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==Cocrystal structure of the human acyl protein thioesterase 2 with an isoform-selective inhibitor, ML349== | |||
<StructureSection load='5syn' size='340' side='right' caption='[[5syn]], [[Resolution|resolution]] 1.64Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5syn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SYN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=71T:2-[4-(4-METHOXYPHENYL)PIPERAZINE-1-CARBONYL]-5LAMBDA~6~-THIENO[3,2-C][1]BENZOTHIOPYRAN-5,5(4H)-DIONE'>71T</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | |||
[[ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5sym|5sym]]</td></tr> | ||
[[Category: Labby, K | <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=5syn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5syn OCA], [http://pdbe.org/5syn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5syn RCSB], [http://www.ebi.ac.uk/pdbsum/5syn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5syn ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: Meagher, J | == Function == | ||
[[Category: Stuckey, J | [[http://www.uniprot.org/uniprot/LYPA2_HUMAN LYPA2_HUMAN]] May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity (By similarity). Deacylates GAP43.<ref>PMID:21152083</ref> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Labby, K J]] | |||
[[Category: Martin, B R]] | |||
[[Category: Meagher, J L]] | |||
[[Category: Stuckey, J A]] | |||
[[Category: Won, S J]] | |||
[[Category: Hydrolase]] | |||
[[Category: Hydrolase-hydrolase inhibitor complex]] | |||
[[Category: Inhibitor]] | |||
[[Category: Thioesterase]] |
Revision as of 21:50, 26 October 2016
Cocrystal structure of the human acyl protein thioesterase 2 with an isoform-selective inhibitor, ML349Cocrystal structure of the human acyl protein thioesterase 2 with an isoform-selective inhibitor, ML349
Structural highlights
Function[LYPA2_HUMAN] May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity (By similarity). Deacylates GAP43.[1] References
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