2ISQ

crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 68
  • Norm. En. per Res.: -3.1736
• 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	-30.4919	-0.8764	-184.439	-215.8073	68	13	2	6600	0	10	4

Interface residues

• A-B: ALA122A, ALA128A, ALA228A, ARG105A, ARG301A, ASN153A, ASN77A, ASP120A, ASP904B, GLN147A, GLN224A, GLU72A, GLU901B, GLY124A, GLY127A, GLY181A, GLY183A, GLY184A, GLY219A, GLY225A, GLY227A, GLY229A, GLY76A, GLY79A, GLY81A, HIS221A, ILE129A, ILE180A, ILE223A, ILE226A, ILE268A, ILE49A, ILE907B, LYS123A, LYS126A, LYS217A, LYS222A, LYS46A, MET101A, MET125A, MET97A, PHE148A, PHE230A, PRO121A, PRO207A, PRO218A, PRO220A, PRO232A, PRO73A, PRO98A, SER100A, SER102A, SER210A, SER269A, SER44A, SER75A, SER903B, THR182A, THR305A, THR74A, THR78A, THR900B, TRP902B, TYR302A, TYR905B, VAL45A, VAL80A, VAL906B