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1ebd
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ebd RCSB], [http://www.ebi.ac.uk/pdbsum/1ebd PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ebd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ebd RCSB], [http://www.ebi.ac.uk/pdbsum/1ebd PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ODP2_BACST ODP2_BACST]] 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 00:12, 25 December 2014
DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE
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