Fig. 10

3D models of wildtype and mutated biotinidase. a. 3D biotinidase model generated by I-TASSER (A, left). Pink residues (57–363) designate the CN-Hydrolase domain whereas the blue residues (1-41) designate the signal peptide. Effect of p.R209C and p.H447R mutations on protein structure (a, middle, right). Btd ^WT (left) is compared to p.R209C (middle) and p.H447R (right) in means of changes in secondary structure (no change, black; helix to strand, light green; strand to helix, dark green; helix to coil, light red; strand to coil, dark red; coil to strand or helix, green). The mutated R209 and H447 residues are depicted with blue Van Der Waals radii and their POLYPHEN2/SIFT scores and residual enzyme activity are indicated. Comparison of MODICT scores and residual enzyme activity, b. MODICT scores from models generated by I-TASSER (negative control, 0.096 ; p.R209C, 0.266 ; p.H447R, 0.584) and PHYRE2 (negative control, 0.301 ; p.R209C, 0.504 ; p.H447R, 1.102) were compared with experimentally measured enzyme activity (wildtype 263eu, p.R209C, 91eu, p.H447R, 61eu) scaled to 1. Ratios of MODICT scores and [1/enzyme activity] are in concordance with each other. (W = wildtype, W ^R = refined wildtype)