Structural Variations of Human Glucokinase Glu256Lys in MODY2 Condition Using Molecular Dynamics Study

Table 2

Molecular docking of glucose into the active site cavity of intact and mutated GK. Docking score shown in the second column indicates the binding affinity of glucose to the active site. The lower is the score, the higher will be the stability of the complex. The interacting active site residues of GK that are involved in formation of hydrogen bonds with glucose are shown in the fourth column, and the respective hydrogen bond lengths are indicated in Angstroms in the last column.

GK structure	Docking score	No. H-bonds	Interacting residue of GK	H-bond length (Å)
			P 153	1.49
			E 256	2.04
Intact	−12.199	6	Q 287	1.45
			E 290	1.58
			L 165	2.63
			K 169	2.95
			S 54	2.45
			N 166	1.54
Mutated	−8.383	5	D 262	1.69
			K 256	2.46
			K 256	3.00