Figure 3.
Figure 3 Mutation site in the K206E/K296E double mutant. (a)
Bias-removed OMIT density (F[o] - F[c], contoured at 3 )
for the mutated residues. (b) Side chains of Glu206 and Glu296
in the mutant structure, shown in gold, superimposed on Lys206
and Lys296 in the wild-type structure, shown in silver. Other
residues common to both proteins are shown in green with atoms
coloured by type. Hydrogen bonds are shown as broken lines and
covalent metal-ligand bonds as solid black lines.
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2007,
63,
408-414)
copyright 2007.
)
for the mutated residues. (b) Side chains of Glu206 and Glu296
in the mutant structure, shown in gold, superimposed on Lys206
and Lys296 in the wild-type structure, shown in silver. Other
residues common to both proteins are shown in green with atoms
coloured by type. Hydrogen bonds are shown as broken lines and
covalent metal-ligand bonds as solid black lines.