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Figure 3.
Figure 3. Stereoviews of the active site of the R236_PAM
structure. (a) A simulated annealing 2F[o]−F[c] electron
density map, contoured at 1.8σ, with PAM (magenta) omitted from
the map calculation. Overlaid onto the electron density map are
the refined positions of the residues. (b) Overlay of the
active sites of the C1 (carbon atoms in light gray) and C6
(carbon atoms in dark gray) chains of the R[236_PAM] structure.
The interactions between the enzyme and PAM in the C1 chain are
shown as dotted lines. An asterisk after the residue number
indicates that the residue is donated from the adjacent C2
chain. Figure 3. Stereoviews of the active site of the
R236_PAM structure. (a) A simulated annealing 2F[o]−F[c]
electron density map, contoured at 1.8σ, with PAM (magenta)
omitted from the map calculation. Overlaid onto the electron
density map are the refined positions of the residues. (b)
Overlay of the active sites of the C1 (carbon atoms in light
gray) and C6 (carbon atoms in dark gray) chains of the
R[236_PAM] structure. The interactions between the enzyme and
PAM in the C1 chain are shown as dotted lines. An asterisk after
the residue number indicates that the residue is donated from
the adjacent C2 chain.
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