3bgi: Difference between revisions

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{{Seed}}
[[Image:3bgi.png|left|200px]]


<!--
==Thiopurine S-Methyltransferase==
The line below this paragraph, containing "STRUCTURE_3bgi", creates the "Structure Box" on the page.
<StructureSection load='3bgi' size='340' side='right'caption='[[3bgi]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3bgi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BGI FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
{{STRUCTURE_3bgi|  PDB=3bgi  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bgi OCA], [https://pdbe.org/3bgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bgi RCSB], [https://www.ebi.ac.uk/pdbsum/3bgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bgi ProSAT]</span></td></tr>
 
</table>
===Thiopurine S-Methyltransferase===
== Function ==
 
[https://www.uniprot.org/uniprot/TPMT_MOUSE TPMT_MOUSE] Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine.
 
== Evolutionary Conservation ==
<!--
[[Image:Consurf_key_small.gif|200px|right]]
The line below this paragraph, {{ABSTRACT_PUBMED_18484748}}, adds the Publication Abstract to the page
Check<jmol>
(as it appears on PubMed at http://www.pubmed.gov), where 18484748 is the PubMed ID number.
  <jmolCheckbox>
-->
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/3bgi_consurf.spt"</scriptWhenChecked>
{{ABSTRACT_PUBMED_18484748}}
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
3BGI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BGI OCA].  
</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=3bgi ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
Structural basis of substrate recognition in thiopurine s-methyltransferase., Peng Y, Feng Q, Wilk D, Adjei AA, Salavaggione OE, Weinshilboum RM, Yee VC, Biochemistry. 2008 Jun 10;47(23):6216-25. Epub 2008 May 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18484748 18484748]
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Peng Y]]
[[Category: Thiopurine S-methyltransferase]]
[[Category: Yee VC]]
[[Category: Peng, Y.]]
[[Category: Yee, V C.]]
[[Category: Cytoplasm]]
[[Category: Methyltransferase]]
[[Category: S-adenosyl-l-methionine]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:46:33 2008''

Latest revision as of 09:28, 21 February 2024

Thiopurine S-Methyltransferase

3bgi, resolution 1.80Å

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