PPIRE01328
Target Protein Information
| Protein_Name | None |
|---|---|
| Protein_Sequence | MRCSTLTLTLVVLLAAECAFGAFRIPLTRFKSVRKQLAEEGIYIHEGPYPEPLVNLLDVEYYGPISIGTPPQDFQVIFDTGSANLWLPSSKCTTKYCLHHHRYDSSKSSTYEADGRNFTIVYGSGNVEGFISKDVCRIGSAKVSGQPLGEALVVGGESLLEAPFDGILGLAYPSIAVDGVVPVFDNMMKQGLLGEQNVFSVYRNRDPSSKEGGEVLFGGIDHDHYKGSITYVPVTAKGYWQFHVDGVKSVSASKSAPELLCKDGCEAIADTGTSLITGPPEEVDSLNQYLGGTKTEGGQYLLDCDKLESLPNVTFTISGKEFSLRSKDYVLKVNQQGQTLCVSGFMGLEMPQPLWILGDVFLGPYYTIFDRDQDRVGFAEVA |
| Organism_Source | Ixodes ricinus |
| Functional_Classification | peptidases |
| Cellular_Localization | lysosome |
| Gene_Names | None |
| UniProt_ID | V5HCK7 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | IrCD1 propeptide fragment [1-8] |
|---|---|
| Peptide_Sequence | XFRIPLXR |
| Peptide_Length | 8 |
| Peptide_SMILES | CC[C@H](C)[C@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](Cc1ccccc1)NC(=O)CN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)O |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Free |
| C-terminal_Modification | amide |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 915.11 |
|---|---|
| Aliphatic_Index | 97.50000 |
| Aromaticity | 0.12500 |
| Average_Rotatable_Bonds | 3.50000 |
| Charge_at_pH_7 | 1.99798 |
| Isoelectric_Point | 12.50011 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 11 |
| Number_of_Hydrogen_Bond_Donors | 14 |
| Topological_Polar_Surface_Area | 382.03000 |
| X_logP_energy | -2.57766 |
Interaction Information
| Affinity | KD=3 nM |
|---|---|
| Affinity_Assay | MicroScale Thermophoresis |
| PDB_ID | 5N70 |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Novel Structural Mechanism of Allosteric Regulation of Aspartic Peptidases via an Evolutionarily Conserved Exosite. |
| Release_Year | 2018 |
| PMID | 29396291 |
| DOI | 10.1016/j.chembiol.2018.01.001 |