2vig: Difference between revisions

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<StructureSection load='2vig' size='340' side='right'caption='[[2vig]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2vig' size='340' side='right'caption='[[2vig]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2vig]] is a 8 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=2VIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VIG FirstGlance]. <br>
<table><tr><td colspan='2'>[[2vig]] is a 8 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=2VIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VIG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Short-chain_acyl-CoA_dehydrogenase Short-chain acyl-CoA dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.1 1.3.8.1] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=2vig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vig OCA], [https://pdbe.org/2vig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vig RCSB], [https://www.ebi.ac.uk/pdbsum/2vig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vig ProSAT]</span></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=2vig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vig OCA], [https://pdbe.org/2vig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vig RCSB], [https://www.ebi.ac.uk/pdbsum/2vig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vig ProSAT]</span></td></tr>
</table>
</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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Short-chain acyl-CoA dehydrogenase]]
[[Category: Arrowsmith CH]]
[[Category: Arrowsmith, C H]]
[[Category: Edwards A]]
[[Category: Delft, F von]]
[[Category: Gileadi O]]
[[Category: Edwards, A]]
[[Category: Oppermann U]]
[[Category: Gileadi, O]]
[[Category: Pantic N]]
[[Category: Oppermann, U]]
[[Category: Parizotto E]]
[[Category: Pantic, N]]
[[Category: Pike ACW]]
[[Category: Parizotto, E]]
[[Category: Ugochukwu E]]
[[Category: Pike, A C.W]]
[[Category: Weigelt J]]
[[Category: Ugochukwu, E]]
[[Category: Von Delft F]]
[[Category: Weigelt, J]]
[[Category: Beta oxidation]]
[[Category: Disease mutation]]
[[Category: Fad]]
[[Category: Fatty acid metabolism]]
[[Category: Flavoprotein]]
[[Category: Lipid metabolism]]
[[Category: Mitochondrion]]
[[Category: Oxidoreductase]]
[[Category: Polymorphism]]
[[Category: Transit peptide]]

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