5phc: Difference between revisions

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New page: '''Unreleased structure''' The entry 5phc is ON HOLD Authors: Krojer, T. Description: PanDDA analysis group deposition --Crystal Structure of JMJD2D in complex with N09649a [[Category:...
 
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'''Unreleased structure'''


The entry 5phc is ON HOLD
==PanDDA analysis group deposition -- Crystal Structure of JMJD2D in complex with N09649a==
<StructureSection load='5phc' size='340' side='right'caption='[[5phc]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5phc]] is a 1 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=5PHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5PHC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.29&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5VL:2-(2-HYDROXYPHENYL)PHENOL'>5VL</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5phc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5phc OCA], [https://pdbe.org/5phc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5phc RCSB], [https://www.ebi.ac.uk/pdbsum/5phc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5phc ProSAT]</span></td></tr>
</table>
== Function ==
[https://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>


Authors: Krojer, T.
==See Also==
 
*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
Description: PanDDA analysis group deposition --Crystal Structure of JMJD2D in complex with N09649a
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Krojer, T]]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Bountra C]]
[[Category: Bradley AR]]
[[Category: Brandao-Neto J]]
[[Category: Brennan PE]]
[[Category: Burgess-Brown N]]
[[Category: Collins P]]
[[Category: Cox O]]
[[Category: Dias A]]
[[Category: Douangamath A]]
[[Category: Edwards A]]
[[Category: Fairhead M]]
[[Category: Krojer T]]
[[Category: MacLean E]]
[[Category: Ng J]]
[[Category: Oppermann U]]
[[Category: Pearce NM]]
[[Category: Renjie Z]]
[[Category: Sethi R]]
[[Category: Szykowska A]]
[[Category: Talon R]]
[[Category: Vollmar M]]
[[Category: Wright N]]
[[Category: Von Delft F]]

Latest revision as of 15:54, 6 March 2024

PanDDA analysis group deposition -- Crystal Structure of JMJD2D in complex with N09649aPanDDA analysis group deposition -- Crystal Structure of JMJD2D in complex with N09649a

Structural highlights

5phc is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.29Å
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]

See Also

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

5phc, resolution 1.29Å

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