5mw3: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry 5mw3 is ON HOLD~~

==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]==

~~Authors: Be, C., Koch, E., Gaul, C., Stauffer, F., Moebitz, H., Scheufler, C.~~

== 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 guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MW3 FirstGlance].

~~Description:~~ 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]

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</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>

[[Category: ~~Unreleased Structures~~]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[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]</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: Gaul, C]]

[[Category: Koch, E]]

[[Category: Moebitz, H]]

[[Category: Scheufler, C]]

[[Category: Stauffer, F]]

[[Category: ~~Scheufler, C~~]]

[[Category: Complex]]

[[Category: ~~Koch, E~~]]

[[Category: Inhibitor]]

[[Category: Methyltransferase]]

[[Category: Transferase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5mw3 is ON HOLD
+==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=''>
-Authors: Be, C., Koch, E., Gaul, C., Stauffer, F., Moebitz, H., Scheufler, C.
+== 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>
-Description: 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]
+</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>
-[[Category: Unreleased Structures]]
+<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=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>
+</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: Gaul, C]]
+[[Category: Koch, E]]
 [[Category: Moebitz, H]]
+[[Category: Scheufler, C]]
 [[Category: Stauffer, F]]
-[[Category: Scheufler, C]]
+[[Category: Complex]]
-[[Category: Koch, E]]
+[[Category: Inhibitor]]
+[[Category: Methyltransferase]]
+[[Category: Transferase]]