1LRP

comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda

• Total interactions analyzed: 3
• Total true interactions: 3
• Strongest Interaction:
  • Chains: B-C
  • Int. Res.: 12
  • Norm. En. per Res.: -0.0378
• Hub Node: A(2)

All Interactions

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
A-B	0.0	0.0	-0.4182	-0.4182	13	0	0	109	0	0	0
A-C	0.0	0.0	-0.4411	-0.4411	13	0	0	112	0	0	0
B-C	0.0	0.0	-0.4541	-0.4541	12	0	0	111	0	0	0

Interface residues

• A-B: ALA81B, ARG82B, GLN9A, GLU10B, GLU74B, LEU7A, LYS5A, PRO6A, PRO78B, SER77B, SER79B, THR8A, TYR85B
• A-C: ALA81A, ARG82A, GLN9C, GLU10A, GLU74A, LEU7C, LYS5C, PRO6C, PRO78A, SER77A, SER79A, THR8C, TYR85A
• B-C: ALA81C, ARG82C, GLN9B, GLU74C, LEU7B, LYS5B, PRO6B, PRO78C, SER77C, SER79C, THR8B, TYR85C