View source for 5rvw


==PanDDA analysis group deposition -- Crystal Structure of DHTKD1 in complex with Z1587220559==
<StructureSection load='5rvw' size='340' side='right'caption='[[5rvw]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5rvw]] 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=5RVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5RVW 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]] 1.614&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=T1J:2-{[(1H-benzimidazol-2-yl)amino]methyl}phenol'>T1J</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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=5rvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5rvw OCA], [https://pdbe.org/5rvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5rvw RCSB], [https://www.ebi.ac.uk/pdbsum/5rvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5rvw ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/DHTK1_HUMAN DHTK1_HUMAN] 2-aminoadipic 2-oxoadipic aciduria;Autosomal dominant Charcot-Marie-Tooth disease type 2Q. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/DHTK1_HUMAN DHTK1_HUMAN] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Bailey HJ]]
[[Category: Bezerra GA]]
[[Category: Bountra C]]
[[Category: Brandao-Neto J]]
[[Category: Burgess-Brown N]]
[[Category: Douangamath A]]
[[Category: Edwards A]]
[[Category: Foster WR]]
[[Category: Krojer T]]
[[Category: Shrestha L]]
[[Category: Yue WW]]
[[Category: Von Delft F]]