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Figure 3
The active site. (a) A view into the narrow active-site cleft of the wild-type enzyme. The van der Waals radii are depicted as a grey semi-transparent surface. Residues are shown as sticks coloured by atomic position (purple, C; red, O; blue, N; yellow, S). Red spheres are waters. Three key catalytic residues are labelled. (b) Superposition of the wild-type and C164Q mutant active sites. The same colour scheme for atoms is used as in (a) except that the C atoms of the mutant are in orange. As a result of the C164Q mutation, Phe400 rotates out of the binding pocket.

ISSN: 2053-230X
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