1UXI
large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface
Total interactions analyzed 1
Total true interactions 1
Strongest Interaction Chains A-B
Int. Res. 194
Norm. En. per Res. -4.231
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 -105.2688 -62.8786 -652.675 -820.8225 194 30 25 25048 6 56 32