Fig. 2: Visualisation of surface hydrophobicity, and electrostatic properties of the LGALS-11 complex with β-D-galactose.

Amino acid substitution in a surface representation of hydrophobicity (a, b) and electrostatic properties (c, d) of residues in isoforms 1 and 2 of LGALS-11 are labelled with a one letter code and position. The glycan-binding groove is highlighted and defined by dotted lines. The hydrophobicity properties of amino acids are indicated using the Kyte and Doolittle hydrophobicity scale; the most polar residues are in medium purple and the most hydrophobic residues are in tan in the surface representation. The electrostatic potential ranges from negative (red) to positive (blue). The surface properties of isoform 2 was derived by mutating the residues in the crystal structure of isoform 1 to isoform 2, using the COOT tool. The hydrophobicity and Coulombic electrostatic potential of both isoforms 1 and 2 were displayed using the surface colouring feature of the UCSF Chimera tool (v.1.10.2).