2Q27

crystal structure of oxalyl-coa decarboxylase from escherichia coli

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 141
  • Norm. En. per Res.: -2.8826
• 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	-52.2394	-76.6003	-277.612	-406.4517	141	8	4	12656	2	40	30

Interface residues

• A-B: ALA133A, ALA133B, ALA134A, ALA134B, ALA146A, ALA146B, ALA148A, ALA148B, ALA150A, ALA150B, ALA193A, ALA193B, ALA315A, ALA315B, ARG149A, ARG149B, ARG152A, ARG152B, ARG158A, ARG158B, ARG280A, ARG280B, ARG312A, ARG312B, ASN125A, ASN189A, ASN189B, ASN311A, ASN311B, ASP142A, ASP142B, ASP302A, ASP302B, ASP309A, ASP309B, ASP321A, ASP321B, CYS197A, CYS197B, GLN139A, GLN139B, GLN141A, GLN141B, GLN300B, GLN306A, GLN306B, GLN327B, GLU188A, GLU188B, GLU304A, GLU304B, GLU307A, GLU307B, GLY144A, GLY144B, GLY157A, GLY157B, GLY320A, GLY320B, ILE145A, ILE145B, ILE151A, ILE151B, ILE184A, ILE184B, ILE303A, ILE303B, ILE308A, ILE308B, ILE314A, ILE314B, LEU147A, LEU147B, LEU194A, LEU194B, LEU195A, LEU195B, LEU281A, LYS128A, LYS128B, LYS132A, LYS132B, LYS186A, LYS186B, LYS199A, LYS199B, LYS289A, LYS289B, PHE135A, PHE135B, PRO129A, PRO129B, PRO190A, PRO190B, PRO192A, PRO192B, PRO196A, PRO196B, PRO198A, PRO198B, PRO305A, PRO305B, PRO313A, PRO313B, PRO317A, PRO317B, SER154A, SER154B, SER156A, SER156B, SER191A, SER191B, SER200A, SER200B, SER310A, SER310B, SER324A, SER324B, SER325A, SER325B, THR182A, THR182B, THR183A, THR183B, VAL153A, VAL153B, VAL155A, VAL155B, VAL162A, VAL162B, VAL185A, VAL185B, VAL187A, VAL187B, VAL201B, VAL316A, VAL316B, VAL318A, VAL318B, VAL319A, VAL319B