Fig. 2
The active sites of AusE-Mn/αKG and PrhA-Fe/αKG/5. a The active site of PrhA-Fe/αKG/5 showing the residues binding the Fe(II) ion and substrate 5. The active site is separated into three regions. Region L includes the 2-His-1-Asp triad binding Fe(II). Region B includes the residues interacting with the D-ring of 5. Finally, Region R includes residues surrounding the A/B-ring of 5. b Comparison of AusE-Mn/αKG and PrhA-Fe/αKG/5 active sites. Selected amino acid residues, co-substrate α-ketoglutarate (αKG, blue) and the substrate 5 (orange) are shown as stick models. Mn(II) or Fe(II) are shown as spheres with the label M. The active site structures of AusE and PrhA are highly similar, except for the three residues (150, 232, and 241) near the A/B-ring of 5. Residues derived from AusE (Leu150, Ser232, and Val241) and PrhA (Val150, Ala232, and Met241) are colored in yellow and orange, respectively
