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Figure 3
Structural characterization of KDM4A in JmjC family. (a) Cartoon representation of FTO in complex with cofactor Ni2+, cosubstrate αKG and catalytic substrate H3K9me3 (PDB code: 2q8c ). Ni2+ is shown as green sphere. αKG and H3K9me3 are shown in sticks with carbon in green and yellow, respectively. The structural domains are indicated in similar color. Connected domain: the region that connecting JmjN domain to JmjC domain. (b) Close-up view of the coordination of the cosubstrate αKG (PDB code: 2q8c ) and 2OG-based inhibitors NOG/R-2HG (PDB codes: 2oq6 and 2ybk ) in the active sites of KDM4A. The hydrogen bonds between KDM4A residues with Ni2+ or αKG are displayed as dashed lines. (c) Close-up view of the coordination of the catalytic substrate H3K9me3. The C—H⋯O hydrogen bonds, formed by one methyl group of methylated lysine and the oxygen atoms from active-site residues are displayed as dashed blue lines.

IUCrJ
Volume 1| Part 6| October 2014| Pages 540-549
ISSN: 2052-2525
doi:10.1107/S2052252514020922