5a7f: Difference between revisions
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==Comparison of the structure and activity of glycosylated and aglycosylated Human Carboxylesterase 1== | ==Comparison of the structure and activity of glycosylated and aglycosylated Human Carboxylesterase 1== | ||
<StructureSection load='5a7f' size='340' side='right' caption='[[5a7f]], [[Resolution|resolution]] 1.86Å' scene=''> | <StructureSection load='5a7f' size='340' side='right'caption='[[5a7f]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a7f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A7F OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5a7f]] is a 1 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=5A7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A7F FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=5a7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a7f OCA], [https://pdbe.org/5a7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a7f RCSB], [https://www.ebi.ac.uk/pdbsum/5a7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a7f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/EST1_HUMAN EST1_HUMAN] Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate.<ref>PMID:7980644</ref> <ref>PMID:9169443</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5a7f" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5a7f" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arena de Souza V]] | ||
[[Category: | [[Category: Charlton M]] | ||
[[Category: | [[Category: Owen RJ]] | ||
[[Category: | [[Category: Scott DJ]] | ||
[[Category: | [[Category: Walsh MA]] | ||