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[[Image:1eaf.png|left|200px]]


{{STRUCTURE_1eaf|  PDB=1eaf  |  SCENE=  }}
==ATOMIC STRUCTURE OF THE CUBIC CORE OF THE PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==
 
<StructureSection load='1eaf' size='340' side='right'caption='[[1eaf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
===ATOMIC STRUCTURE OF THE CUBIC CORE OF THE PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1eaf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EAF FirstGlance]. <br>
 
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
==About this Structure==
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene></td></tr>
[[1eaf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAF OCA].  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eaf OCA], [https://pdbe.org/1eaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eaf RCSB], [https://www.ebi.ac.uk/pdbsum/1eaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eaf ProSAT]</span></td></tr>
 
</table>
==Reference==
== Function ==
<ref group="xtra">PMID:008471601</ref><references group="xtra"/>
[https://www.uniprot.org/uniprot/ODP2_AZOVI ODP2_AZOVI] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/1eaf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1eaf ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
[[Category: Large Structures]]
[[Category: Hol, W G.J.]]
[[Category: Hol WGJ]]
[[Category: Mattevi, A.]]
[[Category: Mattevi A]]
[[Category: Dihydrolipoamide acetyltransferase]]
Retrieved from "https://proteopedia.org/1eaf"