Fig. 3. (A) Stereo image of FadR–myristoyl-CoA structure and ligand electron density. A C_α trace is shown, coloured according to secondary structure. Helices are coloured red (DNA binding domain) or blue (acyl-CoA binding domain), strands green and turns grey. Secondary structure elements are labelled. The ligand, myristoyl-CoA, is shown as a stick model with carbons coloured black. A simulated annealing F_o – F_c map is also shown, contoured around the ligand at 2.25 σ (green). (B) Stereo image of protein–ligand interactions. The protein backbone is shown as a blue trace. Side chains touching the ligand (contact distance less than the sum of van der Waals radii + 0.5 Å) are shown as sticks coloured by atom type. Myristoyl-CoA is shown as a stick model with carbons coloured black. Water molecules interacting with the ligand are shown as green spheres. Hydrogen bonding with the ligand is indicated by black dashed lines.