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2jif

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[[Image:2jif.gif|left|200px]]
 
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{{Structure
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==Structure of human short-branched chain acyl-CoA dehydrogenase (ACADSB)==
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|PDB= 2jif |SIZE=350|CAPTION= <scene name='initialview01'>2jif</scene>, resolution 2.00&Aring;
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<StructureSection load='2jif' size='340' side='right'caption='[[2jif]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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<table><tr><td colspan='2'>[[2jif]] 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=2JIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JIF FirstGlance]. <br>
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|ACTIVITY=
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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]] 2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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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}}
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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=2jif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jif OCA], [https://pdbe.org/2jif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jif RCSB], [https://www.ebi.ac.uk/pdbsum/2jif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jif ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ACDSB_HUMAN ACDSB_HUMAN] 2-methylbutyryl-CoA dehydrogenase deficiency. The disease is caused by variants affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/ACDSB_HUMAN ACDSB_HUMAN] Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (PubMed:7698750, PubMed:11013134, PubMed:21430231, PubMed:10832746). Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA (PubMed:7698750, PubMed:11013134, PubMed:21430231, PubMed:10832746). Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway (PubMed:11013134, PubMed:10832746). Can also act on valproyl-CoA, a metabolite of valproic acid, an antiepileptic drug (PubMed:8660691).<ref>PMID:10832746</ref> <ref>PMID:11013134</ref> <ref>PMID:21430231</ref> <ref>PMID:7698750</ref> <ref>PMID:8660691</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/2jif_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2jif ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF HUMAN SHORT-BRANCHED CHAIN ACYL-COA DEHYDROGENASE (ACADSB)'''
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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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==Disease==
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<references/>
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Known disease associated with this structure: 2-methylbutyrylglycinuria OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600301 600301]]
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__TOC__
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</StructureSection>
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==About this Structure==
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2JIF 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=2JIF OCA].
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Arrowsmith CH]]
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[[Category: Delft, F Von.]]
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[[Category: Edwards A]]
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[[Category: Edwards, A.]]
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[[Category: Hozjan V]]
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[[Category: Hozjan, V.]]
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[[Category: Kavanagh KL]]
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[[Category: Kavanagh, K L.]]
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[[Category: Niesen FH]]
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[[Category: Niesen, F H.]]
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[[Category: Oppermann U]]
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[[Category: Oppermann, U.]]
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[[Category: Pike ACW]]
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[[Category: Pike, A C.W.]]
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[[Category: Smee C]]
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[[Category: Smee, C.]]
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[[Category: Sundstrom M]]
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[[Category: Sundstrom, M.]]
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[[Category: Turnbull AP]]
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[[Category: Turnbull, A P.]]
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[[Category: Umeano C]]
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[[Category: Umeano, C.]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J.]]
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[[Category: Von Delft F]]
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[[Category: CL]]
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[[Category: COS]]
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[[Category: EDO]]
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[[Category: FAD]]
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[[Category: acetylation]]
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[[Category: disease mutation]]
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[[Category: fad]]
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[[Category: fatty acid metabolism]]
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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 Thu Mar 20 17:42:18 2008''
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Current revision

Structure of human short-branched chain acyl-CoA dehydrogenase (ACADSB)

PDB ID 2jif

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