3mek: Difference between revisions

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{{STRUCTURE_3mek|  PDB=3mek  |  SCENE=  }}
===Crystal Structure of Human Histone-Lysine N-methyltransferase SMYD3 in Complex with S-adenosyl-L-methionine===


==Function==
==Crystal Structure of Human Histone-Lysine N-methyltransferase SMYD3 in Complex with S-adenosyl-L-methionine==
[[http://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN]] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref>
<StructureSection load='3mek' size='340' side='right'caption='[[3mek]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[3mek]] 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=3MEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MEK FirstGlance]. <br>
[[3mek]] is a 1 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=3MEK 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]] 2.1&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3mek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mek OCA], [https://pdbe.org/3mek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mek RCSB], [https://www.ebi.ac.uk/pdbsum/3mek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mek ProSAT]</span></td></tr>
<references group="xtra"/><references/>
</table>
[[Category: Histone-lysine N-methyltransferase]]
== Function ==
[https://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</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/me/3mek_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3mek ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H.]]
[[Category: Large Structures]]
[[Category: Bochkarev, A.]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C.]]
[[Category: Bochkarev A]]
[[Category: Dombrovski, L.]]
[[Category: Bountra C]]
[[Category: Edwards, A M.]]
[[Category: Dombrovski L]]
[[Category: Lam, R.]]
[[Category: Edwards AM]]
[[Category: Li, Y.]]
[[Category: Lam R]]
[[Category: Min, J.]]
[[Category: Li Y]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Min J]]
[[Category: Weigelt, J.]]
[[Category: Weigelt J]]
[[Category: Wu, H.]]
[[Category: Wu H]]
[[Category: Chromatin modification]]
[[Category: Chromatin regulator]]
[[Category: Di-methylation]]
[[Category: Dna-binding]]
[[Category: Histone h3]]
[[Category: Histone methyltransferase]]
[[Category: Metal-binding]]
[[Category: Methyltransferase]]
[[Category: Mynd-type zinc finger]]
[[Category: Nucleus]]
[[Category: S-adenosyl-l-methionine]]
[[Category: Set and mynd domain-containing protein 3]]
[[Category: Set domain]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Transcriptional activation]]
[[Category: Transferase]]
[[Category: Tri-methylation]]
[[Category: Zinc finger mynd domain-containing protein 1]]
[[Category: Zinc-finger]]

Latest revision as of 09:25, 30 October 2024

Crystal Structure of Human Histone-Lysine N-methyltransferase SMYD3 in Complex with S-adenosyl-L-methionine

3mek, resolution 2.10Å

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