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1v59
From Proteopedia
(Difference between revisions)
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<StructureSection load='1v59' size='340' side='right'caption='[[1v59]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1v59' size='340' side='right'caption='[[1v59]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1v59]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1v59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V59 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </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=1v59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v59 OCA], [https://pdbe.org/1v59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v59 RCSB], [https://www.ebi.ac.uk/pdbsum/1v59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v59 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/DLDH_YEAST DLDH_YEAST]] Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 06:25, 6 October 2021
Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+
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Categories: Dihydrolipoyl dehydrogenase | Large Structures | Saccharomyces cerevisiae | Adachi, W | Reed, L J | Sekiguchi, T | Suzuki, K | Takenaka, A | Tsunoda, M | 2-oxoacid dehydroganese complex | Dihydrolipoamide dehydrogenase | Lipoamide dehydrogenase | Nad+ | Oxidoreductase | Pyridine nucleotide-disulphide oxidoreductase | Pyruvate dehydrogenase complex
