3CV2

atomic resolution structures of escherichia coli and bacillis anthracis malate synthase a: comparison with isoform g and implications for structure based drug design

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 64
  • Norm. En. per Res.: -1.167
• 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	-5.848	-6.3885	-62.4495	-74.686	64	0	1	3099	0	18	20

Interface residues

• A-B: ALA150B, ALA300A, ALA351A, ALA372B, ALA377B, ARG100B, ARG413A, ASN110B, ASN141B, ASN148B, ASN159B, ASN309A, ASN342A, ASN343A, ASN347A, ASN358A, ASN380B, ASN470A, ASP138B, ASP304A, ASP352A, ASP373B, GLN155B, GLN299A, GLN344A, GLU149B, GLU340A, GLU412A, GLU415A, GLU416A, GLY142B, GLY151B, GLY370B, GLY471A, HIS341A, ILE144B, ILE153B, LEU156B, LEU346A, LEU355A, LEU468A, LYS152B, LYS157B, LYS305A, LYS348A, LYS350A, LYS472A, MET376B, PHE333A, PRO158B, PRO369B, SER145B, SER354A, SER469A, THR143B, THR147B, THR302A, THR374B, THR414A, TYR146B, TYR154B, TYR442A, VAL345A, VAL349A