1w88

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==The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit binding domain of E2==
==The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit binding domain of E2==
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<StructureSection load='1w88' size='340' side='right' caption='[[1w88]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='1w88' size='340' side='right'caption='[[1w88]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1w88]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W88 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W88 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1w88]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W88 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b5s|1b5s]], [[1ebd|1ebd]], [[1lab|1lab]], [[1lac|1lac]], [[1w3d|1w3d]], [[1w4e|1w4e]], [[1w4f|1w4f]], [[1w4g|1w4g]], [[1w4h|1w4h]], [[1w85|1w85]], [[2pdd|2pdd]], [[2pde|2pde]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w88 OCA], [https://pdbe.org/1w88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w88 RCSB], [https://www.ebi.ac.uk/pdbsum/1w88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w88 ProSAT]</span></td></tr>
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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=1w88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w88 OCA], [http://pdbe.org/1w88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w88 RCSB], [http://www.ebi.ac.uk/pdbsum/1w88 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w88 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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). [[http://www.uniprot.org/uniprot/ODPB_GEOSE ODPB_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).
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[https://www.uniprot.org/uniprot/ODPB_GEOSE ODPB_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]]
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==See Also==
==See Also==
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*[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]]
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*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
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*[[Pyruvate dehydrogenase|Pyruvate dehydrogenase]]
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*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 12980]]
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[[Category: Geobacillus stearothermophilus]]
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[[Category: Frank, R A.W]]
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[[Category: Large Structures]]
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[[Category: Luisi, B F]]
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[[Category: Frank RAW]]
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[[Category: Pei, X Y]]
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[[Category: Luisi BF]]
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[[Category: Perham, R N]]
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[[Category: Pei XY]]
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[[Category: Pratap, J V]]
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[[Category: Perham RN]]
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[[Category: Acetyl transferase]]
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[[Category: Pratap JV]]
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[[Category: Catalysis]]
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[[Category: Dihydrolipoyl]]
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[[Category: Multienzyme complex]]
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[[Category: Oxidoreductase]]
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[[Category: Pyruvate dehydrogenase]]
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[[Category: Slinky]]
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[[Category: Transferase]]
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Current revision

The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit binding domain of E2

PDB ID 1w88

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OCA

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