1PEK

structure of the complex of proteinase k with a substrate-analogue hexa-peptide inhibitor at 2.2 angstroms resolution

• Total interactions analyzed: 3
• Total true interactions: 3
• Strongest Interaction:
  • Chains: E-C
  • Int. Res.: 53
  • Norm. En. per Res.: -2.7844
• Hub Node: E(2)

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	-37.5192	0.0	-110.054	-147.5732	53	15	5	4406	0	0	0
E-D	0.0	0.0	84.1853	84.1853	19	18	0	778	0	0	0
C-D	0.0	0.0	-0.4088	-0.4088	3	0	0	50	0	0	0

Interface residues

• E-C: ALA158E, ALA159E, ALA166E, ALA172E, ALA182E, ALA226E, ALA2C, ASN161E, ASN162E, ASN194E, ASN67E, ASN99E, ASP39E, ASP97E, CYS73E, GLN103E, GLY100E, GLY102E, GLY134E, GLY135E, GLY136E, GLY160E, GLY222E, GLY70E, HIS69E, ILE107E, ILE38E, LEU131E, LEU133E, LEU96E, MET225E, PHE192E, PHE4C, PRO171E, PRO1C, PRO228E, PRO3C, SER101E, SER132E, SER170E, SER173E, SER221E, SER224E, THR179E, THR223E, THR227E, THR40E, TYR104E, TYR137E, TYR169E, VAL157E, VAL180E, VAL95E
• E-D: ALA6D, ARG218E, ASN161E, ASN67E, GLY100E, GLY205E, GLY222E, GLY68E, HIS69E, HIS72E, ILE208E, ILE220E, MET225E, SER207E, SER219E, SER221E, SER224E, THR223E, TRP212E
• C-D: ALA6D, PHE4C, PRO3C