1v59: Difference between revisions

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<StructureSection load='1v59' size='340' side='right'caption='[[1v59]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1v59' size='340' side='right'caption='[[1v59]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1v59]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V59 FirstGlance]. <br>
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></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='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=1v59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v59 OCA], [http://pdbe.org/1v59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v59 RCSB], [http://www.ebi.ac.uk/pdbsum/1v59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v59 ProSAT]</span></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=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 ==
[[http://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.  
[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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dihydrolipoyl dehydrogenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Adachi, W]]
[[Category: Adachi W]]
[[Category: Reed, L J]]
[[Category: Reed LJ]]
[[Category: Sekiguchi, T]]
[[Category: Sekiguchi T]]
[[Category: Suzuki, K]]
[[Category: Suzuki K]]
[[Category: Takenaka, A]]
[[Category: Takenaka A]]
[[Category: Tsunoda, M]]
[[Category: Tsunoda M]]
[[Category: 2-oxoacid dehydroganese complex]]
[[Category: Dihydrolipoamide dehydrogenase]]
[[Category: Lipoamide dehydrogenase]]
[[Category: Nad+]]
[[Category: Oxidoreductase]]
[[Category: Pyridine nucleotide-disulphide oxidoreductase]]
[[Category: Pyruvate dehydrogenase complex]]

Latest revision as of 02:57, 28 December 2023

Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+

Structural highlights

1v59 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1v59, resolution 2.20Å

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