1.13.11.50	Cu2+	sulfate, similar binding as Fe2+ in wild-type enzyme	696107	
1.13.11.50	Fe2+	0.9-1.0 iron atoms per subunit, bound to active enzyme, essential for catalytic activity	636327	
1.13.11.50	Fe2+	active site nonheme monoiron(II) center, facially ligated by three histidine residues, overview. Spectral analysis of Dke1 FeII-alpha-keto acid complexes with 4-hydroxyphneylpyruvate, overview	725198	
1.13.11.50	Fe2+	Dke1 contains an atypical, three-histidine-ligated, mononuclear non-heme Fe2+ center, spectroscopic analysis, overview. Stabilizing effect of Glu98 on the 6C geometry of the metal center, priming it for substrate ligation. Also Thr107 stabilizes the Fe(II) cofactor	711267	
1.13.11.50	Fe2+	essential for activity	671683	
1.13.11.50	Fe2+	Fe2+-dependent enzyme, 1 molecule per subunit	675466	
1.13.11.50	Fe2+	its active site consists of a redox-active iron(II) center	764545	
1.13.11.50	Fe2+	nonheme Fe(II) cofactor, distinct organization of the hydrophilic triad in the free and substrate-ligated wild-type enzyme. In the free species, the Fe(II) center is coordinated to three histidines and one glutamate, whereas the substrate-ligated, catalytically competent enzyme-substrate complex has an Fe(II) center with three-histidine coordination, with a small fraction of three-histidine, one-glutamate coordination	725553	
1.13.11.50	Fe2+	sulfate, necessary for enzyme activity. About 0.9 mol Fe2+/mol wild-type enzyme, less than 5% Fe2+ in mutants except 0.27 mol/mol H104E-enzyme and 0.45 mol/mol H104N-enzyme	696107	
1.13.11.50	Fe2+	the Fe(II) coordinating triad is composed of three His residues, geometric and electronic structure of the Fe(II) center, structure and function comparison with other dioxygenases containing a two histidines and a carboxylate coordinating the iron center in a facial triad, overview	711258