Characterization of a Pathogenic Variant in the ABCD1 Gene Through Protein Molecular Modeling

Figure 3

ABCD1 molecular model for full-length human sequence for variant p.K533E. (A) Full-length dimeric model for the entire wild type (WT) ABCD1 structure shown as ribbon structure with VdW sticks for position 533. (B) Zoom-in on the wild-type for the Lys533 residue from the full-length model to better show the interacting residues and dimer interface. Monomer 1 is gray and monomer 2 is orange. The residues within interaction distance to K533 are shown and yellow dash line is H-bonds and pink dash line is salt bridges. (C) Zoom-in on the region around Glu533 variant, showing nearby residues and the resulting distortion of the “pocket” around E533 due to the charge flipping (+ to −).