7zyt
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the I318T pathogenic variant of the human dihydrolipoamide dehydrogenase== | |
| - | + | <StructureSection load='7zyt' size='340' side='right'caption='[[7zyt]], [[Resolution|resolution]] 2.89Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7zyt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZYT FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zyt OCA], [https://pdbe.org/7zyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zyt RCSB], [https://www.ebi.ac.uk/pdbsum/7zyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zyt ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Disease == | ||
| + | [https://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:[https://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. | ||
| + | == Function == | ||
| + | [https://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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Adam-Vizi V]] | ||
| + | [[Category: Ambrus A]] | ||
| + | [[Category: Lennartz F]] | ||
| + | [[Category: Nagy B]] | ||
| + | [[Category: Nemes-Nikodem E]] | ||
| + | [[Category: Szabo E]] | ||
| + | [[Category: Torocsik B]] | ||
| + | [[Category: Vass KR]] | ||
| + | [[Category: Weiss MS]] | ||
Revision as of 08:13, 14 June 2023
Crystal structure of the I318T pathogenic variant of the human dihydrolipoamide dehydrogenase
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Categories: Homo sapiens | Large Structures | Adam-Vizi V | Ambrus A | Lennartz F | Nagy B | Nemes-Nikodem E | Szabo E | Torocsik B | Vass KR | Weiss MS
