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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.
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