Skip to main content
Fig. 2 | Bioresources and Bioprocessing

Fig. 2

From: Structure-guided engineering of a flavin-containing monooxygenase for the efficient production of indirubin

Fig. 2

Docking analysis of bFMO–indole complex, showing the location of active pocket residues (red), substrate tunnel residues (green) and the loop (blue) connected the α4 helix (purple), which have been targeted for mutagenesis. The FAD-binding domain (residues 1–164 and residues 276–445) is shown in yellow; the NADPH-binding domain (residues 165–275) is shown in green. The residues of the substrate tunnel (green) and the active pocket (red) are represented as spheres. The cofactors FAD (orange) and substrate indole (cyan) are represented as sticks. a Six residues located at active pocket within 8 Å with the indole, shown in red sticks. b Seven residues located at substrate tunnel, shown in green sticks. c Loop (residues 220–223, blue) connected with the α4 helix (purple). The π–π stacking interaction in the active pocket of bFMO, as shown in yellow lines

Back to article page