“…The loops that surround the active pocket of most trypsinlike serine proteases have been shown to prominently mediate many interactions between the protease and biomolecules such as cofactors, substrates, and cognate inhibitors (Bode, Turk, & Karshikov, 1992;Dementiev et al, 2018;Horrevoets, Tans, Smilde, van Zonneveld, & Pannekoek, 1993;Madison, Goldsmith, Gerard, Gething, & Sambrook, 1989). As such, the binding of BEN could somewhat interfere with the dynamics of the binding pocket residues in its effort to inactivate β-FXIIa.…”