Figure 2
(a) Close-up stereoview of the active site with the inhibitor phosphoramidon (magenta) that was soaked into the crystals. It displays the typical binding mode of phosphoramidates to TLP. (b) Superposition of phosphoramidon bound to the neutral proteases Gentlyase (pink) and thermolysin (green) shows the overall good agreement of the Trp, Leu and phosphoramidate moieties of the inhibitors. In the Gentlyase crystal a different conformation of the rhamnose moiety is observed that forms a hydrogen bond across a crystal lattice contact to Asn215 of another protein chain (cyan) and displaces the Tyr150 side chain.  [article HTML]