Structures of aminophenol dioxygenase in complex with intermediate, product and inhibitor

Li, D.-F.; Zhang, J.-Y.; Hou, Y.-J.; Liu, L.; Hu, Y.; Liu, S.-J.; Wang, D.-C.; Liu, W.

doi:10.1107/S0907444912042072

Figure 6
Comparison of Fe-ligand coordination geometry at the active site prior to O₂ binding in some 2-His-1-carboxylate enzymes. (a) The APD-4NC complex structure, (b) the 4,5-PCD structure (PDB entry 1b4u ; Sugimoto et al., 1999

), (c) HPCD (PDB entry 2iga ; Kovaleva & Lipscomb, 2007

) and (d) the [alpha]

-KG-dependent enzyme clavaminate synthase (CAS- [alpha]

-KG-PCV; PDB entry 1drt ; Zhang et al., 2000

). Schematic representations of the Fe-coordination scheme are shown in the middle and simplified representations showing Fe coordination with two O^- anions from the carboxylic side chain of the Glu residue and a hydroxyl substituent of the bound ligand are shown at the bottom.