PPIRE06685
Target Protein Information
| Protein_Name | Candidapepsin-1 |
|---|---|
| Protein_Sequence | MVAIVTLTRQVLLTIALALFAQGAAIPEEAAKRDDNPGFVALDFDVLRKPLNLTEALLREKRDSISLSLINEGPSYASKVSVGSNKQQQTVIIDTGSSDFWVVDSNAQCGKGVDCKSSGTFTPSSSSSYKNLGAAFTIRYGDGSTSQGTWGKDTVTINGVSITGQQIADVTQTSVDQGILGIGYTSNEAVYDTSGRQTTPNYDNVPVTLKKQGKIRTNAYSLYLNSPSAETGTIIFGGVDNAKYSGKLVAEQVTSSQPLTISLASVNLKGSSFSFGDGALLDSGTTLTYFPSDFAAQLADKAGARLVQVARDQYLYFIDCNTDTSGTTVFNFGNGAKITVPNTEYVYQNGDGTCLWGIQPSDDTILGDNFLRHAYYLLYNLDANTISIAQVKYTTDSSISAV |
| Organism_Source | Candida parapsilosis |
| Functional_Classification | proteases |
| Cellular_Localization | Extracellular |
| Gene_Names | SAPP1 |
| UniProt_ID | P32951 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | pepstatin A |
|---|---|
| Peptide_Sequence | VVXVVX |
| Peptide_Length | 6 |
| Peptide_SMILES | CC(C)[C@H](N)C(=O)N[C@H](C(=O)NCC(=O)N[C@H](C(=O)N[C@H](C(=O)NCC(=O)O)C(C)C)C(C)C)C(C)C |
| Chemical_Modification | X3=statine; X6=statine |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Isovaleryl |
| C-terminal_Modification | Free |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 528.65 |
|---|---|
| Aliphatic_Index | 193.33333 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 2.50000 |
| Charge_at_pH_7 | -0.00202 |
| Isoelectric_Point | 6.10000 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 7 |
| Number_of_Hydrogen_Bond_Donors | 7 |
| Topological_Polar_Surface_Area | 208.82000 |
| X_logP_energy | -1.29090 |
Interaction Information
| Affinity | Ki=0.3 nM |
|---|---|
| Affinity_Assay | Enzyme Inhibition Kinetics |
| PDB_ID | 3FV3 |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | The crystal structure of the secreted aspartic protease 1 from Candida parapsilosis in complex with pepstatin A. |
| Release_Year | 2009 |
| PMID | 19401235 |
| DOI | 10.1016/j.jsb.2009.04.004 |