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Figure 4.
Figure 4 Details of the water structure. (a) The water
structure at the solvent-exposed edge of a pocket of hydrophobic
residues is shown. Water molecules shown in red (470, 527, 569,
614 and 1709) participate in a water pentamer. The pentamer
fills the groove along the surface of the protein that is formed
by the side chains of residues extending into the hydrophobic
pocket below the surface. Hydrogen bonds made among the members
of the pentamer are shown as red dotted lines and hydrogen bonds
from pentamer members to protein residues are shown as black
dotted lines. The surrounding water structure and the hydrogen
bonds these waters make are shown in blue. Alternate
conformations of protein and water molecules in this region are
omitted for clarity. (b) Stereo image of the acetate molecule
bound within the active site in structure I, the waters in
structure II that occupy the space of the acetate (superimposed,
yellow) and the residues which hydrogen bond to them. Hydrogen
bonds from the acetate O atoms are shown as red dotted lines and
the waters of structure II are shown in yellow, as are the
dotted lines representing the hydrogen bonds they make with each
other and with protein atoms.
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