5ccl
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of SMYD3 with SAM and oxindole compound== |
| - | + | <StructureSection load='5ccl' size='340' side='right' caption='[[5ccl]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5ccl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4ZW:2-OXIDANYLIDENE-N-PIPERIDIN-4-YL-1,3-DIHYDROINDOLE-5-CARBOXAMIDE'>4ZW</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ccm|5ccm]]</td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ccl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ccl RCSB], [http://www.ebi.ac.uk/pdbsum/5ccl PDBsum]</span></td></tr> |
| - | [[Category: Boriack-Sjodin, P | + | </table> |
| + | == Function == | ||
| + | [[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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Histone-lysine N-methyltransferase]] | ||
| + | [[Category: Boriack-Sjodin, P A]] | ||
| + | [[Category: Drug discovery]] | ||
| + | [[Category: Epigenetic]] | ||
| + | [[Category: Methyltransferase]] | ||
| + | [[Category: Protein-inhibitor complex]] | ||
| + | [[Category: Transferase-transferase inhibitor complex]] | ||
Revision as of 11:23, 9 September 2015
Crystal structure of SMYD3 with SAM and oxindole compound
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