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2vig

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(New page: 200px<br /><applet load="2vig" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vig, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:2vig.jpg|left|200px]]<br /><applet load="2vig" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2vig, resolution 1.90&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HUMAN SHORT-CHAIN ACYL COA DEHYDROGENASE'''<br />
 
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==About this Structure==
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==Crystal structure of human short-chain acyl CoA dehydrogenase==
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2VIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=COS:'>COS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Butyryl-CoA_dehydrogenase Butyryl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.2 1.3.99.2] Known structural/functional Sites: <scene name='pdbsite=AC1:Fad Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Fad Binding Site For Chain B'>AC2</scene>, <scene name='pdbsite=AC3:Cos Binding Site For Chain B'>AC3</scene>, <scene name='pdbsite=AC4:Fad Binding Site For Chain C'>AC4</scene>, <scene name='pdbsite=AC5:Cos Binding Site For Chain C'>AC5</scene>, <scene name='pdbsite=AC6:Fad Binding Site For Chain D'>AC6</scene>, <scene name='pdbsite=AC7:Cos Binding Site For Chain D'>AC7</scene>, <scene name='pdbsite=AC8:Fad Binding Site For Chain E'>AC8</scene>, <scene name='pdbsite=AC9:Fad Binding Site For Chain F'>AC9</scene>, <scene name='pdbsite=BC1:Cos Binding Site For Chain F'>BC1</scene>, <scene name='pdbsite=BC2:Fad Binding Site For Chain G'>BC2</scene>, <scene name='pdbsite=BC3:Cos Binding Site For Chain G'>BC3</scene>, <scene name='pdbsite=BC4:Fad Binding Site For Chain H'>BC4</scene>, <scene name='pdbsite=BC5:Edo Binding Site For Chain F'>BC5</scene>, <scene name='pdbsite=BC6:Edo Binding Site For Chain D'>BC6</scene>, <scene name='pdbsite=BC7:Edo Binding Site For Chain E'>BC7</scene>, <scene name='pdbsite=BC8:Edo Binding Site For Chain H'>BC8</scene>, <scene name='pdbsite=BC9:Edo Binding Site For Chain B'>BC9</scene>, <scene name='pdbsite=CC1:Edo Binding Site For Chain D'>CC1</scene>, <scene name='pdbsite=CC2:Edo Binding Site For Chain A'>CC2</scene>, <scene name='pdbsite=CC3:Edo Binding Site For Chain E'>CC3</scene>, <scene name='pdbsite=CC4:Edo Binding Site For Chain H'>CC4</scene>, <scene name='pdbsite=CC5:Edo Binding Site For Chain E'>CC5</scene>, <scene name='pdbsite=CC6:Edo Binding Site For Chain F'>CC6</scene> and <scene name='pdbsite=CC7:Edo Binding Site For Chain F'>CC7</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VIG OCA].
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<StructureSection load='2vig' size='340' side='right'caption='[[2vig]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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[[Category: Butyryl-CoA dehydrogenase]]
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== Structural highlights ==
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[[Category: Homo sapiens]]
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<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>
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[[Category: Single protein]]
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</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>
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[[Category: Arrowsmith, C.H.]]
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<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>
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[[Category: Delft, F.Von.]]
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<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>
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[[Category: Edwards, A.]]
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</table>
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[[Category: Gileadi, O.]]
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== Disease ==
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[[Category: Oppermann, U.]]
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[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.
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[[Category: Pantic, N.]]
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== Function ==
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[[Category: Parizotto, E.]]
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[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>
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[[Category: Pike, A.C.W.]]
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== Evolutionary Conservation ==
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[[Category: Ugochukwu, E.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Weigelt, J.]]
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Check<jmol>
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[[Category: COS]]
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<jmolCheckbox>
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[[Category: EDO]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/2vig_consurf.spt"</scriptWhenChecked>
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[[Category: FAD]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: beta oxidation]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: disease mutation]]
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</jmolCheckbox>
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[[Category: fad]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vig ConSurf].
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[[Category: fatty acid metabolism]]
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<div style="clear:both"></div>
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[[Category: flavoprotein]]
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[[Category: lipid metabolism]]
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[[Category: mitochondrion]]
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[[Category: oxidoreductase]]
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[[Category: polymorphism]]
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[[Category: transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:28:41 2008''
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==See Also==
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*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith CH]]
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[[Category: Edwards A]]
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[[Category: Gileadi O]]
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[[Category: Oppermann U]]
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[[Category: Pantic N]]
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[[Category: Parizotto E]]
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[[Category: Pike ACW]]
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[[Category: Ugochukwu E]]
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[[Category: Weigelt J]]
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[[Category: Von Delft F]]

Current revision

Crystal structure of human short-chain acyl CoA dehydrogenase

PDB ID 2vig

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