1MKX
the co-crystal structure of unliganded bovine alpha- thrombin and prethrombin-2: movement of the yppw segment and active site residues upon ligand binding
Total interactions analyzed 3
Total true interactions 2
Strongest Interaction Chains H-K
Int. Res. 68
Norm. En. per Res. -3.0605
Hub Node H(1)
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.
L-H -86.9705 -73.5506 443.415 282.8938 89 24 2 13736 9 41 31
H-K -10.266 -32.136 -165.712 -208.1141 68 15 0 6196 1 29 24