5ph8: Difference between revisions

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'''Unreleased structure'''


The entry 5ph8 is ON HOLD
==PanDDA analysis group deposition -- Crystal Structure of JMJD2D in complex with N09552a==
 
<StructureSection load='5ph8' size='340' side='right' caption='[[5ph8]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
Authors: Krojer, T.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5ph8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5PH8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5PH8 FirstGlance]. <br>
Description: PanDDA analysis group deposition --Crystal Structure of JMJD2D in complex with N09552a
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1XN:2H-ISOINDOLE-1,3-DIAMINE'>1XN</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=PHT:PHTHALIC+ACID'>PHT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Unreleased Structures]]
<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=5ph8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ph8 OCA], [http://pdbe.org/5ph8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ph8 RCSB], [http://www.ebi.ac.uk/pdbsum/5ph8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ph8 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/KDM4D_HUMAN KDM4D_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arrowsmith, C H]]
[[Category: Bountra, C]]
[[Category: Bradley, A R]]
[[Category: Brandao-Neto, J]]
[[Category: Brennan, P E]]
[[Category: Burgess-Brown, N]]
[[Category: Collins, P]]
[[Category: Cox, O]]
[[Category: Delft, F von]]
[[Category: Dias, A]]
[[Category: Douangamath, A]]
[[Category: Edwards, A]]
[[Category: Fairhead, M]]
[[Category: Krojer, T]]
[[Category: Krojer, T]]
[[Category: MacLean, E]]
[[Category: Ng, J]]
[[Category: Oppermann, U]]
[[Category: Pearce, N M]]
[[Category: Renjie, Z]]
[[Category: Sethi, R]]
[[Category: Szykowska, A]]
[[Category: Talon, R]]
[[Category: Vollmar, M]]
[[Category: Wright, N]]
[[Category: Epigenetic]]
[[Category: Jmj domain]]
[[Category: Oxidoreductase]]
[[Category: Pandda]]
[[Category: Sgc - diamond i04-1 fragment screening]]

Revision as of 00:23, 16 March 2017

PanDDA analysis group deposition -- Crystal Structure of JMJD2D in complex with N09552aPanDDA analysis group deposition -- Crystal Structure of JMJD2D in complex with N09552a

Structural highlights

5ph8 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KDM4D_HUMAN] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.[1]

References

  1. ↑ Whetstine JR, Nottke A, Lan F, Huarte M, Smolikov S, Chen Z, Spooner E, Li E, Zhang G, Colaiacovo M, Shi Y. Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell. 2006 May 5;125(3):467-81. Epub 2006 Apr 6. PMID:16603238 doi:10.1016/j.cell.2006.03.028

5ph8, resolution 1.40Å

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