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Figure 3.
Figure 3. Active site region of catechol oxidase. a, Stereo
view of the active site region with phenylthiourea bound to the
dicopper center. The sulfur of the inhibitor binds to both
copper ions. In addition the hydrophobic cavity formed by
residues Ile 241, His 244, Phe 261 provides van der Waals
contacts with the aromatic ring of the drug. A stick
presentation of the active site residues of the resting
Cu(II)-Cu(II) state of the enzyme is superimposed in light green
to reveal the conformational change induced by the binding of
PTU. b, Presentation of the molecular surface of the hydrophobic
binding cavity of catechol oxidase showing the two metal ions,
the inhibitor, and Phe 261 in a stick presentation. The
electrostatic surface has been generated omitting these
residues. Areas colored in pink have a negative potential and
areas in purple are of positive potential. c, A close-up of the
hydrophobic binding cavity of catechol oxidase. The images have
been computed using the programs SETOR^30 and SPOCK^31.
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