1v59: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
(10 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
< | ==Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+== | ||
<StructureSection load='1v59' size='340' side='right'caption='[[1v59]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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'>[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> | |||
== 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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/1v59_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1v59 ConSurf]. | |||
<div style="clear:both"></div> | |||
== | ==See Also== | ||
*[[Dihydrolipoamide dehydrogenase|Dihydrolipoamide dehydrogenase]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Adachi | [[Category: Adachi W]] | ||
[[Category: Reed | [[Category: Reed LJ]] | ||
[[Category: Sekiguchi | [[Category: Sekiguchi T]] | ||
[[Category: Suzuki | [[Category: Suzuki K]] | ||
[[Category: Takenaka | [[Category: Takenaka A]] | ||
[[Category: Tsunoda | [[Category: Tsunoda M]] | ||
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
FunctionDLDH_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 |
|