Figure 1 | Scientific Reports

Figure 1

From: Trp–His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer

Figure 1

(a) Structure of MvBOxWT from strongly acidic condition. The structure (6I3J) is shown in secondary structure representation (helices are colored red, β–strands yellow, loops green). Copper ions are shown as orange spheres. The Trp396–His398 adduct (shown as magenta sticks), oligosaccharides modifying asparagine side chains (black sticks), the N-terminus, T1 copper and the trinuclear copper cluster are labeled. (b) Chemical environment of the Trp–His adduct in MvBOx. Hydrogen bond distances are given in Ångströms. Values in parentheses are for chain B of the structure 6I3J. The CH – π interactions of Trp396 are marked. The indole–imidazole moiety of the adduct is shown with carbon colored magenta. T1Cu is shown as orange sphere. Molecular graphics were created using PyMOL (Schrödinger, LLC).

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