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3dva
From Proteopedia
(Difference between revisions)
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==Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex== | ==Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex== | ||
| - | <StructureSection load='3dva' size='340' side='right' caption='[[3dva]], [[Resolution|resolution]] 2.35Å' scene=''> | + | <StructureSection load='3dva' size='340' side='right'caption='[[3dva]], [[Resolution|resolution]] 2.35Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3dva]] is a 10 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3dva]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DVA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPW:2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-3-METHYLTHIOPHEN-2-YL}ETHYL+TRIHYDROGEN+DIPHOSPHATE'>TPW</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPW:2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-3-METHYLTHIOPHEN-2-YL}ETHYL+TRIHYDROGEN+DIPHOSPHATE'>TPW</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w85|1w85]], [[1w88|1w88]], [[3duf|3duf]], [[3dv0|3dv0]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w85|1w85]], [[1w88|1w88]], [[3duf|3duf]], [[3dv0|3dv0]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pdhA ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pdhA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980]), pdhB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980]), pdhC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dva OCA], [https://pdbe.org/3dva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dva RCSB], [https://www.ebi.ac.uk/pdbsum/3dva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dva ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[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). [[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== | ||
*[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]] | *[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]] | ||
| - | *[[Pyruvate dehydrogenase|Pyruvate dehydrogenase]] | + | *[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Atcc 12980]] |
| + | [[Category: Large Structures]] | ||
[[Category: Frank, R A.W]] | [[Category: Frank, R A.W]] | ||
[[Category: Leeper, F J]] | [[Category: Leeper, F J]] | ||
Revision as of 19:30, 20 October 2021
Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex
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Categories: Atcc 12980 | Large Structures | Frank, R A.W | Leeper, F J | Luisi, B F | Pei, X Y | Titman, C M | Acetyl transferase | Acyltransferase | Dehydrogenase | Dihydrolipoyl | Glycolysis | Multienzyme complex | Oxidoreductase | Oxidoreductase-transferase complex | Phosphoprotein | Pyruvate | Thiamine pyrophosphate | Transferase

