6h0z: Difference between revisions
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New page: '''Unreleased structure''' The entry 6h0z is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Crystal Structure of KDM4D with tetrazolylhydrazide ligand NR067== | |||
<StructureSection load='6h0z' size='340' side='right'caption='[[6h0z]], [[Resolution|resolution]] 1.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6h0z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H0Z FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FHQ:~{N}-[(~{E})-(4-bromophenyl)methylideneamino]-2-(2~{H}-1,2,3,4-tetrazol-5-yl)ethanamide'>FHQ</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
[[Category: | <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=6h0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h0z OCA], [http://pdbe.org/6h0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h0z RCSB], [http://www.ebi.ac.uk/pdbsum/6h0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h0z 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: Large Structures]] | |||
[[Category: Heinemann, U]] | |||
[[Category: Link, A]] | |||
[[Category: Malecki, P H]] | |||
[[Category: Weiss, M S]] | |||
[[Category: Cancer]] | |||
[[Category: Epigenetic]] | |||
[[Category: Inhibitor design]] | |||
[[Category: Kdm4d]] | |||
[[Category: Ligand binding]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Tetrazole]] | |||
[[Category: Tetrazolylhydrazide]] | |||
Latest revision as of 18:24, 29 January 2020
Crystal Structure of KDM4D with tetrazolylhydrazide ligand NR067Crystal Structure of KDM4D with tetrazolylhydrazide ligand NR067
Structural highlights
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
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