4d6r: Difference between revisions

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<StructureSection load='4d6r' size='340' side='right'caption='[[4d6r]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='4d6r' size='340' side='right'caption='[[4d6r]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4d6r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D6R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D6R FirstGlance]. <br>
<table><tr><td colspan='2'>[[4d6r]] 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=4D6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D6R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IEJ:O-TOLUENESULFONAMIDE'>IEJ</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.398&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d6q|4d6q]], [[4d6s|4d6s]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IEJ:O-TOLUENESULFONAMIDE'>IEJ</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6r OCA], [http://pdbe.org/4d6r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d6r RCSB], [http://www.ebi.ac.uk/pdbsum/4d6r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d6r ProSAT]</span></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=4d6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6r OCA], [https://pdbe.org/4d6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d6r RCSB], [https://www.ebi.ac.uk/pdbsum/4d6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d6r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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>  


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Bradley, A]]
[[Category: Bradley A]]
[[Category: Burgess-Brown, N]]
[[Category: Burgess-Brown N]]
[[Category: Crawley, L]]
[[Category: Crawley L]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Gileadi C]]
[[Category: Gileadi, C]]
[[Category: Johansson C]]
[[Category: Johansson, C]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Oppermann U]]
[[Category: Oppermann, U]]
[[Category: Szykowska A]]
[[Category: Szykowska, A]]
[[Category: Vollmar M]]
[[Category: Vollmar, M]]
[[Category: Von Delft F]]
[[Category: Demethylase/2og]]
[[Category: Flj10251]]
[[Category: Jumonji domain containing 2d]]
[[Category: Kdm4d]]
[[Category: Mgc141909]]
[[Category: Transcription]]

Latest revision as of 14:18, 9 May 2024

crystal structure of human JMJD2D in complex with N-OXALYLGLYCINE and bound o-toluenesulfonamidecrystal structure of human JMJD2D in complex with N-OXALYLGLYCINE and bound o-toluenesulfonamide

Structural highlights

4d6r 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 1.398Å
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

4d6r, resolution 1.40Å

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