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2qq2

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==Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7==
==Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7==
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<StructureSection load='2qq2' size='340' side='right' caption='[[2qq2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='2qq2' size='340' side='right'caption='[[2qq2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2qq2]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QQ2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2qq2]] is a 12 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=2QQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QQ2 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACOT7, BACH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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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]] 2.8&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Palmitoyl-CoA_hydrolase Palmitoyl-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.2 3.1.2.2] </span></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=2qq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qq2 OCA], [https://pdbe.org/2qq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qq2 RCSB], [https://www.ebi.ac.uk/pdbsum/2qq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qq2 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qq2 OCA], [http://pdbe.org/2qq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qq2 RCSB], [http://www.ebi.ac.uk/pdbsum/2qq2 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BACH_HUMAN BACH_HUMAN]] Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.
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[https://www.uniprot.org/uniprot/BACH_HUMAN BACH_HUMAN] Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qq/2qq2_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qq/2qq2_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
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*[[Thioesterase|Thioesterase]]
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*[[Thioesterase 3D structures|Thioesterase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Palmitoyl-CoA hydrolase]]
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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: Berg, S van den]]
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[[Category: Berglund H]]
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[[Category: Berglund, H]]
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[[Category: Busam R]]
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[[Category: Busam, R]]
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[[Category: Collins R]]
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[[Category: Collins, R]]
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[[Category: Dahlgren LG]]
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[[Category: Dahlgren, L G]]
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[[Category: Edwards A]]
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[[Category: Edwards, A]]
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[[Category: Flodin S]]
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[[Category: Flodin, S]]
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[[Category: Flores A]]
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[[Category: Flores, A]]
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[[Category: Graslund S]]
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[[Category: Graslund, S]]
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[[Category: Hallberg BM]]
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[[Category: Hallberg, B M]]
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[[Category: Hammarstrom M]]
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[[Category: Hammarstrom, M]]
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[[Category: Herman MD]]
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[[Category: Herman, M D]]
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[[Category: Holmberg-Schiavone L]]
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[[Category: Holmberg-Schiavone, L]]
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[[Category: Johansson I]]
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[[Category: Johansson, I]]
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[[Category: Kallas A]]
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[[Category: Kallas, A]]
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[[Category: Karlberg T]]
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[[Category: Karlberg, T]]
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[[Category: Kotenyova T]]
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[[Category: Kotenyova, T]]
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[[Category: Lehtio L]]
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[[Category: Lehtio, L]]
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[[Category: Moche M]]
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[[Category: Moche, M]]
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[[Category: Nordlund P]]
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[[Category: Nordlund, P]]
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[[Category: Nyman T]]
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[[Category: Nyman, T]]
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[[Category: Persson C]]
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[[Category: Persson, C]]
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[[Category: Sagemark J]]
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[[Category: Structural genomic]]
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[[Category: Stenmark P]]
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[[Category: Sagemark, J]]
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[[Category: Sundstrom M]]
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[[Category: Stenmark, P]]
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[[Category: Thorsell AG]]
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[[Category: Sundstrom, M]]
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[[Category: Tresaugues L]]
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[[Category: Thorsell, A G]]
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[[Category: Weigelt J]]
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[[Category: Tresaugues, L]]
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[[Category: Welin M]]
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[[Category: Weigelt, J]]
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[[Category: Van den Berg S]]
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[[Category: Welin, M]]
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[[Category: Acot7]]
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[[Category: C-terminal domain]]
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[[Category: Hydrolase]]
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[[Category: Mitochondrion]]
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[[Category: Serine esterase]]
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[[Category: Sgc]]
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[[Category: Thioesterase]]
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Current revision

Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7

PDB ID 2qq2

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