3FX6

x-ray crystallographic studies on the complex of carboxypeptidase a with the inhibitor using alpha-nitro ketone as the zinc-binding group

• Total interactions analyzed: 3
• Total true interactions: 3
• Strongest Interaction:
  • Chains: C-E
  • Int. Res.: 31
  • Norm. En. per Res.: -1.8267
• Hub Node: A(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
A-C	-19.3652	19.121	-106.174	-106.4182	82	5	0	4884	0	31	21
A-E	0.0	0.0	-0.3252	-0.3252	5	0	0	71	0	1	2
C-E	-10.782	-3.4557	-42.3914	-56.6291	31	2	0	1665	0	5	8

Interface residues

• A-C: ALA117A, ALA154C, ALA156C, ALA1A, ALA250C, ALA27A, ARG127C, ARG130A, ARG145C, ARG276C, ARG2A, ARG40A, ARG45A, ARG71C, ASP114A, ASP16A, ASP20A, ASP23A, ASP273C, CYS138C, CYS161C, GLN122A, GLN249C, GLN37A, GLU163C, GLU17A, GLU43A, GLY155C, GLY167C, GLY241C, GLY275C, GLY278C, GLY44A, HIS120A, HIS166C, ILE243C, ILE244C, ILE247C, LEU125C, LEU137C, LEU15A, LEU201C, LEU24A, LEU280C, LEU281C, LYS128C, LYS168C, LYS239C, LYS35A, PHE118A, PHE151C, PHE21A, PHE279C, PRO160C, PRO46A, SER121A, SER131A, SER135C, SER136C, SER157C, SER158C, SER159C, SER162C, SER199C, SER242C, SER3A, SER41A, THR133C, THR14A, THR164C, THR245C, THR246C, THR274C, THR6A, TYR165C, TYR198C, TYR19A, TYR248C, TYR277C, TYR42A, TYR48A, VAL132A
• A-E: ARG276A, ASP215E, LYS264E, PRO214E, TYR277A
• C-E: ALA154C, ARG40E, ASN171E, ASN58E, ASP181E, ASP185E, GLN211C, GLN249C, GLY39E, HIS186E, ILE213C, ILE244C, ILE38E, LEU36E, LYS153C, LYS177E, LYS184E, LYS216C, PHE182E, PRO214C, SER178E, SER212C, THR209C, THR210C, THR217C, THR245C, TYR169E, TYR208C, VAL174E, VAL180E, VAL183E