2C2M
crystal structures of caspase-3 in complex with aza-peptide michael acceptor inhibitors.
Total interactions analyzed 3
Total true interactions 3
Strongest Interaction Chains B-C
Int. Res. 27
Norm. En. per Res. -5.7419
Hub Node A(2)
Click on the Nodes or Edges in the network to see the details
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 -197.6376 -26.9385 -706.386 -930.9621 168 38 13 25061 3 41 35
A-C 0.0 -3.0274 -8.7997 -11.8271 19 0 0 463 0 5 4
B-C -33.2682 -36.8618 -84.9019 -155.0319 27 4 2 2693 2 9 7