Fig. 4
From: Unusual substrate and halide versatility of phenolic halogenase PltM
Crystal structures of PltM. a Full view of the structure of PltM with the conserved halogenase fold in pale yellow and the unique C-terminal region in orange. The red loop indicates the N-terminal unconserved region after the 3rd β-sheet. The substrate binding region is shown by a box. b A zoomed in view of the substrate binding site of the structure of PltM-compound 1 complex (yellow sticks). Residues lining the substrate binding pocket are shown as gray sticks and the mFo–DFc polder omit map contoured at 5.5σ is shown by the gray mesh. c The FAD bound in the holoenzyme state of PltM. d The FAD bound in a putative FAD binding intermediate state. FAD is represented as turquoise sticks in panels c and d. The flexible loop that changes conformation upon FAD binding is shown in brown. Key FAD interacting residues are shown as sticks. Bound Cl− and water are shown as green and salmon spheres, respectively
