4.6.1.12	Co2+	preferred	708124	
4.6.1.12	Mg2+	dependent on	656498	
4.6.1.12	Mg2+	Mg2+ or Mn2+ are required	655417	
4.6.1.12	Mg2+	Mg2+ or Mn2+, positioned between the alpha- and beta-phosphates of the substrate, acts in concert with the Zn2+ to align and polarize the substrate for catalysis	709435	
4.6.1.12	Mg2+	Mn2+ or Mg2+ required	657177	
4.6.1.12	Mg2+	preference	708124	
4.6.1.12	Mg2+	preferred	708124	
4.6.1.12	Mn2+	-	663548	
4.6.1.12	Mn2+	a Mn2+ with octahedral geometry, is positioned between the alpha and beta phosphates acting in concert with the Zn2+ to align and polarize the substrate for catalysis	657196	
4.6.1.12	Mn2+	Mg2+ or Mn2+ are required	655417	
4.6.1.12	Mn2+	Mg2+ or Mn2+, positioned between the alpha- and beta-phosphates of the substrate, acts in concert with the Zn2+ to align and polarize the substrate for catalysis	709435	
4.6.1.12	Mn2+	Mn2+ or Mg2+ required	657177	
4.6.1.12	Mn2+	preferred	708124	
4.6.1.12	additional information	the tetrahedrally arranged transition metal binding site, potentially occupied by Mn2+, sits at the base of the active site cleft. A phosphate oxygen of 2-C-methyl-D-erythritol-2,4-cyclodiphosphate and the side chains of Asp8, His10, and His42 occupy the metal side chains of Asp8, His10, and His42 occupy the metal side coordination sphere	656112	
4.6.1.12	Na+	presence of tetrahedral Zn2+ in one of the metal-binding sites and an octahedral sodium ion in the second metal site in absence of substrate	654130	
4.6.1.12	Zinc	tightly binds one zinc ion per subunit of the trimer at the active site, which helps to position the substrate for direct attack of the 2-phosphate group on the beta-phosphate	656498	
4.6.1.12	Zn2+	-	663548	
4.6.1.12	Zn2+	active site contains a Zn2+ with tetrahedral coordination	657196	
4.6.1.12	Zn2+	active site including a Zn2+ ligand (Asp92-His94-His126)	709487	
4.6.1.12	Zn2+	presence of tetrahedral Zn2+ in one of the metal-binding sites and an octahedral sodium ion in the second metal site in absence of substrate	654130	
4.6.1.12	Zn2+	Zn2+-binding site, addition of a Zn2+-binding moiety may prove valuable in assisting the design of potent and selective inhibitors	709435