2h4u
From Proteopedia
(Difference between revisions)
| Line 2: | Line 2: | ||
<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 [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2h4u]] is a 4 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=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> |
</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> | </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> | ||
| - | <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> | + | <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://pdbe.org/2h4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h4u RCSB], [http://www.ebi.ac.uk/pdbsum/2h4u PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://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]] | ||
| Line 18: | Line 18: | ||
</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> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Acetyl-CoA hydrolase]] | [[Category: Acetyl-CoA hydrolase]] | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Arrowsmith, C]] | [[Category: Arrowsmith, C]] | ||
[[Category: Berglund, H]] | [[Category: Berglund, H]] | ||
Revision as of 06:27, 11 September 2015
Crystal Structure of Human Thioesterase Superfamily Member 2 (CASP Target)
| |||||||||||
Categories: Acetyl-CoA hydrolase | Human | 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
