1X89

crystal structure of siderocalin (ngal, lipocalin 2) complexed with carboxymycobactin s

• Total interactions analyzed: 3
• Total true interactions: 2
• Strongest Interaction:
  • Chains: A-C
  • Int. Res.: 45
  • Norm. En. per Res.: -2.2552
• Hub Node: A(2)

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	6.0136	-8.8991	-2.8855	22	0	0	620	2	18	12
A-C	-15.5731	0.0	-85.9111	-101.4842	45	8	0	3605	0	3	3

Interface residues

• A-B: ARG154A, ARG154B, ARG43A, ASN151B, ASN164A, ASN164B, GLU147A, GLU147B, GLU150A, GLU150B, GLU163A, GLU163B, ILE153A, ILE153B, ILE166B, LYS157A, LYS157B, PHE168A, PHE168B, PRO162B, SER146A, SER146B
• A-C: ALA53A, ARG140A, ASN114A, ASN114C, ASN116A, ASN116C, ASN21C, ASN25A, ASN25C, ASP173A, ASP177A, GLN117A, GLN117C, GLN19C, GLN20C, GLN23C, GLN26A, GLN26C, GLN28A, GLN88C, GLU143A, GLY139A, GLY29A, HIS118A, HIS118C, ILE172A, ILE176A, ILE55A, LYS142A, LYS30A, LYS62C, MET51A, PHE22C, PHE27A, PHE27C, PRO171A, PRO89C, SER112C, THR113C, THR141A, THR54A, TRP31A, TYR115A, TYR115C, TYR32A