5mvs
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Dot1L in complex with adenosine and inhibitor CPD1 [N6-(2,6-dichlorophenyl)-N6-(pent-2-yn-1-yl)quinoline-4,6-diamine]== | |
| - | + | <StructureSection load='5mvs' size='340' side='right' caption='[[5mvs]], [[Resolution|resolution]] 2.18Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5mvs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MVS FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5JJ:N~6~-(2,6-DICHLOROPHENYL)-N~6~-(PENT-2-YN-1-YL)QUINOLINE-4,6-DIAMINE'>5JJ</scene>, <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=5mvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mvs OCA], [http://pdbe.org/5mvs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mvs RCSB], [http://www.ebi.ac.uk/pdbsum/5mvs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mvs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DOT1L_HUMAN DOT1L_HUMAN]] Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Be, C]] | [[Category: Be, C]] | ||
[[Category: Gaul, C]] | [[Category: Gaul, C]] | ||
| + | [[Category: Koch, E]] | ||
[[Category: Moebitz, H]] | [[Category: Moebitz, H]] | ||
| + | [[Category: Scheufler, C]] | ||
[[Category: Stauffer, F]] | [[Category: Stauffer, F]] | ||
| - | [[Category: | + | [[Category: Complex]] |
| - | [[Category: | + | [[Category: Inhibitor]] |
| + | [[Category: Methyltransferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 16:24, 22 March 2017
Crystal structure of Dot1L in complex with adenosine and inhibitor CPD1 [N6-(2,6-dichlorophenyl)-N6-(pent-2-yn-1-yl)quinoline-4,6-diamine]
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