1L5W
crystal structure of the maltodextrin phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltotetraose
Total interactions analyzed 1
Total true interactions 1
Strongest Interaction Chains A-B
Int. Res. 229
Norm. En. per Res. -2.7155
Hub Node A(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.
A-B -63.6375 -38.6714 -519.544 -621.8529 229 26 15 22224 7 96 85