1ZY0

x-ray structure of peptide deformylase from arabidopsis thaliana (atpdf1a); crystals grown in peg-6000

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 101
  • Norm. En. per Res.: -3.1694
• 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	-22.9014	-4.1012	-293.108	-320.1106	101	14	5	11587	0	30	34

Interface residues

• A-B: ALA119A, ALA119B, ALA183A, ALA183B, ALA8A, ALA8B, ARG118A, ARG118B, ARG170A, ARG170B, ARG173A, ARG173B, ASN161A, ASN161B, ASN177A, ASN177B, ASP115A, ASP115B, ASP11A, ASP11B, ASP156A, ASP156B, ASP159A, ASP159B, ASP165A, ASP165B, ASP176A, ASP176B, ASP179A, ASP179B, CYS111A, CYS111B, CYS186A, CYS186B, GLU16A, GLU16B, GLU184A, GLU184B, GLY10A, GLY10B, GLY116A, GLY116B, GLY160A, GLY160B, GLY185A, GLY185B, HIS15A, HIS15B, ILE6B, LEU112A, LEU112B, LEU14A, LEU14B, LEU162A, LEU162B, LEU178A, LEU178B, LEU180A, LEU180B, LEU182A, LEU182B, LYS166A, LYS166B, LYS17A, LYS17B, MET167A, MET167B, PHE108A, PHE108B, PHE117A, PHE117B, PHE172A, PHE172B, PRO12A, PRO12B, PRO169A, PRO169B, PRO181A, PRO181B, SER113A, SER113B, SER9A, SER9B, THR171A, THR171B, THR174A, THR174B, TYR163A, TYR163B, VAL114A, VAL114B, VAL13A, VAL13B, VAL164A, VAL164B, VAL168A, VAL168B, VAL175A, VAL175B, VAL7A, VAL7B