1.14.11.29	Ca2+	the crystal structure reveals an EF domain with two Ca2+-binding motifs inserted within the catalytic domain. The proximity of the EF domain to the active site suggests that Ca2+ binding is relevant to the catalytic activity. Functional analysis demonstrates that Ca2+-binding affinity of P4H-TM is within the range of physiological Ca2+ concentration in the endoplasmic reticulum. P4H-TM is found both as a monomer and a dimer in the solution, but the monomer-dimer equilibrium is not regulated by Ca2+	765073	
1.14.11.29	Fe2+	dependent on	724225, 724523, 724847, 726084	
1.14.11.29	Fe2+	dependent on, non-heme iron	725647, 725653	
1.14.11.29	Fe2+	required	701217, 725596, 741852	
1.14.11.29	Fe2+	required. the enzyme activity is inhibited by substitution of Fe2+ with Co2+ or Ni2+	701218	
1.14.11.29	Fe2+	the catalytic site contained bound Fe2+ and N-oxalylglycine	765073	
1.14.11.29	Fe2+	the enzyme contains Fe2+	701219	
1.14.11.29	Zn2+	the enzyme contains a zinc finger motif	743285