PPIRE10318

Target Protein Information
Protein_Name Peptidyl-prolyl cis-trans isomerase
Protein_Sequence MRFVAVLAVVLCALSFLNVAAEPEVTAKVYFDVMIDSEPLGRITIGLFGKDAPLTTENFRQLCTGEHGFGYKDSIFHRVIQNFMIQGGDFTNFDGTGGKSIYGEKFADENLNVKHFVGALSMANAGPNTNGSQFFITTAPTPWLDGRHVVFGKVLDGMDVVLRIEKTKTNSHDRPVKPVKIVASGEL
Organism_Source Leishmania donovani
Functional_Classification peptidyl-prolyl cis-trans isomerase
Cellular_Localization Cytoplasm
Gene_Names CYP
UniProt_ID Q9U9R3
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name Cyclosporin A
Peptide_Sequence XXXXXXXXXXX
Peptide_Length 11
Peptide_SMILES NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)O
Chemical_Modification None
Cyclization_Method Main chain-main chain cyclization; X1<->X11; amide bond
Linear/Cyclic Cyclic
N-terminal_Modification None
C-terminal_Modification None
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 645.59
Aliphatic_Index 0.00000
Aromaticity 0.00000
Average_Rotatable_Bonds 1.90909
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 12
Number_of_Hydrogen_Bond_Donors 12
Topological_Polar_Surface_Area 354.32000
X_logP_energy -9.80830
Interaction Information
Affinity KD=15.15 nM
Affinity_Assay Isothermal titration calorimetry
PDB_ID 3EOV
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 A resolution: correlation between structure and thermodynamic data.
Release_Year 2009
PMID 19923714
DOI 10.1107/S0907444909034234