PPIRE01307

Target Protein Information
Protein_Name Procathepsin L
Protein_Sequence MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV
Organism_Source Homo sapiens
Functional_Classification cysteine proteases
Cellular_Localization lysosome
Gene_Names CTSL
UniProt_ID P07711
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name p41 fragment
Peptide_Sequence XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
Peptide_Length 65
Peptide_SMILES NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)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 None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 3726.39
Aliphatic_Index 0.00000
Aromaticity 0.00000
Average_Rotatable_Bonds 1.98462
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 66
Number_of_Hydrogen_Bond_Donors 66
Topological_Polar_Surface_Area 1925.72000
X_logP_energy -57.53350
Interaction Information
Affinity Ki=1.7 pM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID 1ICF
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S.
Release_Year 1999
PMID 10022822
DOI 10.1093/emboj/18.4.793