3CS8
structural and biochemical basis for the binding selectivity of pparg to pgc-1a
Total interactions analyzed 1
Total true interactions 1
Strongest Interaction Chains A-B
Int. Res. 47
Norm. En. per Res. -4.0098
Hub Node A(1)
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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 -40.8784 -0.8555 -146.729 -188.4629 47 9 5 6801 0 7 6