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==PanDDA analysis group deposition -- Crystal Structure of DHTKD1 in complex with Z1587220559== | ==PanDDA analysis group deposition -- Crystal Structure of DHTKD1 in complex with Z1587220559== | ||
<StructureSection load='5rvw' size='340' side='right'caption='[[5rvw]]' scene=''> | <StructureSection load='5rvw' size='340' side='right'caption='[[5rvw]], [[Resolution|resolution]] 1.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>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 [ | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.614Å</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> | </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). | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arrowsmith CH]] | [[Category: Arrowsmith CH]] | ||
Latest revision as of 17:08, 6 March 2024
PanDDA analysis group deposition -- Crystal Structure of DHTKD1 in complex with Z1587220559PanDDA analysis group deposition -- Crystal Structure of DHTKD1 in complex with Z1587220559
Structural highlights
DiseaseDHTK1_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. FunctionDHTK1_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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