2RD5
structural basis for the regulation of n-acetylglutamate kinase by pii in arabidopsis thaliana
Total interactions analyzed 6
Total true interactions 3
Strongest Interaction Chains B-C
Int. Res. 60
Norm. En. per Res. -4.0808
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 0.0 -70.13 -271.076 -341.206 108 6 12 12764 1 30 33
A-D -52.8035 -23.8891 -173.69 -250.3826 67 13 0 6168 4 28 27
B-C -49.3645 -22.6946 -172.786 -244.8451 60 11 0 5760 4 26 24