2HA5

crystal structure of mutant s203a of acetylcholinesterase complexed with acetylthiocholine

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 99
  • Norm. En. per Res.: -2.9817
• 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	-50.9479	-5.4917	-238.75	-295.1896	99	11	10	9786	3	19	14

Interface residues

• A-B: ALA374A, ALA374B, ALA375A, ALA375B, ALA377A, ALA377B, ALA506A, ALA506B, ALA507A, ALA507B, ALA526A, ALA526B, ALA530A, ALA530B, ALA542A, ALA542B, ARG356A, ARG356B, ARG521A, ARG521B, ARG522A, ARG522B, ARG525A, ARG525B, ARG534A, ARG534B, ASN533A, ASN533B, ASP372A, ASP372B, ASP384A, ASP384B, CYS529A, CYS529B, GLN508A, GLN508B, GLN509A, GLN509B, GLN527A, GLN527B, GLU376A, GLU376B, GLU389A, GLY523A, GLY523B, HIS381A, HIS381B, HIS387A, HIS387B, LEU360A, LEU360B, LEU373A, LEU373B, LEU380A, LEU380B, LEU386A, LEU386B, LEU524A, LEU524B, LEU536A, LEU536B, LEU539A, LEU539B, LEU540A, LEU540B, LYS538A, LYS538B, PHE531A, PHE531B, PHE535A, PHE535B, PRO388A, PRO388B, PRO537A, PRO537B, SER541A, SER541B, THR383A, THR383B, THR504B, THR505A, THR505B, THR528A, THR528B, THR543B, TRP385A, TRP385B, TRP532A, TRP532B, TYR382A, TYR382B, TYR503A, TYR503B, TYR510A, TYR510B, VAL378A, VAL378B, VAL379A, VAL379B