PPIRE07564

Target Protein Information
Protein_Name Chymotrypsin-C
Protein_Sequence MLGITVFTTFLAYASSCGAPIFQPNLSARVVGGEDAIPHSWPWQISLQYLRDNTWRHTCGGTLITPNHVLTAAHCISNTLTYRVALGKNNLEVEDEAGSLYVGVDTIFVHEKWNSFLVRNDIALIKLAETVELSDTIQVACLPEEGSLLPQDYPCFVTGWGRLYTNGPIAAELQQGLQPVVDYATCSQRDWWGTTVKETMVCAGGDGVISACNGDSGGPLNCQAENGNWDVRGIVSFGSGLSCNTFKKPTVFTRVSAYIDWINQKLQL
Organism_Source Bos taurus
Functional_Classification serine proteases
Cellular_Localization Extracellular
Gene_Names CTRC
UniProt_ID Q7M3E1
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name Pep8
Peptide_Sequence AVPGSWPW
Peptide_Length 8
Peptide_SMILES CC(C)[C@H](NC(=O)[C@H](C)N)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1c[nH]c2ccccc12)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 899.02
Aliphatic_Index 48.75000
Aromaticity 0.25000
Average_Rotatable_Bonds 2.37500
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 10
Number_of_Hydrogen_Bond_Donors 10
Topological_Polar_Surface_Area 301.25000
X_logP_energy -0.44810
Interaction Information
Affinity Ki=0.99 nM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID None
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Detection of native peptides as potent inhibitors of enzymes. Crystal structure of the complex formed between treated bovine alpha-chymotrypsin and an autocatalytically produced fragment, IIe-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp, at 2.2 angstroms resolution.
Release_Year 2005
PMID 15654893
DOI 10.1111/j.1742-4658.2004.04499.x