the zinc ion of the metalloenzyme is coordinated by a conserved binding triad of amino acids consisting of one aspartate and two histidine residues, determination of the metal-binding site, which is essential for the enzyme's catalytic activity, one metal site per monomer, structure and quantum chemical calculations of models, overview. The metal ion occupies a tetrahedral environment with binding to one of the carboxylic oxygen of Asp14, His86, His90 and a water molecule
metal site models show an intrinsic preference for zinc, but also significant flexibility of the site so that binding of other ions can eventually occur, e.g. Fe2+, Co2+, Cu2+, Mg2+, quantum chemical calculations, overview
metal site models show an intrinsic preference for zinc, but also significant flexibility of the site so that binding of other ions can eventually occur, e.g. Fe2+, Co2+, Cu2+, Mg2+, quantum chemical calculations, overview
SpPgdA is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively
SpPgdA is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively