2.7.1.B20	Co2+	enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)	727430	
2.7.1.B20	Co2+	enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+	697882	
2.7.1.B20	Co2+	kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+	728780	
2.7.1.B20	Mg2+	enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)	727430	
2.7.1.B20	Mg2+	enzyme activity requires the presence of divalent cations. Mn2+ is the most efficient, followed by Mg2+, Ni2+ and Co2+. Maximum activity is attained when the ATP/Mg2+ concentration ratio is 0.5	697882	
2.7.1.B20	Mg2+	kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+	728780	
2.7.1.B20	Mg2+	there are two magnesium-binding sites per subunit: one Mg2+ (MO6) is coordinated octahedrally by six water molecules and is located between adenosine and AMPPNP in the active site and one Mg2+ (MO5) is coordinated by five water molecules and is positioned in the interface between the dimers in the crystal	726575	
2.7.1.B20	Mn2+	enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)	727430	
2.7.1.B20	Mn2+	kinase activity is observed with Mg2+ and Co2+ and to a lesser degree with Mn2+	728780	
2.7.1.B20	Ni2+	enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)	727430