1YRR

crystal structure of the n-acetylglucosamine-6-phosphate deacetylase from escherichia coli k12 at 2.0 a resolution

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 97
  • Norm. En. per Res.: -4.1209
• 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	-73.5081	-43.1432	-283.073	-399.7243	97	11	9	10810	6	31	33

Interface residues

• A-B: ALA220A, ALA220B, ALA232A, ALA232B, ALA234A, ALA234B, ALA239A, ALA239B, ALA255A, ALA255B, ALA260A, ALA260B, ARG227A, ARG227B, ARG258A, ARG258B, ARG262A, ARG262B, ASN219A, ASN219B, ASN256A, ASN256B, ASN259A, ASN259B, ASP237A, ASP237B, ASP248A, ASP248B, ASP253A, ASP253B, CYS324A, CYS324B, GLU228A, GLU228B, GLU238A, GLU238B, GLY226A, GLY226B, GLY230A, GLY230B, GLY233A, GLY233B, GLY249A, GLY249B, GLY308B, HIS251A, HIS251B, ILE224A, ILE224B, ILE235A, ILE235B, ILE245A, ILE245B, ILE246A, ILE246B, ILE257A, ILE257B, LEU200A, LEU200B, LEU217A, LEU217B, LEU236A, LEU236B, LEU250A, LEU250B, LEU263A, LEU263B, LEU298A, LEU306A, LYS201A, LYS201B, LYS204A, LYS204B, LYS261A, LYS261B, LYS264A, LYS264B, MET221A, MET221B, PRO222A, PRO222B, PRO229A, PRO229B, SER307A, SER307B, SER309B, THR225A, THR225B, THR305A, TYR218A, TYR218B, TYR223A, TYR223B, TYR254A, TYR254B, VAL252A, VAL252B