Skip to main content
. 2017 Jul 22;18(7):1593. doi: 10.3390/ijms18071593

Figure 3.

Figure 3

Structural model of human ABCD1. (A) Ribbon representation of the ABCD1 monomer. TMD helices are numbered from 1 to 6 and rainbow colored from dark blue to red. NBD is in light grey; (B) Ribbon representation of the ABCD1 homodimer with the two subunits respectively colored in dark blue and yellow; (C) Cytoplasmic view of a 32 Å cross-section of the ABCD1 TMD (with the two subunits respectively colored in dark blue and yellow) showing the TMHs organization. Transmembrane helices of each subunit are numbered from 1 to 6 for one monomer (yellow) and from 1′ to 6′ for the second monomer (dark blue). Red lines contour the two putative “supra-domains” at the interface of which the substrate could access the center of the TMD; (D) Ribbon representation of hydrophobic interactions between TMH 2 (in yellow) and TMH 5′ (in dark blue), sidechains of interacting amino acids are shown in CPK colored sticks. The PDB file of the model and the alignment of ABCD1 with ABCB10 are available in supplementary material and in Appendix A (Figure A1) respectively.