2vhs
From Proteopedia
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- | [[ | + | ==CATHSILICATEIN, A CHIMERA== |
+ | <StructureSection load='2vhs' size='340' side='right' caption='[[2vhs]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2vhs]] is a 4 chain structure with 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=2VHS OCA]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vhs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vhs RCSB], [http://www.ebi.ac.uk/pdbsum/2vhs PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vh/2vhs_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </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]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Carter, L G.]] | [[Category: Carter, L G.]] |
Revision as of 08:36, 7 May 2014
CATHSILICATEIN, A CHIMERA
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Categories: Homo sapiens | Carter, L G. | Fairhead, M. | Johnson, K A. | Kowatz, T. | Liu, H. | Mcmahon, S A. | Naismith, J H. | Oke, M. | Wal, C F.V D. | Glycoprotein | Hydrolase | Lysosome | Protease | Silica condensation | Thiol protease | Zymogen