4d6r
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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" 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.398Å</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'>[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> | <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 == | ||
| - | + | [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== | ||
Current revision
crystal structure of human JMJD2D in complex with N-OXALYLGLYCINE and bound o-toluenesulfonamide
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Bountra C | Bradley A | Burgess-Brown N | Crawley L | Edwards A | Gileadi C | Johansson C | Krojer T | Oppermann U | Szykowska A | Vollmar M | Von Delft F
