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Figure 2.
FIG. 2. Stereo view of the active site, primary specificity
pocket, and Na^+-binding site of the thrombin mutant WE. The
PPACK-inhibited WE structure (blue) is superimposed to the SL
structure (red) of the wild type (15). Notwithstanding the
drastic difference in atomic resolution (2.4 Å for
WE-PPACK and 1.55 Å for SL), the two structures are
remarkably similar overall (r.m.s. deviation = 0.4 Å).
There is no evidence of bound Na^+ in the WE-PPACK structure,
and there is a notable 1:1 correspondence for the water
molecules in the Na^+ site between the two structures. Relevant
side chains are labeled. In the WE structure, the side chain of
Lys-224 moves away from residue 217 because of the E217A
mutation.
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