2AUO

residue f4 plays a key role in modulating the oxygen affinity and cooperatrivity in scapharca dimeric hemoglobin

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 88
  • Norm. En. per Res.: -3.4843
• 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	-35.9675	-46.7004	-223.952	-306.6199	88	3	3	9449	5	42	26

Interface residues

• A-B: ALA76A, ALA76B, ALA98A, ALA98B, ARG104A, ARG104B, ARG53A, ARG53B, ARG67A, ARG67B, ASN100A, ASN100B, ASN63A, ASN63B, ASN79A, ASN79B, ASN86A, ASN86B, ASP64A, ASP64B, ASP82A, ASP82B, ASP88A, ASP88B, ASP89A, ASP89B, CYS92A, CYS92B, GLN78A, GLN78B, GLN83A, GLN83B, GLU95A, GLU95B, GLY68A, GLY68B, HIS69A, HIS69B, ILE102A, ILE71A, ILE71B, ILE81A, ILE81B, LEU54A, LEU54B, LEU66A, LEU66B, LEU73A, LEU73B, LEU77A, LEU77B, LEU90A, LEU90B, LYS29A, LYS29B, LYS30A, LYS30B, LYS65A, LYS65B, LYS96A, LYS96B, MET61A, MET61B, MET74A, MET74B, PHE80A, PHE80B, PRO87A, PRO87B, SER70A, SER70B, THR103A, THR103B, THR72A, THR72B, TYR4A, TYR75A, TYR75B, TYR97A, TYR97B, VAL91A, VAL91B, VAL93A, VAL93B, VAL94A, VAL94B, VAL99A, VAL99B