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![[Figure 5]](cb5088fig5mag.jpg)
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Figure 5
(a) An overlay of the structures of ERK5 in complex with compound 1 (C atoms in pink) and compound 2 (C atoms in green) highlights their similarity in binding mode. Hydrogen bonds between compound 2 and ERK5 are shown as black dashed lines. (b) Compound 3 binds to the ATP-binding site of ERK5, making hydrogen-bond interactions with the hinge (Met140), solvent channel (Asp143 and Gln146) and catalytic lysine (Lys84). The 2mFo − DFc OMIT electron density for compound 3 is shown as a lilac mesh contoured at 1.5σ. Hydrogen bonds are shown as dashed black lines. ERK5 and compound 3 are shown in stick representation with C atoms in grey. (c) Compounds 1, 2 and 3 show subtle differences in binding mode as a result of differences in their substitutions, although they utilize a similar aminopyrimidine hinge-binding motif. ERK5 is rendered as sticks with C atoms in grey (complex with compound 1). Compounds are rendered as sticks with C atoms in pink (compound 1), green (compound 2) or grey (compound 3). Leu137 (the gatekeeper residue), Leu139 in the hinge, the front pocket (FP) and the back pocket (BP) are labelled. |
![[Figure 5]](cb5088fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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