Figure 9. Unanticipated covalent adducts at previously reported allosteric sites only at room temperature (RT).

(A) RT structure with the fragment covalently bound to both K197 and K237 (z0048, red), aligned with cryogenic (cryo) structure with a previously reported allosteric inhibitor covalently bound to K197C (6b95, green). (B) Fragment bound to K197 at the 197 allosteric site, with RT event density at 1.5 σ. (C) Fragment bound to K237 at the L16 allosteric site, with RT event density at 1.5 σ.

Figure 9—figure supplement 1. Conformational difference for the active-site P loop.

(A) 180° rotation around the vertical axis of main Figure 9A, to view the backside of z0048 (red) aligned with 6b95 (green). The WPD loop remains open, but the P loop and the nearby substrate-binding loop adopt different conformations. (B) z0048 aligned with 6b95 and a structure with Cys215 in the P loop oxidized, PDB ID 1oes (orange). Room temperature (RT) event density is shown at 1.5 σ (red mesh). The new loop conformation at RT matches 1oes, not 6b95.