1iyu
From Proteopedia
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==LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE== | ==LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE== | ||
- | <StructureSection load='1iyu' size='340' side='right'caption='[[1iyu | + | <StructureSection load='1iyu' size='340' side='right'caption='[[1iyu]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1iyu]] is a 1 chain structure with sequence from [ | + | <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> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [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]] | ||
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==See Also== | ==See Also== | ||
- | *[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]] | + | *[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
- | [[Category: Dihydrolipoyllysine-residue acetyltransferase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Berg | + | [[Category: Berg A]] |
- | [[Category: Kok | + | [[Category: De Kok A]] |
- | [[Category: Vervoort | + | [[Category: Vervoort J]] |
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Current revision
LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE
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