Atomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole

Crystal structures of wild-type L. enzymogenes LysC and of the K30R variant near the substrate-binding site have been determined in complex with the covalent inhibitor TLCK that mimics a tetrahedral reaction intermediate. H-atom density indicates a hydroxyl group in the oxyanion hole.