3bpt

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(New page: 200px<br /><applet load="3bpt" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bpt, resolution 1.50&Aring;" /> '''Crystal structure of...)
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[[Image:3bpt.jpg|left|200px]]<br /><applet load="3bpt" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="3bpt, resolution 1.50&Aring;" />
 
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'''Crystal structure of human beta-hydroxyisobutyryl-CoA hydrolase in complex with quercetin'''<br />
 
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==About this Structure==
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==Crystal structure of human beta-hydroxyisobutyryl-CoA hydrolase in complex with quercetin==
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3BPT 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=QUE:'>QUE</scene> and <scene name='pdbligand=HIU:'>HIU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-hydroxyisobutyryl-CoA_hydrolase 3-hydroxyisobutyryl-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.4 3.1.2.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BPT OCA].
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<StructureSection load='3bpt' size='340' side='right'caption='[[3bpt]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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[[Category: 3-hydroxyisobutyryl-CoA hydrolase]]
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3bpt]] is a 1 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=3BPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BPT FirstGlance]. <br>
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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]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIU:(2R)-3-HYDROXY-2-METHYLPROPANOIC+ACID'>HIU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=QUE:3,5,7,3,4-PENTAHYDROXYFLAVONE'>QUE</scene></td></tr>
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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=3bpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bpt OCA], [https://pdbe.org/3bpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bpt RCSB], [https://www.ebi.ac.uk/pdbsum/3bpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bpt ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/HIBCH_HUMAN HIBCH_HUMAN] Defects in HIBCH are the cause of HIBCH deficiency (HIBCHD) [MIM:[https://omim.org/entry/250620 250620]; also known as deficiency of beta-hydroxyisobutyryl CoA deacylase or methacrylic aciduria. The enzyme defect results in accumulation of methacrylyl-CoA, a highly reactive compound, which readily undergoes addition reactions with free sulfhydryl groups. Affected individuals showed delayed development of motor skills, hypotonia, initial poor feeding, and a deterioration in neurological function during first stages of life.<ref>PMID:17160907</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/HIBCH_HUMAN HIBCH_HUMAN] Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA.<ref>PMID:8824301</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/bp/3bpt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3bpt ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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 AM]]
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[[Category: Edwards, A.M.]]
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[[Category: Guo K]]
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[[Category: Guo, K.]]
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[[Category: King ONF]]
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[[Category: King, O.N.F.]]
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[[Category: Oppermann U]]
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[[Category: Oppermann, U.]]
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[[Category: Phillips C]]
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[[Category: Phillips, C.]]
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[[Category: Pike ACW]]
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[[Category: Pike, A.C.W.]]
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[[Category: Pilka ES]]
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[[Category: Pilka, E.S.]]
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[[Category: Weigelt J]]
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[[Category: SGC, Structural.Genomics.Consortium.]]
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[[Category: Von Delft F]]
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[[Category: Weigelt, J.]]
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[[Category: HIU]]
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[[Category: QUE]]
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[[Category: alternative splicing]]
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[[Category: beta-hydroxyisobutyryl acid]]
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[[Category: branched-chain amino acid catabolism]]
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[[Category: coenzyme a]]
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[[Category: disease mutation]]
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[[Category: hydrolase]]
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[[Category: mitochondrion]]
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[[Category: polymorphism]]
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[[Category: quercetin]]
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[[Category: sgc]]
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[[Category: structural genomics consortium]]
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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 11:16:53 2008''
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Current revision

Crystal structure of human beta-hydroxyisobutyryl-CoA hydrolase in complex with quercetin

PDB ID 3bpt

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