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3de4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Proteinase K by Classical hanging drop method after the first step of high X-Ray dose on ESRF ID23-1 beamline== | |
| + | <StructureSection load='3de4' size='340' side='right'caption='[[3de4]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3de4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DE4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3DE4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d9q|3d9q]], [[3ddz|3ddz]], [[3de0|3de0]], [[3de1|3de1]], [[3de2|3de2]], [[3de3|3de3]], [[3de5|3de5]], [[3de6|3de6]], [[3de7|3de7]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3de4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3de4 OCA], [http://pdbe.org/3de4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3de4 RCSB], [http://www.ebi.ac.uk/pdbsum/3de4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3de4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PRTK_TRIAL PRTK_TRIAL]] Hydrolyzes keratin at aromatic and hydrophobic residues. | ||
| + | == 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/de/3de4_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/main_output.php?pdb_ID=3de4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A detailed analysis of structural and intensity changes induced by X-ray radiation is presented for two types of proteinase K crystals: crystal grown by classical hanging drop method and those grown by Langmuir-Blodgett (LB) nanotemplate. The comparison of various parameters (e.g. intensity per sigma ratio, unit-cell volume, number of unique reflections, B-factors) and electron density maps as a function of radiation dose, demonstrates that crystals, grown by the LB nanotemplate method, appear to be more resistant against radiation damage than crystals grown by the classical hanging drop method. | ||
| - | + | Radiation stability of proteinase K crystals grown by LB nanotemplate method.,Pechkova E, Tripathi S, Ravelli RB, McSweeney S, Nicolini C J Struct Biol. 2009 Dec;168(3):409-18. Epub 2009 Aug 15. PMID:19686853<ref>PMID:19686853</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3de4" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Proteinase|Proteinase]] | ||
| + | *[[Proteinase 3D structures|Proteinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Engyodontium album]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Peptidase K]] | ||
| + | [[Category: Nicolini, C]] | ||
| + | [[Category: Pechkova, E]] | ||
| + | [[Category: Tripathi, S K]] | ||
| + | [[Category: Alpha beta protein]] | ||
| + | [[Category: Calcium]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Protease]] | ||
| + | [[Category: Serine protease]] | ||
| + | [[Category: Zymogen]] | ||
Current revision
Proteinase K by Classical hanging drop method after the first step of high X-Ray dose on ESRF ID23-1 beamline
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