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[[Image:1fj2.png|left|200px]]


{{STRUCTURE_1fj2|  PDB=1fj2  |  SCENE=  }}
==Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution==
 
<StructureSection load='1fj2' size='340' side='right'caption='[[1fj2]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
===Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1fj2]] 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=1FJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FJ2 FirstGlance]. <br>
{{ABSTRACT_PUBMED_11080636}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fj2 OCA], [https://pdbe.org/1fj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fj2 RCSB], [https://www.ebi.ac.uk/pdbsum/1fj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fj2 ProSAT]</span></td></tr>
[[1fj2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJ2 OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYPA1_HUMAN LYPA1_HUMAN] Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity and also low lysophospholipase activity.<ref>PMID:20418879</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/1fj2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=1fj2 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Thioesterase|Thioesterase]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:011080636</ref><references group="xtra"/>
__TOC__
[[Category: Alkylglycerophosphoethanolamine phosphodiesterase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Dauter, Z.]]
[[Category: Large Structures]]
[[Category: Derewenda, Z.]]
[[Category: Dauter Z]]
[[Category: Devedjiev, Y.]]
[[Category: Derewenda Z]]
[[Category: Jones, T.]]
[[Category: Devedjiev Y]]
[[Category: Kuznetsov, S.]]
[[Category: Jones T]]
[[Category: Alpha/beta hydrolase]]
[[Category: Kuznetsov S]]
[[Category: Anomalous diffraction]]
[[Category: Hydrolase]]
[[Category: Sad]]
[[Category: Serine hydrolase]]
Retrieved from "https://proteopedia.org/1fj2"