View source for 8phf


==Cryo-EM structure of human ACAD9-S191A==
<StructureSection load='8phf' size='340' side='right'caption='[[8phf]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8phf]] 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=8PHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PHF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=8phf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8phf OCA], [https://pdbe.org/8phf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8phf RCSB], [https://www.ebi.ac.uk/pdbsum/8phf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8phf ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ACAD9_HUMAN ACAD9_HUMAN] Acyl-CoA dehydrogenase 9 deficiency. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/ACAD9_HUMAN ACAD9_HUMAN] As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation (PubMed:20816094, PubMed:24158852, PubMed:32320651). This moonlighting protein has also a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs (PubMed:12359260, PubMed:16020546, PubMed:21237683, PubMed:24158852). However, in vivo, it does not seem to play a primary role in fatty acid oxidation (PubMed:20816094, PubMed:24158852). In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein (PubMed:24158852).<ref>PMID:12359260</ref> <ref>PMID:16020546</ref> <ref>PMID:20816094</ref> <ref>PMID:21237683</ref> <ref>PMID:24158852</ref> <ref>PMID:32320651</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Acajjaoui S]]
[[Category: Bacia-Verloop M]]
[[Category: Bowler MW]]
[[Category: Desfosses A]]
[[Category: Gutsche I]]
[[Category: Juyoux P]]
[[Category: Kandiah E]]
[[Category: McCarthy A]]
[[Category: McGregor L]]
[[Category: Saidi M]]
[[Category: Schwarz JJ]]
[[Category: Soler-Lopez M]]
[[Category: Von Velsen J]]