1SPD

amyotrophic lateral sclerosis and structural defects in cu, zn superoxide dismutase

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 77
  • Norm. En. per Res.: -2.8073
• Hub Node: A(1)

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	-29.9659	-3.7741	-182.42	-216.16	77	20	6	7728	0	8	6

Interface residues

• A-B: ALA152A, ALA152B, ALA1A, ALA4A, ALA4B, ALA55A, ALA55B, ALA60A, ALA60B, ARG115A, ARG115B, ASN19A, ASN19B, ASN53A, ASN53B, ASP109A, ASP52A, ASP52B, CYS111A, CYS111B, CYS6A, CYS6B, GLN153A, GLN153B, GLU49A, GLU49B, GLY114A, GLY114B, GLY147A, GLY147B, GLY150A, GLY150B, GLY16A, GLY16B, GLY51A, GLY51B, GLY56A, GLY56B, GLY61B, HIS48A, HIS48B, ILE112A, ILE112B, ILE113A, ILE113B, ILE149A, ILE149B, ILE151A, ILE151B, ILE17A, ILE17B, ILE18A, ILE18B, LEU8B, LYS3A, LYS3B, LYS9A, LYS9B, PHE50A, PHE50B, PHE64A, PHE64B, SER59A, SER59B, THR116A, THR116B, THR2A, THR2B, THR54A, THR54B, THR58B, VAL148A, VAL148B, VAL5A, VAL5B, VAL7A, VAL7B