Figure 4.
FIG. 4. Dhurrin bound in the active sites to SbDhr1-E189D
and glucotetrazole bound to ZmGlu1-E191D. A, electron density
surrounding the dhurrin molecule in the active site of
SbDhr1-E189D. The 2F[o] - F[c] Fourier difference maps at the
final stage of refinement are shown contoured at 1 above
the mean density. B, a slice in the surface representation of
SbDhr1 in complex with dhurrin showing the cyano group-binding
pocket. The dipole moment of the polar pocket, calculated with
GRASP (28), coincides with that of the cyano group. C, electron
density around the glucotetrazole molecule in the active site of
ZmGlu1-E191D. The F[o] - F[c] Fourier difference maps before
refinement are shown, calculated using only the enzyme model
phases without substrate, contoured at 2.5 above the mean density.
D, superimposition of the active sites of myrosinase (blue) and
ZmGlu1 (yellow), both in complex with the glucotetrazole
inhibitor molecule.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
31796-31803)
copyright 2004.
above
the mean density. B, a slice in the surface representation of
SbDhr1 in complex with dhurrin showing the cyano group-binding
pocket. The dipole moment of the polar pocket, calculated with
GRASP (28), coincides with that of the cyano group. C, electron
density around the glucotetrazole molecule in the active site of
ZmGlu1-E191D. The F[o] - F[c] Fourier difference maps before
refinement are shown, calculated using only the enzyme model
phases without substrate, contoured at 2.5