2V2H
the a178l mutation in the c-terminal hinge of the flexible loop-6 of triosephosphate isomerase (tim) induces a more closed conformation of this hinge region in dimeric and monomeric tim
Total interactions analyzed 3
Total true interactions 3
Strongest Interaction Chains A-B
Int. Res. 54
Norm. En. per Res. -1.0265
Hub Node A(2)
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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 -19.4145 -6.5806 -29.4333 -55.4284 54 4 0 1897 0 13 18
A-C -2.1901 -9.6208 -30.5293 -42.3402 51 1 0 1769 1 13 17
B-C 0.0 1.6503 -25.6542 -24.0039 47 0 0 1702 0 11 18