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. Author manuscript; available in PMC: 2010 Jul 20.

Published in final edited form as: Dalton Trans. 2008 Jun 27;(38):5132–5142. doi: 10.1039/b803512a

Fig. 7 — Structure of the histone demethylase JMJD2A (PDB 2p5b). (A) The overall view of the histone demethylase, with bound zinc shown as a grey sphere, the peptide substrate shown with pink carbons, and the αKG homologue N-oxalylglycine replacing the cosubstrate. (B) The active site of JMJD2A with just the trimethyl-Lys portion of the substrate shown. The coloring scheme is the same above.

Fig. 7 — Structure of the histone demethylase JMJD2A (PDB 2p5b). (A) The overall view of the histone demethylase, with bound zinc shown as a grey sphere, the peptide substrate shown with pink carbons, and the αKG homologue N-oxalylglycine replacing the cosubstrate. (B) The active site of JMJD2A with just the trimethyl-Lys portion of the substrate shown. The coloring scheme is the same above.