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3lq2

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==E. coli pyruvate dehydrogenase complex E1 E235A mutant with low TDP concentration==
==E. coli pyruvate dehydrogenase complex E1 E235A mutant with low TDP concentration==
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<StructureSection load='3lq2' size='340' side='right' caption='[[3lq2]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
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<StructureSection load='3lq2' size='340' side='right'caption='[[3lq2]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3lq2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LQ2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3lq2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LQ2 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=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2iea|2iea]], [[3lpl|3lpl]], [[3lq4|3lq4]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2iea|2iea]], [[3lpl|3lpl]], [[3lq4|3lq4]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aceE, B0114, ECs0118, Z0124 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aceE, B0114, ECs0118, Z0124 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [https://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lq2 OCA], [http://pdbe.org/3lq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lq2 RCSB], [http://www.ebi.ac.uk/pdbsum/3lq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lq2 ProSAT]</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=3lq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lq2 OCA], [https://pdbe.org/3lq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lq2 RCSB], [https://www.ebi.ac.uk/pdbsum/3lq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lq2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ODP1_ECO57 ODP1_ECO57]] Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2) (By similarity).
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[[https://www.uniprot.org/uniprot/ODP1_ECO57 ODP1_ECO57]] Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2) (By similarity).
== 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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*[[Pyruvate dehydrogenase|Pyruvate dehydrogenase]]
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*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Eco57]]
[[Category: Eco57]]
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[[Category: Large Structures]]
[[Category: Furey, W]]
[[Category: Furey, W]]
[[Category: Glycolysis]]
[[Category: Glycolysis]]

Revision as of 10:24, 4 August 2021

E. coli pyruvate dehydrogenase complex E1 E235A mutant with low TDP concentration

PDB ID 3lq2

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