Structural characterization of core-bradavidin in complex with biotin
Fig 5
Comparison of Asp40 in core- (orange; bold labels) [PDB:4BBO] and wt bradavidin (magenta; labels in brackets) [PDB:2Y32].
In core-bradavidin (a), the side chain of Asp40 is flipped to an opposite direction as compared to wt bradavidin (b). Biotin (a) and residues K132 and L133 (b) occupying the same space as biotin in core-bradavidin (see a) are shown as spheres. Non-carbon atoms are coloured as in Fig 2. H-bonds are shown as dashed lines; distances in Ångströms. The weighted 2Fo-Fc electron density map around Asp40 (a, b) is shown as a blue mesh (contour level of 1.0 σ).