7ots

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<StructureSection load='7ots' size='340' side='right'caption='[[7ots]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
<StructureSection load='7ots' size='340' side='right'caption='[[7ots]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7ots]] is a 2 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=7OTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OTS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7ots]] is a 2 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=7OTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OTS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.792&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABHD6 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acylglycerol_lipase Acylglycerol lipase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.23 3.1.1.23] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ots FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ots OCA], [https://pdbe.org/7ots PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ots RCSB], [https://www.ebi.ac.uk/pdbsum/7ots PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ots 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=7ots FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ots OCA], [https://pdbe.org/7ots PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ots RCSB], [https://www.ebi.ac.uk/pdbsum/7ots PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ots ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ABHD6_HUMAN ABHD6_HUMAN]] Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (By similarity). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism (PubMed:26491015). BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (PubMed:26491015).[UniProtKB:Q8R2Y0]<ref>PMID:22969151</ref> <ref>PMID:26491015</ref>
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[https://www.uniprot.org/uniprot/ABHD6_HUMAN ABHD6_HUMAN] Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (By similarity). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism (PubMed:26491015). BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (PubMed:26491015).[UniProtKB:Q8R2Y0]<ref>PMID:22969151</ref> <ref>PMID:26491015</ref>
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==See Also==
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*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acylglycerol lipase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Miallau, L]]
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[[Category: Miallau L]]
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[[Category: Nawrotek, A]]
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[[Category: Nawrotek A]]
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[[Category: Talagas, A]]
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[[Category: Talagas A]]
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[[Category: Vuillard, L]]
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[[Category: Vuillard L]]
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[[Category: 2-ag signalling]]
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[[Category: 2-arachidonoylglycerol hydrolase]]
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[[Category: Alpha/beta-hydrolase domain containing 6]]
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[[Category: Endocannabinoid system]]
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[[Category: Hydrolase]]
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[[Category: Monoacylglycerol lipase abhd6]]
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[[Category: Nervous system]]
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Current revision

Crystal structure of human Monoacylglycerol Lipase ABHD6 in complex with oleic acid and octyl glucoside

PDB ID 7ots

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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