PPIRE05784
Target Protein Information
| Protein_Name | Stromelysin-1 |
|---|---|
| Protein_Sequence | MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC |
| Organism_Source | Homo sapiens |
| Functional_Classification | matrix metalloproteinases |
| Cellular_Localization | Extracellular |
| Gene_Names | MMP3 |
| UniProt_ID | P08254 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | Ac-RCGVP |
|---|---|
| Peptide_Sequence | RCGVP |
| Peptide_Length | 5 |
| Peptide_SMILES | CC(C)[C@H](NC(=O)CNC(=O)[C@H](CS)NC(=O)[C@@H](N)CCCNC(=N)N)C(=O)N1CCC[C@H]1C(=O)O |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Acetyl |
| C-terminal_Modification | Free |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 530.64 |
|---|---|
| Aliphatic_Index | 58.00000 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 2.80000 |
| Charge_at_pH_7 | 0.93601 |
| Isoelectric_Point | 8.54991 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 8 |
| Number_of_Hydrogen_Bond_Donors | 9 |
| Topological_Polar_Surface_Area | 232.83000 |
| X_logP_energy | -2.67583 |
Interaction Information
| Affinity | IC50=10 pM |
|---|---|
| Affinity_Assay | Enzyme Inhibition Kinetics |
| PDB_ID | None |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Peptides based on the conserved predomain sequence of matrix metalloproteinases inhibit human stromelysin and collagenase. |
| Release_Year | 1993 |
| PMID | 8273554 |
| DOI | 10.1007/bf01972749 |