PPIRE05106
Target Protein Information
| Protein_Name | Renin |
|---|---|
| Protein_Sequence | MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR |
| Organism_Source | Homo sapiens |
| Functional_Classification | aspartic proteases |
| Cellular_Localization | Extracellular |
| Gene_Names | REN |
| UniProt_ID | P00797 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | RYLP |
|---|---|
| Peptide_Sequence | RYLP |
| Peptide_Length | 4 |
| Peptide_SMILES | CC(C)C[C@H](NC(=O)[C@H](Cc1ccc(O)cc1)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 | Free |
| C-terminal_Modification | Free |
| Amino_Acid_Distribution | |
|
|
|
Peptide Physicochemical
| Molecular_Weight | 547.65 |
|---|---|
| Aliphatic_Index | 97.50000 |
| Aromaticity | 0.25000 |
| Average_Rotatable_Bonds | 3.50000 |
| Charge_at_pH_7 | 0.99713 |
| Isoelectric_Point | 9.34881 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 7 |
| Number_of_Hydrogen_Bond_Donors | 8 |
| Topological_Polar_Surface_Area | 223.96000 |
| X_logP_energy | -0.38343 |
Interaction Information
| Affinity | IC50=0.54 mM |
|---|---|
| Affinity_Assay | Enzyme Inhibition Kinetics |
| PDB_ID | None |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Structure-based design and optimization of antihypertensive peptides to obtain high inhibitory potency against both renin and angiotensin I-converting enzyme. |
| Release_Year | 2015 |
| PMID | 26524626 |
| DOI | 10.1080/1062936X.2015.1104725 |