Those structures reveal that Ag+ binds to 6PGDH at both catalytic and non-catalytic sites with dominant binding residues of Cys, His and Met in quasi-linear and trigonal geometry, which is generally consistent with our previous reports36,40. Together with the site-directed mutagenesis study, we unveil that Ag+ abolishes the enzymatic activity of 6PGDH through targeting His185 in the active site and morphing its catalytic pocket.