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2wbk
From Proteopedia
(Difference between revisions)
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==Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis== | ==Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis== | ||
<StructureSection load='2wbk' size='340' side='right' caption='[[2wbk]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2wbk' size='340' side='right' caption='[[2wbk]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vqt|2vqt]], [[2vot|2vot]], [[2vl4|2vl4]], [[2vqu|2vqu]], [[2vo5|2vo5]], [[2je8|2je8]], [[2vr4|2vr4]], [[2vjx|2vjx]], [[2vmf|2vmf]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vqt|2vqt]], [[2vot|2vot]], [[2vl4|2vl4]], [[2vqu|2vqu]], [[2vo5|2vo5]], [[2je8|2je8]], [[2vr4|2vr4]], [[2vjx|2vjx]], [[2vmf|2vmf]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-mannosidase Beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.25 3.2.1.25] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-mannosidase Beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.25 3.2.1.25] </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=2wbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wbk OCA], [http://pdbe.org/2wbk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wbk RCSB], [http://www.ebi.ac.uk/pdbsum/2wbk PDBsum]</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=2wbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wbk OCA], [http://pdbe.org/2wbk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wbk RCSB], [http://www.ebi.ac.uk/pdbsum/2wbk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wbk ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wb/2wbk_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wb/2wbk_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> | ||
Revision as of 09:02, 26 September 2018
Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis
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