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Figure 4.
Figure 4. Effect of the D422G mutation. (a) Superposition of
the structures of ΔΔI[hh]-SM (green) and ΔΔI[hh]-CM (red).
(b) Detailed comparison of the area of residue 422. Water
molecules in this area are shown as spheres, light green for
ΔΔI[hh]-SM and rose for ΔΔI[hh]-CM. In ΔΔI[hh]-CM, two
water molecules are found bound tightly to the protein in the
area of the missing Asp422 side-chain. Figure 4. Effect of
the D422G mutation. (a) Superposition of the structures of
ΔΔI[hh]-SM (green) and ΔΔI[hh]-CM (red). (b) Detailed
comparison of the area of residue 422. Water molecules in this
area are shown as spheres, light green for ΔΔI[hh]-SM and rose
for ΔΔI[hh]-CM. In ΔΔI[hh]-CM, two water molecules are found
bound tightly to the protein in the area of the missing Asp422
side-chain.
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