Fig. 2: Structure of USP30 in complex with NK036.
a, Cartoon representation of the crystal structure of USP30ch3 bound to NK036. The compound is shown under an orange surface. b, Composite omit electron density map of NK036 in chain A (2mFo – DFc, contoured at 1σ, covering all atoms of the compound, created with simulated annealing from the final coordinates). See Extended Data Fig. 5e,f for unbiased mFo – DFc maps. c, Structure as in a with surface representation of USP30. d, Compound binding site highlighting typical USP regions involved in binding to NK036. These include the switching loop (yellow), blocking loop 1 (pink) and blocking loop 2 (red). Residues of the catalytic triad are shown as sticks. e, Close-up view of the compound binding site highlighting key residues involved in hydrogen bonding. f, Close-up view of the USP30 hydrophobic patch engaging the fluorobenzoyl moiety of the compound. g, Close-up view of hydrophobic interactions of the phenylalanine group of the compound. h, Close-up view of the benzenesulfonamide moiety of the compound engaged by USP30 residues.
