5yjo
From Proteopedia
(Difference between revisions)
m (Protected "5yjo" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of SmyD3 in complex with covalent inhibitor 4== | |
| - | + | <StructureSection load='5yjo' size='340' side='right' caption='[[5yjo]], [[Resolution|resolution]] 2.13Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5yjo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YJO FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8W0:propyl+(3~{S})-4-[[(6~{R})-6-(aminomethyl)-5,6,7,8-tetrahydroacridin-3-yl]carbonyl]-3-methyl-piperazine-1-carboxylate'>8W0</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | [[Category: | + | <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> |
| + | <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=5yjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yjo OCA], [http://pdbe.org/5yjo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yjo RCSB], [http://www.ebi.ac.uk/pdbsum/5yjo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yjo ProSAT]</span></td></tr> | ||
| + | </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: Baburajendran, N]] | ||
| + | [[Category: E, J Anna]] | ||
| + | [[Category: Covalent inhibitor]] | ||
| + | [[Category: Methyltransferase]] | ||
| + | [[Category: Methyltransferase inhibitor]] | ||
| + | [[Category: Transferase-inhibitor complex]] | ||
Revision as of 07:50, 17 October 2018
Crystal structure of SmyD3 in complex with covalent inhibitor 4
| |||||||||||
