2OS2

Crystal structure of JMJD2A complexed with histone H3 peptide trimethylated at Lys36

Summary for 2OS2

• Entry DOI: 10.2210/pdb2os2/pdb
• Related: 2OQ6 2OQ7 2OT7 2OX0
• Descriptor: JmjC domain-containing histone demethylation protein 3A, histone 3 peptide, NICKEL (II) ION, ... (6 entities in total)
• Functional Keywords: fe, double-stranded beta helix, demethylase, oxygenase, structural genomics, structural genomics consortium, sgc, oxidoreductase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: O75164
• Total number of polymer chains: 4
• Total formula weight: 91745.92

Authors

Kavanagh, K.L.,Ng, S.S.,Pilka, E.,McDonough, M.A.,Savitsky, P.,von Delft, F.,Arrowsmith, C.H.,Weigelt, J.,Edwards, A.,Sundstrom, M.,Schofield, C.J.,Oppermann, U.,Structural Genomics Consortium (SGC) (deposition date: 2007-02-05, release date: 2007-03-13, Last modification date: 2023-08-30)

• Primary citation: Ng, S.S.,Kavanagh, K.L.,McDonough, M.A.,Butler, D.,Pilka, E.S.,Lienard, B.M.,Bray, J.E.,Savitsky, P.,Gileadi, O.,von Delft, F.,Rose, N.R.,Offer, J.,Scheinost, J.C.,Borowski, T.,Sundstrom, M.,Schofield, C.J.,Oppermann, U.; Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.; Nature, 448:87-91, 2007; PubMed: 17589501; DOI: 10.1038/nature05971

Experimental method

X-RAY DIFFRACTION (2.3 Å)