2BBA
crystal structure and thermodynamic characterization of the ephb4 receptor in complex with an ephrin-b2 antagonist peptide reveals the determinants for receptor specificity.
Total interactions analyzed 1
Total true interactions 1
Strongest Interaction Chains A-P
Int. Res. 67
Norm. En. per Res. -3.7876
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-P -14.0645 -38.0661 -201.64 -253.7706 67 4 8 8090 2 5 4