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==Crystal structure of Dot1L in complex with inhibitor CPD1 [N6-(2,6-dichlorophenyl)-N6-(pent-2-yn-1-yl)quinoline-4,6-diamine] and inhibitor CPD2 [(R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-amine]==
==Crystal structure of Dot1L in complex with inhibitor CPD1 [N6-(2,6-dichlorophenyl)-N6-(pent-2-yn-1-yl)quinoline-4,6-diamine] and inhibitor CPD2 [(R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-amine]==
<StructureSection load='5mw3' size='340' side='right' caption='[[5mw3]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
<StructureSection load='5mw3' size='340' side='right'caption='[[5mw3]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5mw3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MW3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5mw3]] is a 2 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=5MW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MW3 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=5JT:(3R)-1-(7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)PIPERIDIN-3-AMINE'>5JT</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09&#8491;</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5JT:(3R)-1-(7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)PIPERIDIN-3-AMINE'>5JT</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=5mw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mw3 OCA], [http://pdbe.org/5mw3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mw3 RCSB], [http://www.ebi.ac.uk/pdbsum/5mw3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mw3 ProSAT]</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=5mw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mw3 OCA], [https://pdbe.org/5mw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mw3 RCSB], [https://www.ebi.ac.uk/pdbsum/5mw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mw3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.  
[https://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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5mw3" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5mw3" style="background-color:#fffaf0;"></div>
==See Also==
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Be, C]]
[[Category: Large Structures]]
[[Category: Gaul, C]]
[[Category: Be C]]
[[Category: Koch, E]]
[[Category: Gaul C]]
[[Category: Moebitz, H]]
[[Category: Koch E]]
[[Category: Scheufler, C]]
[[Category: Moebitz H]]
[[Category: Stauffer, F]]
[[Category: Scheufler C]]
[[Category: Complex]]
[[Category: Stauffer F]]
[[Category: Inhibitor]]
[[Category: Methyltransferase]]
[[Category: Transferase]]

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