6sy1
From Proteopedia
(Difference between revisions)
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<StructureSection load='6sy1' size='340' side='right'caption='[[6sy1]], [[Resolution|resolution]] 1.87Å' scene=''> | <StructureSection load='6sy1' size='340' side='right'caption='[[6sy1]], [[Resolution|resolution]] 1.87Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6sy1]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6sy1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SY1 FirstGlance]. <br> |
</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=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | </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=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | ||
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DHTKD1, KIAA1630 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DHTKD1, KIAA1630 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxoglutarate_dehydrogenase_(succinyl-transferring) Oxoglutarate dehydrogenase (succinyl-transferring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.2 1.2.4.2] </span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6sy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sy1 OCA], [https://pdbe.org/6sy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sy1 RCSB], [https://www.ebi.ac.uk/pdbsum/6sy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sy1 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == 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 == | == 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). |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Revision as of 10:27, 4 August 2021
Crystal structure of the human 2-oxoadipate dehydrogenase DHTKD1 (E1)
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Categories: Human | Large Structures | Arrowsmith, C | Bezerra, G A | Bountra, C | Coker, J | Delft, F von | Edwards, A | Foster, W | Kolker, S | Nicola, B B | Pena, I A | Structural genomic | Shrestha, L | Yue, W W | Dehydrogenase | Mg | Sgc | Thiamine pyrophosphate | Transketolase