2IX9
respective role of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase a
Total interactions analyzed 1
Total true interactions 1
Strongest Interaction Chains A-B
Int. Res. 79
Norm. En. per Res. -1.6991
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 -27.8838 20.4546 -126.8 -134.2293 79 11 2 4952 0 8 13