3NVL

crystal structure of phosphoglycerate mutase from trypanosoma brucei

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 91
  • Norm. En. per Res.: -1.8695
• 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	-10.117	20.0362	-180.04	-170.1207	91	7	0	7027	1	54	41

Interface residues

• A-B: ALA222A, ALA222B, ALA230A, ALA230B, ALA246A, ALA246B, ALA485A, ALA485B, ARG218A, ARG218B, ARG221A, ARG221B, ARG229A, ARG229B, ARG242A, ARG242B, ARG475A, ARG475B, ARG483A, ARG483B, ASN247A, ASN247B, ASN301A, ASN301B, ASN488A, ASN488B, ASP245A, ASP245B, ASP476A, ASP476B, ASP484A, ASP484B, GLU217A, GLU217B, GLU227A, GLU227B, GLU243A, GLU243B, GLU244A, GLU244B, GLU486A, GLU486B, GLY226A, GLY226B, GLY228A, GLY228B, GLY479A, GLY479B, GLY487A, GLY487B, ILE248A, ILE248B, LEU225A, LEU225B, LEU489A, LEU489B, LYS240A, LYS240B, LYS477A, LYS477B, LYS478A, LYS478B, LYS480A, LYS480B, PHE203A, PHE203B, PHE231A, PHE231B, PHE241A, PHE241B, PHE256A, PHE256B, PHE300A, PHE300B, PRO254A, PRO254B, PRO255A, PRO255B, PRO481A, PRO481B, SER214A, SER214B, TYR252A, TYR252B, TYR32A, VAL257A, VAL257B, VAL303A, VAL303B, VAL482A, VAL482B