PPIRE05849
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 | Pep5 |
|---|---|
| Peptide_Sequence | TPGVY |
| Peptide_Length | 5 |
| Peptide_SMILES | CC(C)[C@H](NC(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H](N)[C@@H](C)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Free |
| C-terminal_Modification | Free |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 535.60 |
|---|---|
| Aliphatic_Index | 58.00000 |
| Aromaticity | 0.20000 |
| Average_Rotatable_Bonds | 2.40000 |
| Charge_at_pH_7 | -0.00287 |
| Isoelectric_Point | 6.09320 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 8 |
| Number_of_Hydrogen_Bond_Donors | 7 |
| Topological_Polar_Surface_Area | 211.39000 |
| X_logP_energy | -1.53980 |
Interaction Information
| Affinity | Ki=34 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 |