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{{STRUCTURE_3pdn|  PDB=3pdn  |  SCENE=  }}
===Crystal structure of SmyD3 in complex with methyltransferase inhibitor sinefungin===
{{ABSTRACT_PUBMED_21167177}}


==Function==
==Crystal structure of SmyD3 in complex with methyltransferase inhibitor sinefungin==
[[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='3pdn' size='340' side='right'caption='[[3pdn]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[3pdn]] 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=3PDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PDN FirstGlance]. <br>
[[3pdn]] 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=3PDN 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]] 1.7&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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=3pdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdn OCA], [https://pdbe.org/3pdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pdn RCSB], [https://www.ebi.ac.uk/pdbsum/3pdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pdn ProSAT]</span></td></tr>
<ref group="xtra">PMID:021167177</ref><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>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Brunzelle, J.]]
[[Category: Large Structures]]
[[Category: Sirinupong, N.]]
[[Category: Brunzelle J]]
[[Category: Yang, Z.]]
[[Category: Sirinupong N]]
[[Category: Methyltransferase]]
[[Category: Yang Z]]
[[Category: Rossmann fold]]
[[Category: Transferase]]
[[Category: Transferase-transferase inhibitor complex]]
[[Category: Zinc finger]]
Retrieved from "https://proteopedia.org/3pdn"