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[[Category: Naismith JH]]
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[[Category: Oke M]]
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[[Category: Wal CFVD]]

Current revision

Cathsilicatein, a chimera

PDB ID 2vhs

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