Fig. 6: Inhibition of USP30 by NK036 uses a ligandability hotspot and a cryptic pocket, distinct from other USP DUB inhibitors. | Nature Structural & Molecular Biology

Fig. 6: Inhibition of USP30 by NK036 uses a ligandability hotspot and a cryptic pocket, distinct from other USP DUB inhibitors.

From: Chimeric deubiquitinase engineering reveals structural basis for specific inhibition of the mitophagy regulator USP30

Fig. 6

a–g, Cartoon representations of human USP family DUB catalytic domains in complex with the indicated small-molecule inhibitors (USP7 and compound 2 (PDB 5N9R; a), USP7 and GNE6776 (PDB 5UQX; b), USP14 and IU1-206 (PDB 6IIM; c), USP28 and FT206 (PDB 8P1Q; d), USP1 and ML323 (PDB 7ZH4; e), USP7 and compound 23 (PDB 6VN3; f), USP30 and NK036 (g)). Compounds are shown as both sticks and transparent surfaces. Structural elements of DUBs are labeled, and PDB codes of structures are given44,45,48,54,56,57. The Leu73 ubiquitin binding site is shown with an arrow when engaged by compounds. h, Comparison of USP30 inhibition by NK036 to other DUB inhibitors. Superposition of the structure of USP30 + NK036 on other structures shown in a–f. Compounds are shown as surfaces and are labeled. All USP cartoons except USP30 are semitransparent.

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