2TYS
crystal structures of mutant (betak87t) tryptophan synthase alpha2 beta2 complex with ligands bound to the active sites of the alpha and beta subunits reveal ligand-induced conformational changes
Total interactions analyzed 1
Total true interactions 1
Strongest Interaction Chains A-B
Int. Res. 119
Norm. En. per Res. -3.4457
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 -60.7762 -4.9731 -344.292 -410.0413 119 22 6 13691 2 13 16