2NLX

crystal structure of the apo e. coli xylulose kinase

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 91
  • Norm. En. per Res.: -2.7209
• 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	-27.4549	-2.4433	-217.706	-247.6042	91	25	6	10673	0	13	9

Interface residues

• A-B: ALA301A, ALA301B, ALA302A, ALA302B, ALA316B, ALA345A, ALA345B, ALA362A, ALA362B, ALA364B, ARG474B, ASN359A, ASN359B, CYS297A, CYS297B, GLN344A, GLN344B, GLN355A, GLN355B, GLN477B, GLN478A, GLN478B, GLU325A, GLU325B, GLU360A, GLU360B, GLY306A, GLY306B, GLY347A, GLY347B, GLY351A, GLY351B, GLY357A, GLY357B, HIS354A, HIS354B, HIS356A, HIS356B, LEU304A, LEU304B, LEU307A, LEU307B, LEU330A, LEU330B, LEU352A, LEU352B, LEU361A, LEU361B, LEU475A, LEU475B, LEU479A, LEU479B, LEU480B, LEU482A, LEU482B, LYS303A, LYS303B, LYS346A, LYS346B, MET483A, PHE329A, PHE329B, PHE349A, PHE349B, PHE350A, PHE350B, PRO326B, PRO331A, PRO331B, PRO343A, PRO358A, PRO358B, PRO481A, PRO481B, SER296A, SER296B, SER308A, THR305A, THR305B, THR353A, THR353B, TRP300A, TRP300B, TRP328A, TYR332A, TYR332B, TYR476B, VAL327A, VAL327B, VAL348A, VAL348B