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[[Image:2qq2.png|left|200px]]


{{STRUCTURE_2qq2|  PDB=2qq2  |  SCENE=  }}
==Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7==
 
<StructureSection load='2qq2' size='340' side='right'caption='[[2qq2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
===Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7===
== Structural highlights ==
 
<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>
 
</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>
==About this Structure==
<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>
[[2qq2]] is a 12 chain structure of [[Thioesterase]] with 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=2QQ2 OCA].  
</table>
== Function ==
[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 ==
[[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/qq/2qq2_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=2qq2 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Thioesterase|Thioesterase]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Palmitoyl-CoA hydrolase]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith CH]]
[[Category: Berg, S van den.]]
[[Category: Berglund H]]
[[Category: Berglund, H.]]
[[Category: Busam R]]
[[Category: Busam, R.]]
[[Category: Collins R]]
[[Category: Collins, R.]]
[[Category: Dahlgren LG]]
[[Category: Dahlgren, L G.]]
[[Category: Edwards A]]
[[Category: Edwards, A.]]
[[Category: Flodin S]]
[[Category: Flodin, S.]]
[[Category: Flores A]]
[[Category: Flores, A.]]
[[Category: Graslund S]]
[[Category: Graslund, S.]]
[[Category: Hallberg BM]]
[[Category: Hallberg, B M.]]
[[Category: Hammarstrom M]]
[[Category: Hammarstrom, M.]]
[[Category: Herman MD]]
[[Category: Herman, M D.]]
[[Category: Holmberg-Schiavone L]]
[[Category: Holmberg-Schiavone, L.]]
[[Category: Johansson I]]
[[Category: Johansson, I.]]
[[Category: Kallas A]]
[[Category: Kallas, A.]]
[[Category: Karlberg T]]
[[Category: Karlberg, T.]]
[[Category: Kotenyova T]]
[[Category: Kotenyova, T.]]
[[Category: Lehtio L]]
[[Category: Lehtio, L.]]
[[Category: Moche M]]
[[Category: Moche, M.]]
[[Category: Nordlund P]]
[[Category: Nordlund, P.]]
[[Category: Nyman T]]
[[Category: Nyman, T.]]
[[Category: Persson C]]
[[Category: Persson, C.]]
[[Category: Sagemark J]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Stenmark P]]
[[Category: Sagemark, J.]]
[[Category: Sundstrom M]]
[[Category: Stenmark, P.]]
[[Category: Thorsell AG]]
[[Category: Sundstrom, M.]]
[[Category: Tresaugues L]]
[[Category: Thorsell, A G.]]
[[Category: Weigelt J]]
[[Category: Tresaugues, L.]]
[[Category: Welin M]]
[[Category: Weigelt, J.]]
[[Category: Van den Berg S]]
[[Category: Welin, M.]]
[[Category: Acot7]]
[[Category: C-terminal domain]]
[[Category: Hydrolase]]
[[Category: Mitochondrion]]
[[Category: Serine esterase]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Thioesterase]]
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