Figure 2 | Scientific Reports

Figure 2

From: Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking

Figure 2

LmTXNPx structure in fully folded conformation.

(A). Decameric assembly of LmTXNPx. Two pentamers belonging to adjacent asymmetric units are colored in red and blue respectively. (B). Functional dimer. The two fold symmetry-related subunits are indicated by different colors (red and blue). The residues of the C-terminal region (169–199) are indicated in cyan, the residues of the Cp loop in yellow. The catalytic cysteines Cp (Cys52) and Cr′ (Cys173) are depicted as spheres. (C). Superimposition between LmTXNPx in FF (4K1F) and LU (3TUE) conformations: blow-up of the catalytic site. The LmTXNPx-LU monomers of the dimer are depicted in orange whereas the LmTXNPx-FF monomers are depicted in red and blue, respectively. The residues of the C-terminal region (169–199), visible only in the FF conformation, are indicated in cyan and the residues of the Cp loop in FF conformation in yellow. The catalytic cysteines are indicated and depicted as spheres. (D). Catalytic cysteines moiety. The catalytic cysteines, the residues surrounding and interacting with the catalytic cysteines are indicated and depicted as sticks.

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