3.6.4.B7	K+	Mg2+ als well as K+ ions are absorbed at the ATPase center. K+ (but not Na+), stimulates the ATP hydrolysis reaction with an apparent dissociation constant of about 40 mM. The strand exchange activity of the wild-type enzyme is also stimulated by potassium with an apparent dissociation constant of 35 mM	725699	
3.6.4.B7	KCl	stimulates the ATPase activity in the absence of ssDNA as well as the strand-exchange activity in the presence of AMPPNP	723824	
3.6.4.B7	Mg2+	ATP hydrolysis is not detected in presence of Mg2+	723283	
3.6.4.B7	Mg2+	Mg2+ als well as K+ ions are absorbed at the ATPase center	725699	
3.6.4.B7	Mg2+	required	722331, 725102, 733620, 734044, 756571, 756730, 757584, 757833, 757864	
3.6.4.B7	Mg2+	required for ATPase activity. The enzyme contains a secondary Mg2+ site as well as a canonical P-loop and nucleotide-lined primary Mg2+ site. The secondary Mg2+ site is important for modulating the ATPase activity	724274	
3.6.4.B7	Mg2+	required. A magnesium ion is observed in all nucleotide-bound structures. It is positioned in the same location in ATP and AMPPNP structures, co-ordinated by the beta- and gamma-phosphate groups and the hydroxyl group of Thr145. In the ADP structure, the Mg2+ ion is shifted slightly towards the beta-phosphate group, it is also co-ordinated by the beta-phosphate and the hydroxyl group of Thr145, in addition to four water molecules. The residue Glu174 likely activates a water molecule for hydrolysis of ATP. Glu174 forms an indirect interaction with the Mg2+ ion via a bridging water molecule. As magnesium is not present in the crystallisation conditions of RadA, the phosphate-bound form also lacks magnesium, but this appears to have little impact on the binding of the phosphate	756730	
3.6.4.B7	Mg2+	the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+	724905	
3.6.4.B7	Mn2+	the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+	724905	
3.6.4.B7	NaCl	20 mM NaCl used in this mixture was found to be optimal for ATP hydrolysis	725237	
3.6.4.B7	NH4Cl	stimulates the ATPase activity in the absence of ssDNA as well as the strand-exchange activity in the presence of AMPPNP	723824	
3.6.4.B7	RbCl	stimulates the ssDNA-dependent ATPase activity. 1.0 M RbCl does not stimulate the ATPase activity of MmRadA in the absence of DNA	723824