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{{STRUCTURE_3o7w|  PDB=3o7w  |  SCENE=  }}
===The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1===
{{ABSTRACT_PUBMED_21206058}}


==Function==
==The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1==
[[http://www.uniprot.org/uniprot/LCMT1_HUMAN LCMT1_HUMAN]] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.<ref>PMID:10600115</ref>
<StructureSection load='3o7w' size='340' side='right'caption='[[3o7w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[3o7w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O7W FirstGlance]. <br>
[[3o7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [https://pdbe.org/3o7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [https://www.ebi.ac.uk/pdbsum/3o7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7w ProSAT]</span></td></tr>
<ref group="xtra">PMID:021206058</ref><references group="xtra"/><references/>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LCMT1_HUMAN LCMT1_HUMAN] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.<ref>PMID:10600115</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/o7/3o7w_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=3o7w ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Cronin, N.]]
[[Category: Large Structures]]
[[Category: Djordjevic, S.]]
[[Category: Cronin N]]
[[Category: Tsai, M L.]]
[[Category: Djordjevic S]]
[[Category: Modified rossmann fold]]
[[Category: Tsai ML]]
[[Category: Pp2a]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/3o7w"