Fig. 5

Three-dimensional structure analysis of MpADC. a, b Predicted 3D structure of MpADC. The predicted structure of subunit A was shown on the top (β-sheet, magenta; α-sheet, blue; loop, orange); the subunit B was shown at the bottom (grey). The predicted active pockets were shown in green. c The A-subunit of MpADC. The amino acids are colored by their conservation grades using the color-coding bar, with turquoise-through-maroon indicating variable-through-conserved. The C-terminal, N-terminal and 40th residue of N-terminal of A-subunit were indicated by red arrow. d Three-dimensional (3D) docking models between the substrates, PLP and L-ASP (light yellow sticks) and MpADC (the green dotted line, magenta dotted line, pink dotted line, orange dotted line and split pea represented hydrogen bonds, pi-alkyl interactions, pi-anion interactions, cation-pi interactions, pi-donor hydrogen bond, respectively). The predicted amino acid sites bound to the substrates include Leu135, His235, Asp317, His348, Lys349, and Arg510 from subunit A (purple sticks) and Tyr158 and Cys399 from subunit B (light-blue sticks). e, f The modeled 3D structure of variant Δ39. The spatial position corresponds to a