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2h4u
From Proteopedia
(Difference between revisions)
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<StructureSection load='2h4u' size='340' side='right'caption='[[2h4u]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2h4u' size='340' side='right'caption='[[2h4u]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2h4u]] is a 4 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 11:05, 5 January 2022
Crystal Structure of Human Thioesterase Superfamily Member 2 (CASP Target)
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Categories: Acetyl-CoA hydrolase | Human | Large Structures | Arrowsmith, C | Berglund, H | Edwards, A | Ehn, M | Flodin, S | Grasslund, S | Hallberg, M | Hammerstrom, M | Hogbom, M | Holmberg-Schiavone, L | Kotenyova, T | Nilsson-Ehle, P | Nordlund, P | Nyman, T | Ogg, D J | Persson, C | Structural genomic | Sagemark, J | Sundstrom, M | Thorsell, A G | Uppenberg, J | Weigelt, J | Hydrolase | Sgc | Thioesterase
