2VEM

structure-based enzyme engineering efforts with an inactive monomeric tim variant: the importance of a single point mutation for generating an active site with suitable binding properties

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 96
  • Norm. En. per Res.: -1.5534
• 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	-6.6753	-19.3763	-123.071	-149.1225	96	5	1	5452	2	27	31

Interface residues

• A-B: ALA118A, ALA118B, ALA157A, ALA157B, ALA160A, ALA160B, ARG207A, ARG207B, ARG54A, ASN29A, ASN34A, ASN34B, ASN89A, ASN89B, ASP158A, ASP158B, ASP201A, ASP201B, ASP26A, ASP36A, ASP36B, ASP85A, ASP85B, CYS39B, GLN38A, GLN38B, GLN5A, GLN5B, GLU205A, GLU205B, GLU53A, GLY120A, GLY120B, GLY204B, GLY87A, GLY87B, HIS35A, HIS35B, HIS57A, HIS57B, ILE33A, ILE33B, ILE62A, ILE62B, ILE7B, LEU27A, LEU55A, LEU55B, LEU83A, LYS155B, LYS156A, LYS156B, LYS161A, LYS161B, LYS3A, LYS3B, LYS52A, LYS52B, LYS59A, LYS59B, LYS84A, LYS84B, MET122A, MET122B, PHE121A, PHE121B, PHE28A, PHE60A, PHE60B, PHE86A, PHE86B, PRO4A, PRO4B, PRO58A, PRO58B, PRO6A, PRO6B, SER119A, SER2A, SER2B, SER30A, SER32A, SER56A, SER56B, THR31A, TRP159A, TRP90A, TRP90B, VAL117A, VAL202B, VAL37A, VAL37B, VAL61A, VAL61B, VAL88A, VAL88B