5nhg

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'''Unreleased structure'''
 
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The entry 5nhg is ON HOLD until Paper Publication
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==Crystal structure of the human dihydrolipoamide dehydrogenase==
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<StructureSection load='5nhg' size='340' side='right' caption='[[5nhg]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
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Authors: Szabo, E., Mizsei, R., Wilk, P., Zambo, Z., Torocsik, B., Weiss, M.S., Adam-Vizi, V., Ambrus, A.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5nhg]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NHG FirstGlance]. <br>
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Description: Crystal structure of the human dihydrolipoamide dehydrogenase
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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[[Category: Unreleased Structures]]
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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/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>
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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=5nhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nhg OCA], [http://pdbe.org/5nhg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nhg RCSB], [http://www.ebi.ac.uk/pdbsum/5nhg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nhg ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/DLDH_HUMAN DLDH_HUMAN]] Note=Defects in DLD are involved in the development of congenital infantile lactic acidosis. Defects in DLD are a cause of maple syrup urine disease (MSUD) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is characterized by mental and physical retardation, feeding problems and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine, resulting from a block in oxidative decarboxylation.
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== Function ==
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[[http://www.uniprot.org/uniprot/DLDH_HUMAN DLDH_HUMAN]] Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.
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__TOC__
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</StructureSection>
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[[Category: Dihydrolipoyl dehydrogenase]]
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[[Category: Adam-Vizi, V]]
[[Category: Ambrus, A]]
[[Category: Ambrus, A]]
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[[Category: Zambo, Z]]
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[[Category: Mizsei, R]]
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[[Category: Wilk, P]]
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[[Category: Adam-Vizi, V]]
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[[Category: Szabo, E]]
[[Category: Szabo, E]]
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[[Category: Mizsei, R]]
 
[[Category: Torocsik, B]]
[[Category: Torocsik, B]]
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[[Category: Weiss, M.S]]
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[[Category: Weiss, M S]]
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[[Category: Wilk, P]]
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[[Category: Zambo, Z]]
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[[Category: Alpha-ketoglutarate dehydrogenase complex]]
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[[Category: Dihydrolipoamide dehydrogenase]]
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[[Category: E3 subunit]]
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[[Category: Oxidoreductase]]
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[[Category: Pyruvate dehydrogenase complex]]

Revision as of 05:19, 16 May 2018

Crystal structure of the human dihydrolipoamide dehydrogenase

5nhg, resolution 2.27Å

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