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. 2008 Apr 4;283(14):9435–9443. doi: 10.1074/jbc.M709135200

FIGURE 1.

FIGURE 1.

A, ribbon diagram of the overall fold of the human VLCAD dimer. The monomers are represented in cyan and blue. The FADs are shown in yellow, and a partial model of C14-CoA is shown in magenta. The C-terminal domain is marked near the bottom of the figure. B, overall polypeptide fold of a VLCAD monomer showing the N-terminal α-dom1 (blue), the β-sheet domain (gold), α-dom2 (cyan), and the C-terminal α-dom3 (green). The FAD cofactor and the partially hydrolyzed model of substrate/product (C14-CoA) are shown with sticks in yellow and pink, respectively. α-Helices are labeled alphabetically, and β-strands are numbered consecutively from the N to C terminus. The numbers in a smaller font are residue numbers. Unless otherwise noted, all figures were generated using Pymol (52).