3TDU
n-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: structure of a human cul1whb- dcn1p-acetylated ubc12n complex
Total interactions analyzed 15
Total true interactions 7
Strongest Interaction Chains B-D
Int. Res. 60
Norm. En. per Res. -4.3868
Hub Node A(4)
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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 -28.4626 -1.6499 -100.169 -130.2815 82 7 0 4601 3 43 52
A-C -52.5706 -57.2041 -155.474 -265.2486 64 11 0 5854 5 50 26
A-D -11.2006 7.0006 -46.4991 -50.6992 29 3 0 1672 0 19 13
A-F -34.2397 -17.0584 -103.926 -155.2241 55 5 6 4803 1 15 7
B-C 0.0 4.0359 -24.8105 -20.7746 26 0 0 1441 1 17 16
B-D -60.6727 -55.627 -146.906 -263.2057 60 9 0 5818 4 50 27
B-E -20.8691 -16.5285 -111.253 -148.6506 57 6 6 4778 1 15 4