2C4M
starch phosphorylase: structural studies explain oxyanion- dependent kinetic stability and regulatory control.
Total interactions analyzed 6
Total true interactions 6
Strongest Interaction Chains A-B
Int. Res. 258
Norm. En. per Res. -3.4516
Hub Node A(3)
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Weak Strong
Width of edge <-> No. of inter. res.
All Interactions
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Chains Hydro. Bond Ener. (kJ/mol) Elec. Ener. (kJ/mol) VDW. Ener. (kJ/mol) Tot. Stab. Ener. (kJ/mol) #int. res. # Short cont. #Hydr. int. #VDW pairs #salt bridges #Pot. fav. elec. int #Pot. unfav. elec. int int. res.
A-B -109.8307 -29.6452 -751.04 -890.5159 258 29 5 28847 8 140 123
A-C -22.8245 27.3255 -133.475 -128.9739 77 10 1 4493 0 27 34
A-D -4.5647 22.8551 -98.814 -80.5236 61 4 0 3551 1 19 23
B-C -26.0467 34.9455 -102.805 -93.9062 64 5 0 3759 0 21 24
B-D 0.0 11.8789 -4.3648 7.5141 6 1 0 280 0 4 4
C-D -100.4658 -32.3784 -753.238 -886.0822 257 28 7 28881 8 143 120