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2h4u

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2h4u]] is a 4 chain structure 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=2H4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H4U FirstGlance]. <br>
<table><tr><td colspan='2'>[[2h4u]] is a 4 chain structure 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=2H4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H4U FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_hydrolase Acetyl-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.1 3.1.2.1] </span></td></tr>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_hydrolase Acetyl-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.1 3.1.2.1] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h4u RCSB], [http://www.ebi.ac.uk/pdbsum/2h4u PDBsum]</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=2h4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h4u RCSB], [http://www.ebi.ac.uk/pdbsum/2h4u PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/THEM2_HUMAN THEM2_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. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis (By similarity).<ref>PMID:16934754</ref> <ref>PMID:19170545</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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/chain_selection.php?pdb_ID=2ata ConSurf].
</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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acetyl-CoA hydrolase]]
[[Category: Acetyl-CoA hydrolase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C.]]
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[[Category: Arrowsmith, C]]
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[[Category: Berglund, H.]]
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[[Category: Berglund, H]]
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[[Category: Edwards, A.]]
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[[Category: Edwards, A]]
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[[Category: Ehn, M.]]
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[[Category: Ehn, M]]
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[[Category: Flodin, S.]]
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[[Category: Flodin, S]]
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[[Category: Grasslund, S.]]
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[[Category: Grasslund, S]]
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[[Category: Hallberg, M.]]
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[[Category: Hallberg, M]]
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[[Category: Hammerstrom, M.]]
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[[Category: Hammerstrom, M]]
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[[Category: Hogbom, M.]]
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[[Category: Hogbom, M]]
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[[Category: Holmberg-Schiavone, L.]]
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[[Category: Holmberg-Schiavone, L]]
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[[Category: Kotenyova, T.]]
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[[Category: Kotenyova, T]]
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[[Category: Nilsson-Ehle, P.]]
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[[Category: Nilsson-Ehle, P]]
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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: Ogg, D J.]]
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[[Category: Ogg, D J]]
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[[Category: Persson, C.]]
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[[Category: Persson, C]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Structural genomic]]
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[[Category: Sagemark, J.]]
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[[Category: Sagemark, J]]
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[[Category: Sundstrom, M.]]
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[[Category: Sundstrom, M]]
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[[Category: Thorsell, A G.]]
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[[Category: Thorsell, A G]]
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[[Category: Uppenberg, J.]]
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[[Category: Uppenberg, J]]
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[[Category: Weigelt, J.]]
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[[Category: Weigelt, J]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Sgc]]
[[Category: Sgc]]
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[[Category: Structural genomic]]
 
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[[Category: Structural genomics consortium]]
 
[[Category: Thioesterase]]
[[Category: Thioesterase]]

Revision as of 12:34, 25 December 2014

Crystal Structure of Human Thioesterase Superfamily Member 2 (CASP Target)

2h4u, resolution 2.20Å

Drag the structure with the mouse to rotate

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