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5t06
From Proteopedia
(Difference between revisions)
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<StructureSection load='5t06' size='340' side='right'caption='[[5t06]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5t06' size='340' side='right'caption='[[5t06]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5t06]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5t06]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T06 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.898Å</td></tr> |
| - | <tr id=' | + | <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=HXC:HEXANOYL-COENZYME+A'>HXC</scene></td></tr> |
| - | < | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t06 OCA], [https://pdbe.org/5t06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t06 RCSB], [https://www.ebi.ac.uk/pdbsum/5t06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t06 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/YBGC_ECOLI YBGC_ECOLI] Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond. |
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli O157:H7]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Anderson | + | [[Category: Anderson WF]] |
| - | + | [[Category: Di Leo R]] | |
| - | [[Category: Leo | + | [[Category: Savchenko A]] |
| - | [[Category: Savchenko | + | [[Category: Skarina T]] |
| - | [[Category: Skarina | + | [[Category: Stogios PJ]] |
| - | [[Category: Stogios | + | [[Category: Watanabe N]] |
| - | [[Category: Watanabe | + | |
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Current revision
Crystal structure of a putative acyl-CoA thioesterase EC709/ECK0725 from Escherichia coli in complex with Hexanoyl-CoA
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