2QTM

crystal structure of nicotinate mononucleotide adenylyltransferase

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 95
  • Norm. En. per Res.: -3.9171
• 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	-53.2524	-52.0705	-266.801	-372.124	95	14	7	10622	9	32	29

Interface residues

• A-B: ALA132A, ALA132B, ALA153A, ALA153B, ALA22A, ALA22B, ALA28A, ALA28B, ALA63A, ALA63B, ALA66A, ALA66B, ARG133A, ARG133B, ARG162A, ARG162B, ASN23A, ASN23B, ASN30A, ASP108A, ASP108B, CYS169A, CYS169B, GLU148A, GLU148B, GLU151A, GLU151B, GLU175A, GLU175B, GLU24A, GLU24B, GLU67A, GLU67B, GLU68A, GLU68B, GLY17A, GLY17B, HIS18A, HIS18B, HIS27A, HIS27B, HIS69A, HIS69B, ILE149A, ILE149B, ILE21A, ILE21B, LEU158A, LEU158B, LEU159A, LEU159B, LEU172A, LEU172B, LEU19A, LEU19B, LEU20A, LEU20B, LYS166A, LYS166B, LYS167A, LYS167B, LYS170A, LYS170B, PHE152A, PHE152B, PHE36A, PHE36B, PHE70A, PHE70B, PRO134A, PRO134B, PRO150A, PRO150B, PRO174A, PRO174B, SER155A, SER155B, THR168A, THR168B, THR64A, THR64B, TYR136A, TYR136B, TYR16A, TYR16B, TYR171A, TYR171B, TYR26A, TYR26B, VAL147A, VAL147B, VAL154A, VAL154B, VAL25A, VAL25B