8sgs: Difference between revisions

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'''Unreleased structure'''


The entry 8sgs is ON HOLD
==human liver mitochondrial Short-chain specific acyl-CoA dehydrogenase==
 
<StructureSection load='8sgs' size='340' side='right'caption='[[8sgs]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
Authors:
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8sgs]] is a 4 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=8SGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SGS FirstGlance]. <br>
Description:  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.15&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <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=8sgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sgs OCA], [https://pdbe.org/8sgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sgs RCSB], [https://www.ebi.ac.uk/pdbsum/8sgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sgs ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ACADS_HUMAN ACADS_HUMAN] Short chain acyl-CoA dehydrogenase deficiency. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/ACADS_HUMAN ACADS_HUMAN] Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains (PubMed:21237683, PubMed:11134486).[UniProtKB:P15651]<ref>PMID:11134486</ref> <ref>PMID:21237683</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Zhang Z]]

Latest revision as of 11:58, 21 February 2024

human liver mitochondrial Short-chain specific acyl-CoA dehydrogenasehuman liver mitochondrial Short-chain specific acyl-CoA dehydrogenase

Structural highlights

8sgs is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ACADS_HUMAN Short chain acyl-CoA dehydrogenase deficiency. The disease is caused by variants affecting the gene represented in this entry.

Function

ACADS_HUMAN Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains (PubMed:21237683, PubMed:11134486).[UniProtKB:P15651][1] [2]

References

  1. ↑ Corydon MJ, Vockley J, Rinaldo P, Rhead WJ, Kjeldsen M, Winter V, Riggs C, Babovic-Vuksanovic D, Smeitink J, De Jong J, Levy H, Sewell AC, Roe C, Matern D, Dasouki M, Gregersen N. Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res. 2001 Jan;49(1):18-23. PMID:11134486 doi:10.1203/00006450-200101000-00008
  2. ↑ He M, Pei Z, Mohsen AW, Watkins P, Murdoch G, Van Veldhoven PP, Ensenauer R, Vockley J. Identification and characterization of new long chain acyl-CoA dehydrogenases. Mol Genet Metab. 2011 Apr;102(4):418-29. PMID:21237683 doi:10.1016/j.ymgme.2010.12.005

8sgs, resolution 3.15Å

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