IndraLab
Statements
reach
"Computational protonation state analysis with PropKa (Søndergaard et al, 2011) suggests that the proximity of both side chains leads to a doubly protonated H261 thereby rendering engagement in multiple bonds with E366 and with the AZ1 trifluoro-methyl group possible.VSM and FT206 bind to USP28 at similar sites located further towards the wider and open Ub-tail proximal position of the USP28-inhibitor-binding cleft (Fig. 1A,B)."
reach
"AZ1, VSM, and FT206 bind to USP28 at different overlapping positions inside the same hydrophobic cleft, located at the intersection of the USP-thumb and palm subdomains in the center of the concave part of the USP S1-site, which acts as a binding surface for the globular domain of the distal Ub moiety of the cleaved substrate (Figs."