Figure 1.

(a) Overview of the α/β hydrolase fold shared by all Fph proteins. Shared and unique features color coding illustrated. (b) Molecular size and hydrolase domain Pfam family association for FphA-J. Grey box represents the predicted size of the hydrolase domain with unique helices in cyan. (c) FphF structure as an example of the hydrolase domain (PDB ID 6VH9). Active site triad residues in black with hydrogen bonds as red dotted lines. α helices in purple, active site helices marked black. Core β-strands in red. (d) FphF KT130 inhibitor bound to the hydrophobic active site pocket. Residues of this pocked in purple, with active site triad and covalent bound KT130 in black.