2PM8

crystal structure of recombinant full length human butyrylcholinesterase

• Total interactions analyzed: 3
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 85
  • Norm. En. per Res.: -1.1012
• 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	-8.0821	11.2559	-96.7752	-93.6013	85	3	4	5292	0	30	36

Interface residues

• A-B: ALA459A, ALA459B, ALA516A, ALA516B, ARG381A, ARG381B, ARG509A, ARG509B, ARG515A, ARG515B, ARG520A, ARG520B, ASN504A, ASN504B, ASP378A, ASP378B, ASP379A, ASP379B, CYS519A, GLN380A, GLN380B, GLN486A, GLN486B, GLN517A, GLN517B, GLN518A, GLN518B, GLU460A, GLU460B, GLU461A, GLU461B, GLU497A, GLU497B, GLU506A, GLU506B, HIS372A, HIS423B, ILE399A, ILE462A, ILE462B, ILE510A, ILE510B, LEU403A, LEU403B, LEU463A, LEU463B, LEU514A, LEU514B, LYS458A, LYS458B, LYS499A, LYS499B, LYS513A, LYS513B, MET511A, MET511B, PHE371A, PRO491A, SER487A, SER487B, SER489A, SER507A, SER507B, THR457A, THR457B, THR488A, THR488B, THR502A, THR502B, THR505A, THR505B, THR508A, THR508B, THR512A, THR512B, TRP376A, TRP376B, TYR420A, TYR420B, TYR456A, TYR456B, TYR500A, TYR500B, VAL377A, VAL377B