Fig. 4: The reverting mutations.
From: Evolution of enzyme functionality in the flavin-containing monooxygenases
a Model of tAncFMO1–4 with 4′× (I60T, N222S, H275N, H426N) residues shown in green. b, c Focused views with 4′× residues labeled. The distances between an H at the Cγ1 of the I60 side chain and the O at the C4 of the FAD (2.6 Å) and between the Nε2 of H275 and the Cε1 of H426 with two O atoms of the phosphate moiety of NADP+ (6.7 and 3.3 Å), respectively, are shown. d Hydrogen bonding interactions for I60 are shown in light blue. e Hydrogen bonding interactions for H275 and H426 are described in light blue. tAncFMO1–5 secondary structure and residues are shown in purple. FAD and NADP+ molecules are depicted in yellow and blue, respectively.
