1iyu

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==LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE==
==LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE==
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<StructureSection load='1iyu' size='340' side='right' caption='[[1iyu]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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<StructureSection load='1iyu' size='340' side='right'caption='[[1iyu]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1iyu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IYU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1iyu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IYU FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iyv|1iyv]]</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">Solution NMR</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/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </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=1iyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyu OCA], [https://pdbe.org/1iyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iyu RCSB], [https://www.ebi.ac.uk/pdbsum/1iyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyu 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=1iyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iyu RCSB], [http://www.ebi.ac.uk/pdbsum/1iyu PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ODP2_AZOVI ODP2_AZOVI]] 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/ODP2_AZOVI ODP2_AZOVI] 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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/1iyu_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/1iyu_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iyu ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 1iyu" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]]
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*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
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[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
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[[Category: Large Structures]]
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[[Category: Berg, A]]
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[[Category: Berg A]]
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[[Category: Kok, A De]]
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[[Category: De Kok A]]
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[[Category: Vervoort, J]]
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[[Category: Vervoort J]]
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[[Category: Acyltransferase]]
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[[Category: Glycolysis]]
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[[Category: Lipoyl]]
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[[Category: Transferase]]
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Current revision

LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE

PDB ID 1iyu

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