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Figure 5 | BMC Structural Biology

Figure 5

From: Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames)

Figure 5

Position of residues taking part in intermonomer contacts is highly conserved among various Alrs, despite differences in hinge angles. Following a structural alignment of the N-terminal domains of various Alrs, the position for the Cα atoms from residues that take part in intermonomer contacts and are in the N-terminal domain (shown as colored spheres) was plotted on the main chain representation of Alr Bax (shown in green). Likewise, the position for the Cα atoms from residues that take part in intermonomer contacts and are at the C-terminal domain (shown as colored spheres) were plotted on the main chain representation of Alr Bax after a structural alignment of the C-terminal domains of various Alrs. Residues are colored according to the legend on figure 3. The PLP cofactor from Alr Bax is shown as a ball and stick model. N and C indicate the position of the C- and N-termini in the monomer.

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