Fig. 3: Recognition of urate by URAT1.

a The interaction network between urate and URAT1 residues is depicted. A red dot indicates a water molecule, hydrogen bonds are highlighted with red dashed lines, and the corresponding density maps of the residues and ligand are shown as a mesh (contour level: σ = 5). b Schematic representation of the interactions between URAT1 and urate in 2D format. c 14C-urate uptake activities of mutants of pocket-forming residues relative to the wild-type URAT1. Data are shown as “mean values ± SEM”; Four independent replicates were performed. Data were analyzed by two-sided, one-way ANOVA Tukey’s test. *P < 0.05, **P < 0.01, ***P < 0.001. d Cut-open surface view showing the substrate binding pocket in URAT1 and rOAT1. The distances from F241 to F449 in URAT1 and Y230 to F38 in rOAT1 are measured and marked. e The alignment includes residues around the urate binding site in URAT1, OAT1, rOAT1, OAT2, OAT3, OAT4, OAT5, OAT6, and OAT7. These transporters are organized based on sequence homology.