1RAA
crystal structure of ctp-ligated t state aspartate transcarbamoylase at 2.5 angstroms resolution: implications for atcase mutants and the mechanism of negative cooperativity
Total interactions analyzed 6
Total true interactions 3
Strongest Interaction Chains B-D
Int. Res. 100
Norm. En. per Res. -4.7696
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 -29.5345 -12.4169 -185.233 -227.1844 69 4 4 7030 2 28 24
B-D -95.2641 -58.1407 -323.553 -476.9578 100 22 5 11907 7 27 26
C-D -43.2024 -12.132 -193.353 -248.6874 64 7 4 7070 3 29 24