2zu7: Difference between revisions
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==Crystal structure of mannosyl-3-phosphoglycerate synthase from Pyrococcus horikoshii== | ==Crystal structure of mannosyl-3-phosphoglycerate synthase from Pyrococcus horikoshii== | ||
<StructureSection load='2zu7' size='340' side='right' caption='[[2zu7]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2zu7' size='340' side='right'caption='[[2zu7]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zu7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2zu7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZU7 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]] 2.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zu7 OCA], [https://pdbe.org/2zu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zu7 RCSB], [https://www.ebi.ac.uk/pdbsum/2zu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zu7 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/MPGS_PYRHO MPGS_PYRHO] Transfers a mannosyl group from GDP-mannose to phosphoglycerate to form mannosyl-3-phosphoglycerate (MPG). The enzyme is absolutely specific for GDP-mannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration. | ||
== 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/zu/2zu7_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/2zu7_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 23: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Kawamura | [[Category: Kawamura T]] | ||
[[Category: Tanaka | [[Category: Tanaka I]] | ||
[[Category: Watanabe | [[Category: Watanabe N]] | ||
Latest revision as of 11:43, 30 October 2024
Crystal structure of mannosyl-3-phosphoglycerate synthase from Pyrococcus horikoshiiCrystal structure of mannosyl-3-phosphoglycerate synthase from Pyrococcus horikoshii
Structural highlights
FunctionMPGS_PYRHO Transfers a mannosyl group from GDP-mannose to phosphoglycerate to form mannosyl-3-phosphoglycerate (MPG). The enzyme is absolutely specific for GDP-mannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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