3s7j: Difference between revisions

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[[Image:3s7j.png|left|200px]]


{{STRUCTURE_3s7j|  PDB=3s7j  |  SCENE=  }}
==Structural Basis of Substrate Methylation and Inhibition of SMYD2==
 
<StructureSection load='3s7j' size='340' side='right'caption='[[3s7j]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
===Structural Basis of Substrate Methylation and Inhibition of SMYD2===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3s7j]] 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=3S7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S7J FirstGlance]. <br>
{{ABSTRACT_PUBMED_21782458}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.04&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3s7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s7j OCA], [https://pdbe.org/3s7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s7j RCSB], [https://www.ebi.ac.uk/pdbsum/3s7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s7j ProSAT]</span></td></tr>
[[3s7j]] 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=3S7J OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.<ref>PMID:17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref> <ref>PMID:20870719</ref>


==See Also==
==See Also==
*[[Histone methyltransferase|Histone methyltransferase]]
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:021782458</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ferguson, A D.]]
[[Category: Large Structures]]
[[Category: Methyltransferase]]
[[Category: Ferguson AD]]
[[Category: P53]]
[[Category: Transferase]]