2h4u: Difference between revisions

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<StructureSection load='2h4u' size='340' side='right'caption='[[2h4u]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2h4u' size='340' side='right'caption='[[2h4u]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2h4u]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2H4U FirstGlance]. <br>
<table><tr><td colspan='2'>[[2h4u]] 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=2H4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H4U FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetyl-CoA_hydrolase Acetyl-CoA hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.1 3.1.2.1] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4u OCA], [https://pdbe.org/2h4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h4u RCSB], [https://www.ebi.ac.uk/pdbsum/2h4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h4u ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4u OCA], [https://pdbe.org/2h4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h4u RCSB], [https://www.ebi.ac.uk/pdbsum/2h4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h4u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ACO13_HUMAN ACO13_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).  
[https://www.uniprot.org/uniprot/ACO13_HUMAN ACO13_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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acetyl-CoA hydrolase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C]]
[[Category: Arrowsmith C]]
[[Category: Berglund, H]]
[[Category: Berglund H]]
[[Category: Edwards, A]]
[[Category: Edwards A]]
[[Category: Ehn, M]]
[[Category: Ehn M]]
[[Category: Flodin, S]]
[[Category: Flodin S]]
[[Category: Grasslund, S]]
[[Category: Grasslund S]]
[[Category: Hallberg, M]]
[[Category: Hallberg M]]
[[Category: Hammerstrom, M]]
[[Category: Hammerstrom M]]
[[Category: Hogbom, M]]
[[Category: Hogbom M]]
[[Category: Holmberg-Schiavone, L]]
[[Category: Holmberg-Schiavone L]]
[[Category: Kotenyova, T]]
[[Category: Kotenyova T]]
[[Category: Nilsson-Ehle, P]]
[[Category: Nilsson-Ehle P]]
[[Category: Nordlund, P]]
[[Category: Nordlund P]]
[[Category: Nyman, T]]
[[Category: Nyman T]]
[[Category: Ogg, D J]]
[[Category: Ogg DJ]]
[[Category: Persson, C]]
[[Category: Persson C]]
[[Category: Structural genomic]]
[[Category: Sagemark J]]
[[Category: Sagemark, J]]
[[Category: Sundstrom M]]
[[Category: Sundstrom, M]]
[[Category: Thorsell A-G]]
[[Category: Thorsell, A G]]
[[Category: Uppenberg J]]
[[Category: Uppenberg, J]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Hydrolase]]
[[Category: Sgc]]
[[Category: Thioesterase]]

Latest revision as of 09:52, 30 August 2023

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

2h4u, resolution 2.20Å

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