PPIRE05926
Target Protein Information
| Protein_Name | Secreted aspartic protease 3 |
|---|---|
| Protein_Sequence | MFLKNIFIALAIALLADATPTTFNNSPGFVALNFDVIKTHKNVTGPQGEINTNVNVKRQTVPVKLINEQVSYASDITVGSNKQKLTVVIDTGSSDLWVPDSQVSCQAGQGQDPNFCKNEGTYSPSSSSSSQNLNSPFSIEYGDGTTSQGTWYKDTIGFGGISITKQQFADVTSTSVDQGILGIGYKTHEAEGNYDNVPVTLKNQGIISKNAYSLYLNSRQATSGQIIFGGVDNAKYSGTLIALPVTSDNELRIHLNTVKVAGQSINADVDVLLDSGTTITYLQQGVADQVISAFNGQETYDANGNLFYLVDCNLSGSVDFAFDKNAKISVPASEFTAPLYTEDGQVYDQCQLLFGTSDYNILGDNFLRSAYIVYDLDDNEISLAQVKYTTASNIAALT |
| Organism_Source | Candida albicans |
| Functional_Classification | aspartic proteinase |
| Cellular_Localization | Extracellular |
| Gene_Names | SAP3 |
| UniProt_ID | P0CY28 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | Pepstatin A |
|---|---|
| Peptide_Sequence | XXXXX |
| Peptide_Length | 5 |
| Peptide_SMILES | NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=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 | 303.27 |
|---|---|
| Aliphatic_Index | 0.00000 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 1.80000 |
| Charge_at_pH_7 | -0.00202 |
| Isoelectric_Point | 6.10000 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 6 |
| Number_of_Hydrogen_Bond_Donors | 6 |
| Topological_Polar_Surface_Area | 179.72000 |
| X_logP_energy | -4.50550 |
Interaction Information
| Affinity | Ki=60 nM |
|---|---|
| Affinity_Assay | Enzyme Inhibition Kinetics |
| PDB_ID | 2H6T |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A. |
| Release_Year | 2007 |
| PMID | 17510964 |
| DOI | 10.1002/prot.21425 |