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2dnc
From Proteopedia
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==Solution Structure of RSGI RUH-054, a lipoyl domain from human 2-oxoacid dehydrogenase== | ==Solution Structure of RSGI RUH-054, a lipoyl domain from human 2-oxoacid dehydrogenase== | ||
| - | <StructureSection load='2dnc' size='340' side='right' caption='[[2dnc | + | <StructureSection load='2dnc' size='340' side='right'caption='[[2dnc]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2dnc]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2dnc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DNC FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2dnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dnc OCA], [https://pdbe.org/2dnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dnc RCSB], [https://www.ebi.ac.uk/pdbsum/2dnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dnc ProSAT], [https://www.topsan.org/Proteins/RSGI/2dnc TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ODPX_HUMAN ODPX_HUMAN] Defects in PDHX are the cause of pyruvate dehydrogenase E3-binding protein deficiency (PDHXD) [MIM:[https://omim.org/entry/245349 245349].<ref>PMID:9399911</ref> |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ODPX_HUMAN ODPX_HUMAN] Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. |
== 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/dn/2dnc_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dn/2dnc_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> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dnc ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Pyruvate dehydrogenase|Pyruvate dehydrogenase]] | + | *[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Hayashi | + | [[Category: Large Structures]] |
| - | [[Category: Hirota | + | [[Category: Hayashi F]] |
| - | [[Category: Kurosaki | + | [[Category: Hirota H]] |
| - | [[Category: Momen | + | [[Category: Kurosaki C]] |
| - | + | [[Category: Ruhul Momen AZM]] | |
| - | [[Category: Yokoyama | + | [[Category: Yokoyama S]] |
| - | [[Category: Yoshida | + | [[Category: Yoshida M]] |
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Current revision
Solution Structure of RSGI RUH-054, a lipoyl domain from human 2-oxoacid dehydrogenase
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