PPIRE10054

Target Protein Information
Protein_Name Protein farnesyltransferase subunit beta
Protein_Sequence MASSSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQKPVPGFEECEDAVTSDPATD
Organism_Source Rattus norvegicus
Functional_Classification prenyltransferases
Cellular_Localization Cytoplasm
Gene_Names Fntb
UniProt_ID Q02293
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name KKKSKTKCVIM
Peptide_Sequence KKKSKTKCVIM
Peptide_Length 11
Peptide_SMILES CC[C@H](C)[C@H](NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCCCN)[C@@H](C)O)C(C)C)C(=O)N[C@@H](CCSC)C(=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 1293.69
Aliphatic_Index 61.81818
Aromaticity 0.00000
Average_Rotatable_Bonds 4.54545
Charge_at_pH_7 4.93453
Isoelectric_Point 10.97880
Number_of_Hydrogen_Bond_Acceptors 21
Number_of_Hydrogen_Bond_Donors 20
Topological_Polar_Surface_Area 524.88000
X_logP_energy -4.35060
Interaction Information
Affinity IC50=50 nM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID 1D8D
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Identification, functional gastrointestinal stability and molecular docking studies of lentil peptides with dual antioxidant and angiotensin I converting enzyme inhibitory activities.
Release_Year 2000
PMID None
DOI 10.1016/S0969-2126(00)80012-8