2wtx
From Proteopedia
(Difference between revisions)
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| - | == | + | |
| + | ==Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase== | ||
<StructureSection load='2wtx' size='340' side='right' caption='[[2wtx]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2wtx' size='340' side='right' caption='[[2wtx]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gz5|1gz5]], [[1uqu|1uqu]], [[1uqt|1uqt]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gz5|1gz5]], [[1uqu|1uqu]], [[1uqt|1uqt]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha,alpha-trehalose-phosphate_synthase_(UDP-forming) Alpha,alpha-trehalose-phosphate synthase (UDP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.15 2.4.1.15] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha,alpha-trehalose-phosphate_synthase_(UDP-forming) Alpha,alpha-trehalose-phosphate synthase (UDP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.15 2.4.1.15] </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=2wtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wtx OCA], [http://pdbe.org/2wtx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wtx RCSB], [http://www.ebi.ac.uk/pdbsum/2wtx 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=2wtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wtx OCA], [http://pdbe.org/2wtx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wtx RCSB], [http://www.ebi.ac.uk/pdbsum/2wtx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wtx ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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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/wt/2wtx_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wt/2wtx_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> | ||
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[[Category: Lee, S S]] | [[Category: Lee, S S]] | ||
[[Category: Martinez-Fleites, C]] | [[Category: Martinez-Fleites, C]] | ||
| - | [[Category: | + | [[Category: OSullivan, A]] |
[[Category: Glycosyltransferase]] | [[Category: Glycosyltransferase]] | ||
[[Category: Potassium]] | [[Category: Potassium]] | ||
Revision as of 09:10, 26 September 2018
Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase
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