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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== | ==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 == | ||
| - | <table><tr><td colspan='2'>[[2wtx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WTX OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[2wtx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WTX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WTX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=VDO:[(1R,2R,3S,4S,5S)-2,3,4-TRIHYDROXY-5-{[(1S,4R,5S,6S)-4,5,6-TRIHYDROXY-3-(HYDROXYMETHYL)CYCLOHEX-2-EN-1-YL]AMINO}CYCLOHEXYL]METHYL+DIHYDROGEN+PHOSPHATE'>VDO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=VDO:[(1R,2R,3S,4S,5S)-2,3,4-TRIHYDROXY-5-{[(1S,4R,5S,6S)-4,5,6-TRIHYDROXY-3-(HYDROXYMETHYL)CYCLOHEX-2-EN-1-YL]AMINO}CYCLOHEXYL]METHYL+DIHYDROGEN+PHOSPHATE'>VDO</scene></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='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:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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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</StructureSection> | </StructureSection> | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Barry, C S]] | [[Category: Barry, C S]] | ||
[[Category: Davies, G J]] | [[Category: Davies, G J]] | ||
Revision as of 09:10, 1 July 2020
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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