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[[Image:2vig.jpg|left|200px]]


{{Structure
==Crystal structure of human short-chain acyl CoA dehydrogenase==
|PDB= 2vig |SIZE=350|CAPTION= <scene name='initialview01'>2vig</scene>, resolution 1.90&Aring;
<StructureSection load='2vig' size='340' side='right'caption='[[2vig]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE= <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>
== Structural highlights ==
|LIGAND= <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>
<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>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</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>
|GENE=
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vig OCA], [http://www.ebi.ac.uk/pdbsum/2vig PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vig RCSB]</span>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/2vig_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF HUMAN SHORT-CHAIN ACYL COA DEHYDROGENASE'''
==See Also==
 
*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
 
== References ==
==About this Structure==
<references/>
2VIG is a [[Single protein]] structure of sequence from [http://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].
__TOC__
[[Category: Butyryl-CoA dehydrogenase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith CH]]
[[Category: Delft, F Von.]]
[[Category: Edwards A]]
[[Category: Edwards, A.]]
[[Category: Gileadi O]]
[[Category: Gileadi, O.]]
[[Category: Oppermann U]]
[[Category: Oppermann, U.]]
[[Category: Pantic N]]
[[Category: Pantic, N.]]
[[Category: Parizotto E]]
[[Category: Parizotto, E.]]
[[Category: Pike ACW]]
[[Category: Pike, A C.W.]]
[[Category: Ugochukwu E]]
[[Category: Ugochukwu, E.]]
[[Category: Weigelt J]]
[[Category: Weigelt, J.]]
[[Category: Von Delft F]]
[[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]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:12:42 2008''