Table 4.
Protein | Amino Acid | Distance | Amino Acid | Distance | Amino Acid | Distance |
MIOX3 | Asp-160/Lys-201 | 2.67 Å | Asp-163/Lys-331 | 2.91 Å | Ser-167/Arg-116 | 12.15 Å |
MIOX2 | Asp-112/Lys-153 | 2.66 Å | Asp-115/Lys-283 | 2.91 Å | Ser-119/Arg-68 | 12.15 Å |
MIOX1 | Asp-117/Lys-157 | 2.65 Å | Asp-120/Lys-287 | 2.91 Å | Ser-124/Arg-71 | 3.55 Å |
musculus | Asp-85/Lys-127 | 2.31 Å | Asp-88/Lys-257 | 2.97 Å | Asp-92/Arg-39 | 2.98 Å |
The amino acids involved in the myo-inositol substrate lid are conserved among the four proteins with the exception of a substitution of Ser for Asp in all three computationally modeled C. neoformans MIOX proteins. Predicted bonding distances indicate the salt bridge formation is conserved for MIOX1. The distance measured between the substituted Ser and Arg in both computationally modeled MIOX2 and MIOX3 proteins (12.15 Å) does not support the formation of a salt bridge at these locations.