5ph3: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "5ph3" [edit=sysop:move=sysop]
No edit summary
Line 1: Line 1:
'''Unreleased structure'''


The entry 5ph3 is ON HOLD
==PanDDA analysis group deposition -- Crystal Structure of JMJD2D in complex with N09575a==
 
<StructureSection load='5ph3' size='340' side='right' caption='[[5ph3]], [[Resolution|resolution]] 1.24&Aring;' scene=''>
Authors: Krojer, T.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5ph3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5PH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5PH3 FirstGlance]. <br>
Description: PanDDA analysis group deposition --Crystal Structure of JMJD2D in complex with N09575a
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMD:5,6-DIMETHYLBENZIMIDAZOLE'>DMD</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=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=5ph3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ph3 OCA], [http://pdbe.org/5ph3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ph3 RCSB], [http://www.ebi.ac.uk/pdbsum/5ph3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ph3 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 00:22, 16 March 2017

PanDDA analysis group deposition -- Crystal Structure of JMJD2D in complex with N09575aPanDDA analysis group deposition -- Crystal Structure of JMJD2D in complex with N09575a

Structural highlights

5ph3 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

5ph3, resolution 1.24Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA