7bj1: Difference between revisions
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==Crystal structure of SMYD3 with diperodon S enantiomer bound to allosteric site== | ==Crystal structure of SMYD3 with diperodon S enantiomer bound to allosteric site== | ||
<StructureSection load='7bj1' size='340' side='right'caption='[[7bj1]]' scene=''> | <StructureSection load='7bj1' size='340' side='right'caption='[[7bj1]], [[Resolution|resolution]] 1.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6z2r 6z2r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BJ1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7bj1]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6z2r 6z2r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BJ1 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7bj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bj1 OCA], [https://pdbe.org/7bj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bj1 RCSB], [https://www.ebi.ac.uk/pdbsum/7bj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bj1 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=QKT:Diperodon+(S-enantiomer)'>QKT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/[Histone_H3]-lysine(4)_N-trimethyltransferase [Histone H3]-lysine(4) N-trimethyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.354 2.1.1.354] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7bj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bj1 OCA], [https://pdbe.org/7bj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bj1 RCSB], [https://www.ebi.ac.uk/pdbsum/7bj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bj1 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Danielson | [[Category: Danielson, U H]] | ||
[[Category: Dobritzsch D]] | [[Category: Dobritzsch, D]] | ||
[[Category: Eriksson D]] | [[Category: Eriksson, D]] | ||
[[Category: Talibov | [[Category: Talibov, V O]] | ||
[[Category: Complex]] | |||
[[Category: Inhibitor]] | |||
[[Category: Methyltransferase]] | |||
[[Category: Oncoprotein]] | |||
