4URA

Crystal structure of human JMJD2A in complex with compound 14a

Summary for 4URA

• Entry DOI: 10.2210/pdb4ura/pdb
• Descriptor: LYSINE-SPECIFIC DEMETHYLASE 4A, 1,2-ETHANEDIOL, SULFATE ION, ... (7 entities in total)
• Functional Keywords: oxidoreductase, jumonjic, histone demethylase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus : O75164
• Total number of polymer chains: 2
• Total formula weight: 84591.95

Authors

Krojer, T.,England, K.S.,Vollmar, M.,Crawley, L.,Williams, E.,Riesebos, E.,Szykowska, A.,Burgess-Brown, N.,Oppermann, U.,Brennan, P.E.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.,von Delft, F. (deposition date: 2014-06-27, release date: 2015-06-17, Last modification date: 2024-05-08)

Primary citation

England, K.S.,Tumber, A.,Krojer, T.,Scozzafava, G.,Ng, S.S.,Daniel, M.,Szykowska, A.,Che, K.,von Delft, F.,Burgess-Brown, N.A.,Kawamura, A.,Schofield, C.J.,Brennan, P.E.
Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor.
Medchemcomm, 5:1879-1886, 2014

PubMed Abstract: A potent inhibitor of the JmjC histone lysine demethylase KDM2A (compound , pIC 7.2) with excellent selectivity over representatives from other KDM subfamilies has been developed; the discovery that a triazolopyridine compound binds to the active site of JmjC KDMs was followed by optimisation of the triazole substituent for KDM2A inhibition and selectivity.

PubMed: 26682034
DOI: 10.1039/C4MD00291A

Experimental method

X-RAY DIFFRACTION (2.23 Å)