Fig. 9: Structural basis for dual functionality of 2-HID from P. lobata.
From: The protein conformational basis of isoflavone biosynthesis
a 2Fo-Fc electron density map at 1.0 σ for p-nitrophenyl (NPO) and a catalytic triad, Thr168, Asp269 and His301 for carboxylesterase activity; b Active site of 2-HID docked with substrate 2,7,4´-trihydroxyisoflavanone close to the catalytic acid Glu89 and catalytic base His301. Key residues involved in substrate binding are shown as bond models and colored according to element: oxygen, red; nitrogen, blue; and carbon, cyan. NPO and 2,7,4’-trihydroxyisoflavanone are also shown as bond models with their carbon atoms in yellow.
