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==Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi-castanospermine== | ==Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi-castanospermine== | ||
<StructureSection load='2wc3' size='340' side='right' caption='[[2wc3]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2wc3' size='340' side='right' caption='[[2wc3]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wc4|2wc4]], [[1w3j|1w3j]], [[2j78|2j78]], [[2j75|2j75]], [[2j7g|2j7g]], [[2jal|2jal]], [[2vrj|2vrj]], [[2j7e|2j7e]], [[2j7h|2j7h]], [[2cbu|2cbu]], [[1oin|1oin]], [[2j7c|2j7c]], [[1oif|1oif]], [[2j79|2j79]], [[2cet|2cet]], [[2j7b|2j7b]], [[1uz1|1uz1]], [[1od0|1od0]], [[2ces|2ces]], [[2j7d|2j7d]], [[2j7f|2j7f]], [[2wbg|2wbg]], [[1oim|1oim]], [[2j77|2j77]], [[2cbv|2cbv]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wc4|2wc4]], [[1w3j|1w3j]], [[2j78|2j78]], [[2j75|2j75]], [[2j7g|2j7g]], [[2jal|2jal]], [[2vrj|2vrj]], [[2j7e|2j7e]], [[2j7h|2j7h]], [[2cbu|2cbu]], [[1oin|1oin]], [[2j7c|2j7c]], [[1oif|1oif]], [[2j79|2j79]], [[2cet|2cet]], [[2j7b|2j7b]], [[1uz1|1uz1]], [[1od0|1od0]], [[2ces|2ces]], [[2j7d|2j7d]], [[2j7f|2j7f]], [[2wbg|2wbg]], [[1oim|1oim]], [[2j77|2j77]], [[2cbv|2cbv]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </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-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </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=2wc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wc3 OCA], [http://pdbe.org/2wc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wc3 RCSB], [http://www.ebi.ac.uk/pdbsum/2wc3 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=2wc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wc3 OCA], [http://pdbe.org/2wc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wc3 RCSB], [http://www.ebi.ac.uk/pdbsum/2wc3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wc3 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/wc/2wc3_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wc/2wc3_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 12:40, 26 September 2018
Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi-castanospermineStructure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi-castanospermine
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSynthesis of a panel of iso(thio)urea-type ring-modified castanospermine analogues bearing a freely mutarotating pseudoanomeric hydroxyl group results in tight-binding beta-glucosidase inhibitors with unusual binding signatures; the presence of an N-octyl substituent imparts a remarkable anomeric selectivity, promoting strong binding of the appropriate beta-anomer by the beta-glucosidase. Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.,Aguilar-Moncayo M, Gloster TM, Turkenburg JP, Garcia-Moreno MI, Ortiz Mellet C, Davies GJ, Garcia Fernandez JM Org Biomol Chem. 2009 Jul 7;7(13):2738-47. Epub 2009 May 22. PMID:19532990[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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