2pdd: Difference between revisions

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<StructureSection load='2pdd' size='340' side='right'caption='[[2pdd]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''>
<StructureSection load='2pdd' size='340' side='right'caption='[[2pdd]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pdd]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PDD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PDD FirstGlance]. <br>
<table><tr><td colspan='2'>[[2pdd]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PDD FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pde|2pde]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pde|2pde]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </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=2pdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pdd OCA], [http://pdbe.org/2pdd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pdd RCSB], [http://www.ebi.ac.uk/pdbsum/2pdd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pdd ProSAT]</span></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=2pdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pdd OCA], [https://pdbe.org/2pdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pdd RCSB], [https://www.ebi.ac.uk/pdbsum/2pdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pdd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ODP2_GEOSE ODP2_GEOSE]] 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).  
[[https://www.uniprot.org/uniprot/ODP2_GEOSE ODP2_GEOSE]] 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]]