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7y0a
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human short-chain acyl-CoA dehydrogenase== | |
| - | + | <StructureSection load='7y0a' size='340' side='right'caption='[[7y0a]], [[Resolution|resolution]] 2.32Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7y0a]] 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=7Y0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y0A 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]] 2.317Å</td></tr> | |
| - | [[Category: | + | <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>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7y0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y0a OCA], [https://pdbe.org/7y0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y0a RCSB], [https://www.ebi.ac.uk/pdbsum/7y0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y0a ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == 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: Huang Y]] | ||
| + | [[Category: Li J]] | ||
| + | [[Category: Xu Y]] | ||
Current revision
Crystal structure of human short-chain acyl-CoA dehydrogenase
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Categories: Homo sapiens | Large Structures | Huang Y | Li J | Xu Y
