PPIRE01519

Target Protein Information
Protein_Name Cathepsin E
Protein_Sequence MKTLLLLLLVLLELGEAQGSLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESVTEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYMSSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRGNNRVGLAPAVP
Organism_Source Homo sapiens
Functional_Classification aspartic proteases
Cellular_Localization lysosome
Gene_Names CTSE
UniProt_ID P14091
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name L-364,099
Peptide_Sequence HPFHX
Peptide_Length 5
Peptide_SMILES N[C@@H](Cc1c[nH]cn1)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)NCC(=O)O
Chemical_Modification X6=4-amino-5-cyclohexyl-3-hydroxypentanoic acid
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Isovaleryl
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 593.64
Aliphatic_Index 0.00000
Aromaticity 0.20000
Average_Rotatable_Bonds 2.80000
Charge_at_pH_7 0.17980
Isoelectric_Point 7.71436
Number_of_Hydrogen_Bond_Acceptors 8
Number_of_Hydrogen_Bond_Donors 7
Topological_Polar_Surface_Area 228.29000
X_logP_energy -1.35060
Interaction Information
Affinity Ki=60 nM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID None
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title X-ray studies of aspartic proteinase-statine inhibitor complexes.
Release_Year 1989
PMID 2690945
DOI 10.1021/bi00447a049