5juw: Difference between revisions

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'''Unreleased structure'''


The entry 5juw is ON HOLD
==complex of Dot1l with SS148==
 
<StructureSection load='5juw' size='340' side='right' caption='[[5juw]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
Authors: Yu, W., Tempel, W., Li, Y., Spurr, S.S., Bayle, E.D., Fish, P.V., Schapira, M., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Weigelt, J., Brown, P.J., Structural Genomics Consortium (SGC)
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5juw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JUW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JUW FirstGlance]. <br>
Description: complex of Dot1l with SS148
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6NR:(2~{S})-2-AZANYL-4-[[(2~{S},3~{S},4~{R},5~{R})-5-(4-AZANYL-5-CYANO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHYLSULFANYL]BUTANOIC+ACID'>6NR</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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>
[[Category: Bayle, E.D]]
<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=5juw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5juw OCA], [http://pdbe.org/5juw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5juw RCSB], [http://www.ebi.ac.uk/pdbsum/5juw PDBsum]</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: Arrowsmith, C H]]
[[Category: Bayle, E D]]
[[Category: Bountra, C]]
[[Category: Brown, P J]]
[[Category: Edwards, A M]]
[[Category: Fish, P V]]
[[Category: Li, Y]]
[[Category: Li, Y]]
[[Category: Yu, W]]
[[Category: Structural genomic]]
[[Category: Schapira, M]]
[[Category: Schapira, M]]
[[Category: Bountra, C]]
[[Category: Spurr, S S]]
[[Category: Tempel, W]]
[[Category: Tempel, W]]
[[Category: Arrowsmith, C.H]]
[[Category: Fish, P.V]]
[[Category: Brown, P.J]]
[[Category: Edwards, A.M]]
[[Category: Structural Genomics Consortium (Sgc)]]
[[Category: Spurr, S.S]]
[[Category: Weigelt, J]]
[[Category: Weigelt, J]]
[[Category: Yu, W]]
[[Category: Sgc]]
[[Category: Transferase]]
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