Figure 5 - full size

Figure 5. Figure 5. (a) Geometry of the catalytic triad site. (b) Stereo view of the catalytic site in the vicinity of the K167 side-chain. The lysine amino group interacts with a cluster of five water molecules filling a hydrophilic cavity. (c) Stereo view of the substrate binding site. DHQ is wrapped up by the N and C-terminal parts of the protein: contacts are established via hydrophilic interactions or hydrophobic residues of both N and C-terminal domains. The color code is the same as in the legend to Figure 4. Figure 5. (a) Geometry of the catalytic triad site. (b) Stereo view of the catalytic site in the vicinity of the K167 side-chain. The lysine amino group interacts with a cluster of five water molecules filling a hydrophilic cavity. (c) Stereo view of the substrate binding site. DHQ is wrapped up by the N and C-terminal parts of the protein: contacts are established via hydrophilic interactions or hydrophobic residues of both N and C-terminal domains. The color code is the same as in the legend to [3]Figure 4.