Figure 2.
FIGURE 2. Interactions between FMN and amino acid residues
in the active site. a, schematic diagram showing contacts of the
FMN cofactor to amino acid residues. Hydrogen bonds are shown as
broken green lines (red residue numbers) and van der Waals'
interactions by red shading (black residue numbers). Each atom
element is represented by a sphere of different colors with a
chemical symbol. b, SIGMAA-weighted 2mF[o] - DF[c] electron
density maps surrounding the FMN. The map was calculated using
the data of P4[2]2[1]2 crystal structure and is contoured at 1.2
.
c, the electrostatic potential of AzoR is mapped onto the
solvent-accessible surface, as calculated with GRASP. The FMN
molecules shown in a and b are represented by a stick model,
with color coding identical to that in Fig. 1.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
20567-20576)
copyright 2006.
.
c, the electrostatic potential of AzoR is mapped onto the
solvent-accessible surface, as calculated with GRASP. The FMN
molecules shown in a and b are represented by a stick model,
with color coding identical to that in Fig. 1.