2GHV

crystal structure of sars spike protein receptor binding domain

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: E-C
  • Int. Res.: 87
  • Norm. En. per Res.: -4.3788
• Hub Node: E(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
E-C	-66.1548	2.6009	-317.401	-380.9549	87	12	15	12605	0	2	7

Interface residues

• E-C: ALA350C, ALA350E, ALA371C, ALA371E, ASN330C, ASN330E, ASN357C, ASN357E, ASN375C, ASN375E, ASP351C, ASP351E, ASP376C, ASP376E, CYS366C, CYS366E, CYS378C, CYS378E, CYS419C, CYS419E, GLY326C, GLY326E, GLY368C, GLY368E, GLY418C, GLY418E, LEU355C, LEU355E, LEU374C, LEU374E, LEU377C, LEU377E, LEU421C, LEU421E, LEU499C, LEU499E, LYS365C, LYS365E, LYS373C, LYS373E, MET417C, MET417E, PHE325C, PHE325E, PHE329C, PHE329E, PHE360C, PHE360E, PHE361C, PHE361E, PHE364C, PHE364E, PHE379C, PHE379E, PHE501C, PHE501E, SER353C, SER353E, SER358C, SER358E, SER362C, SER362E, SER370C, SER370E, THR359C, THR359E, THR363C, THR363E, THR372C, THR372E, TRP423C, TRP423E, TYR352C, TYR352E, TYR356C, TYR356E, TYR367C, TYR367E, VAL349C, VAL354C, VAL354E, VAL369C, VAL369E, VAL420C, VAL420E, VAL497C, VAL497E