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2qq2
From Proteopedia
(Difference between revisions)
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==Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7== | ==Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7== | ||
| - | <StructureSection load='2qq2' size='340' side='right' caption='[[2qq2]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='2qq2' size='340' side='right'caption='[[2qq2]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2qq2]] is a 12 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2qq2]] is a 12 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=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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACOT7, BACH ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACOT7, BACH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Palmitoyl-CoA_hydrolase Palmitoyl-CoA hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.2 3.1.2.2] </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=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> |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Thioesterase|Thioesterase]] | + | *[[Thioesterase 3D structures|Thioesterase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Palmitoyl-CoA hydrolase]] | [[Category: Palmitoyl-CoA hydrolase]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
Revision as of 08:28, 25 June 2021
Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7
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Categories: Human | Large Structures | Palmitoyl-CoA hydrolase | Arrowsmith, C H | Berg, S van den | Berglund, H | Busam, R | Collins, R | Dahlgren, L G | Edwards, A | Flodin, S | Flores, A | Graslund, S | Hallberg, B M | Hammarstrom, M | Herman, M D | Holmberg-Schiavone, L | Johansson, I | Kallas, A | Karlberg, T | Kotenyova, T | Lehtio, L | Moche, M | Nordlund, P | Nyman, T | Persson, C | Structural genomic | Sagemark, J | Stenmark, P | Sundstrom, M | Thorsell, A G | Tresaugues, L | Weigelt, J | Welin, M | Acot7 | C-terminal domain | Hydrolase | Mitochondrion | Serine esterase | Sgc | Thioesterase
