Fig. 3

Comparison of normal and mutant glucokinase models at residue 254. a, b Pymol structures for normal asparigine and mutant histidine, respectively. Each residue is denoted in red and surrounding residues in orange. Dashed lines represent the distance in Ångström (Å) for internal contacts. c, d Graphic results for residue interactions obtained in the STING Millennium analysis. a, c The native Asn254 forms hydrogen bond interactions with E256, N231 and L58. b, d The mutant His254 suppresses the interaction with N231, maintains the contact with L58, introduces four additional hydrophobic interactions with C233, V207, N204 and T60, creates a new aromatic stacking with K459 and changes the hydrogen bond wiht E256 to a charge attractive interaction. Between c and d, color legend for internal interactions provided by BlueStar STING software