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

Table 3

Interaction of glucose with active site of intact and mutated GK and energy transitions of GK-glucose complexes during molecular dynamics simulations for a period of 10 ns.

Simulation^a period; (ps)	No. H-bonds^b		Interacting residues of GK active site^c		Energy of the complex^d; (Kcal/mol)
	Intact	Mutated	Intact	Mutated	Intact	Mutated
0	6	5	P153, L165, K169, E256, E290, Q287	S54,  D262, N166, K256, K256	527.75	366.85
500	5	8	P153, L165, N166, K169, Q287	A53, K56, N166, Q286, Q286, D262, D262, D262	5135.83	8536.07
1000	5	6	P153, L165, N166, K169, Q287	A53, N166, K256, D262, D262, Q286	5054.68	8600.38
1500	6	8	P153, L165, N166, K169, Q287, E290	A53, L165, K256, K256, D262, D262, D262, Q286	5066.78	8553.16
2000	6	4	L165, N166, K169, E256, Q287, Q287	A53, D262, D262, Q286	5112.49	8625.42
2500	8	4	L165, L165, N166, N166, K169, K169, E256, Q287	A53, K256, D262, D262	5094.22	8536.71
3000	6	4	L165, N166, K169, K169, E256, E290	A53, D262, D262, Q286	5087.11	8534.96
3500	8	6	L165, L165, N166, N166, K169, K169, K169, E256	A53, S54, D262, D262, D262, Q286	5154.06	8633.15
4000	8	7	L165, L165, N166, N166, K169, K169, K169, E256	A53, D262, D262, D262, Q286, Q286, Q287	5088.23	8608.42
4500	8	7	L165, N166, N166, K169, K169, K169, E256, Q287	A53, S54, D262, D262, D262, Q286, Q287	5014.87	8579.74
5000	8	5	L165, L165, N166, N166, K169, K169, K169, E256	A53, D262, D262, Q286, Q286	5078.62	8521.10
5500	6	5	L165, N166, K169, K169, K169, E256	A53, D262, D262, D262, Q286	5087.78	8548.05
6000	8	5	L165, L165, N166, N166, K169, K169, K169, E256	A53, D262, D262, D262, Q286	5116.11	8566.65
6500	8	7	L165, L165, N166, N166, K169, K169, K169, E256	A53, S54, D262, D262, D262, Q286, Q286	5059.85	8542.55
7000	7	6	L165, N166, N166, K169, K169, K169, E256	A53, D262, D262, D262, Q286, Q286	5030.70	8446.74
7500	8	6	L165, L165, N166, N166, K169, K169, K169, E256	A53, S54, D262, D262, D262, Q286	5063.48	8597.48
8000	4	7	N166, N166, K169, E256	A53, S54, D262, D262, D262, Q286, Q287	5106.54	8658.68
8500	8	5	L165, L165, N166, N166, K169, K169, E256, Q287	A53, D262, D262, D262, Q286	5104.12	8548.79
9000	6	7	L165, N166, K169, K169, K169, E256	A53, S54, D262, D262, D262, Q286, Q287	5127.97	8518.22
9500	7	4	L165, L165, N166, K169, K169, K169, E256	A53, D262, D262, Q286	5105.28	8574.21
10000	8	6	L165, L165, N166, N166, K169, K169, K169, E256	A53, S54, D262, D262, D262, Q286	5160.90	8522.43

^aDuration of simulation period where the respective conformation was analyzed.
^bNumber of hydrogen bonds formed between the glucose and active site residues of intact and mutated GK.
^cInteracting residues of intact and mutated GK during simulations in a specified conformation. The residues in bold are active site residues that are interacting with glucose specifically from intact GK, the residues in italic are found to be interacting with glucose in both intact and mutated GK, and the residues in bold italic are found to be interacting with glucose in mutated GK only.
^dEnergies of the docking complexes of intact and mutated GK at specified simulation periods.