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. 2022 Oct 17;19(2):159–167. doi: 10.1038/s41589-022-01147-8

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Fig. 3 — a, A 2.7-Å resolution structure of ClbP crystallized in the presence of 1 shows the compound (cyan sticks) bound in the expected pocket of the active site near the catalytic triad. Continuous electron density in the polder difference map contoured at 7σ (gray mesh) indicates the inhibitor is covalently bound to S95. b, A 90° rotation relative to a details the 2F_o–F_c density map contoured at 1σ for the inhibitor and proximal residues. N331 mediates recognition of the d-Asn side chain. c, The boronate ester, a structural mimic of the tetrahedral intermediates in colibactin hydrolysis, is stabilized by hydrogen bonds from Q330 and Y186.