2AQS

cu/zn superoxide dismutase from neisseria meningitidis k91e, k94e double mutant

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 98
  • Norm. En. per Res.: -2.3074
• 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	0.0	2.5562	-228.677	-226.1208	98	5	3	9310	4	7	9

Interface residues

• A-B: ALA128A, ALA128B, ALA137A, ALA137B, ALA143A, ALA143B, ARG145A, ARG145B, ASN139A, ASN139B, ASN165A, ASN165B, ASN59A, ASN59B, ASP119A, ASP119B, ASP120A, ASP120B, ASP134A, ASP134B, ASP164A, ASP164B, GLN118A, GLN118B, GLU57A, GLU57B, GLU73A, GLU73B, GLY163A, GLY163B, GLY61A, GLY61B, GLY74A, GLY74B, GLY77A, GLY77B, HIS133A, HIS133B, HIS166A, HIS166B, HIS76A, HIS76B, LEU123A, LEU123B, LEU126A, LEU126B, LEU129A, LEU129B, LEU132A, LEU132B, LEU142A, LEU142B, LEU146A, LEU146B, LEU62A, LEU62B, LEU75A, LEU75B, LYS108A, LYS108B, LYS147A, LYS147B, PHE64A, PHE64B, PRO116A, PRO116B, PRO127A, PRO127B, PRO140A, PRO140B, PRO144A, PRO144B, PRO66A, PRO66B, SER58A, SER58B, THR130A, THR130B, THR136A, THR136B, THR138A, THR138B, THR56A, THR56B, THR65A, THR65B, TRP117A, TRP117B, TYR115A, TYR115B, TYR60A, TYR60B, VAL131A, VAL131B, VAL141A, VAL141B, VAL63A, VAL63B