1TWR

crystal structures of ferrous and ferrous-no forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 104
  • Norm. En. per Res.: -3.3445
• 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	-44.1612	-21.4183	-282.246	-347.8254	104	17	2	11163	6	25	28

Interface residues

• A-B: ALA151A, ALA151B, ALA154A, ALA165A, ALA165B, ALA173A, ALA173B, ALA175A, ALA175B, ALA87A, ALA87B, ALA88A, ALA88B, ALA94A, ALA94B, ARG100A, ARG100B, ARG44B, ARG85A, ARG85B, ASN171A, ASN171B, ASP156A, ASP156B, ASP92A, ASP92B, GLN102A, GLN102B, GLN145B, GLN152A, GLN152B, GLN91A, GLN91B, GLU103A, GLU103B, GLU162A, GLU162B, GLU81A, GLU81B, GLU82A, GLU82B, GLU90A, GLU90B, GLY161A, GLY161B, GLY163A, GLY163B, GLY98A, GLY98B, HIS84A, HIS84B, ILE172A, ILE172B, LEU155A, LEU155B, LEU157A, LEU157B, LEU164A, LEU164B, LEU89A, LEU89B, LEU93A, LEU93B, LYS148A, LYS148B, LYS149A, LYS149B, LYS153A, LYS153B, LYS177A, LYS177B, LYS86A, LYS86B, PHE166A, PHE166B, PHE167A, PHE167B, PHE169A, PHE169B, PHE47A, PHE95A, PHE95B, PRO158A, PRO158B, PRO170A, PRO170B, PRO80A, PRO99A, PRO99B, SER159A, SER159B, SER160A, SER160B, SER174A, SER174B, THR168A, THR168B, THR176A, TRP101A, TRP101B, TRP96A, TRP96B, TYR55A, TYR55B