3PMP

crystal structure of cyclophilin a from moniliophthora perniciosa in complex with cyclosporin a

• Total interactions analyzed: 6
• Total true interactions: 3
• Strongest Interaction:
  • Chains: A-C
  • Int. Res.: 14
  • Norm. En. per Res.: -0.2917
• 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-B	0.0	16.9799	-14.864	2.1159	16	1	0	703	0	10	12
A-C	0.0	0.0	-4.0839	-4.0839	14	0	0	273	0	0	0
B-D	0.0	0.0	-3.8711	-3.8711	14	0	0	267	0	0	0

Interface residues

• A-B: ARG138A, ARG138B, ASP135A, ASP135B, GLU141A, GLU141B, LEU134A, LEU134B, LYS92A, LYS92B, PRO116A, PRO116B, PRO93A, PRO93B, THR91A, THR91B
• A-C: ALA101A, ALA7C, ARG53A, ASN69A, GLN61A, GLY148A, GLY70A, HIS52A, ILE55A, MET59A, PHE58A, SER147A, THR71A, VAL5C
• B-D: ALA101B, ALA7D, ARG53B, ASN69B, GLN61B, GLY148B, GLY70B, HIS52B, ILE55B, MET59B, PHE58B, SER147B, THR71B, VAL5D