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2es4
From Proteopedia
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==Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase== | ==Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase== | ||
| - | <StructureSection load='2es4' size='340' side='right' caption='[[2es4]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='2es4' size='340' side='right'caption='[[2es4]], [[Resolution|resolution]] 1.85Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2es4]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2es4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ES4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ES4 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]] 1.85Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=2es4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2es4 OCA], [https://pdbe.org/2es4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2es4 RCSB], [https://www.ebi.ac.uk/pdbsum/2es4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2es4 ProSAT]</span></td></tr> | |
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| - | <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/LIP_BURPL LIP_BURPL] Catalyzes the hydrolysis of triacylglycerol.<ref>PMID:1476423</ref> <ref>PMID:7786905</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/2es4_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/2es4_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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==See Also== | ==See Also== | ||
| - | *[[Lipase|Lipase]] | + | *[[Lipase 3D Structures|Lipase 3D Structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 33617]] | ||
[[Category: Burkholderia glumae]] | [[Category: Burkholderia glumae]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Pauwels K]] | |
| - | [[Category: Pauwels | + | [[Category: Savvides SN]] |
| - | [[Category: Savvides | + | [[Category: Tommassen J]] |
| - | [[Category: Tommassen | + | [[Category: Van Gelder P]] |
| - | [[Category: | + | [[Category: Wyns L]] |
| - | [[Category: | + | |
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Current revision
Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase
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