Figure 2: Relative binding activity of AtPDIL1-2 for 2,4,6-TCP. | Scientific Reports

Figure 2: Relative binding activity of AtPDIL1-2 for 2,4,6-TCP.

From: Disulfide isomerase-like protein AtPDIL1–2 is a good candidate for trichlorophenol phytodetoxification

Figure 2

(A) Sequence alignment of AtPDIL1-2 and ERp57. Both proteins shared more similarity sequence within the a-type domains than the b-type domains. The regions for oxidoreductase activity were underlined. (B) Contrasting the crystal structures of AtPDIL1-2 with ERp57. Both proteins showed similar structures of both a-type and b-type domains. (C) Docking analysis of the binding interaction of 2,4,6-TCP inside AtPDIL1-2 with AutoDock. A close-up of the docking result of the AtPDIL1-2–2,4,6-TCP binding mode, showing that a hydrogen bond formed between the 1-hydroxyl group of TCP and His-254 of AtPDIL1-2. Atoms were labeled with different colors. Red: oxygen; white: hydrogen; green: chlorine; gray: carbon. The radius of the sphere represents interaction strength.

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