8PCH

crystal structure of porcine cathepsin h determined at 2.1 angstrom resolution: location of the mini-chain c-terminal carboxyl group defines cathepsin h aminopeptidase function

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-P
  • Int. Res.: 60
  • Norm. En. per Res.: 10.5386
• 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-P	-24.62	0.0	656.935	632.315	60	12	0	4789	0	0	2

Interface residues

• A-P: ALA111A, ALA133A, ALA160A, ALA203A, ALA204A, ALA206A, ALA82P, ASN112A, ASN116A, ASN158A, ASN59A, ASN60A, ASN79P, ASP155A, CYS205A, CYS25A, CYS63A, CYS80P, GLN19A, GLN64A, GLN70A, GLN78P, GLU135A, GLU73A, GLU76P, GLY201A, GLY23A, GLY62A, GLY65A, GLY66A, HIS159A, HIS61A, ILE113A, LEU67A, LYS156A, MET115A, MET121A, PHE132A, PHE134A, PHE72A, PRO155A, PRO68A, PRO77P, SER131A, SER207A, SER24A, SER29A, SER69A, SER81P, THR114A, THR155A, THR27A, THR83P, TRP26A, TYR208A, VAL110A, VAL130A, VAL136A, VAL157A, VAL161A