PPIRE04729
Target Protein Information
| Protein_Name | Streptopain |
|---|---|
| Protein_Sequence | MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP |
| Organism_Source | Streptococcus pyogenes |
| Functional_Classification | cysteine proteases |
| Cellular_Localization | Extracellular |
| Gene_Names | speB |
| UniProt_ID | P0C0J0 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | Ac-AEIK-CHO |
|---|---|
| Peptide_Sequence | AEIK |
| Peptide_Length | 4 |
| Peptide_SMILES | CC[C@H](C)[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)N)C(=O)N[C@@H](CCCCN)C(=O)O |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Acetyl |
| C-terminal_Modification | aldehyde |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 459.54 |
|---|---|
| Aliphatic_Index | 122.50000 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 4.00000 |
| Charge_at_pH_7 | -0.00054 |
| Isoelectric_Point | 6.40880 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 7 |
| Number_of_Hydrogen_Bond_Donors | 7 |
| Topological_Polar_Surface_Area | 213.94000 |
| X_logP_energy | -1.08750 |
Interaction Information
| Affinity | IC50=205 nM |
|---|---|
| Affinity_Assay | Enzyme Inhibition Kinetics |
| PDB_ID | 4D8I |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Ultrahigh and high resolution structures and mutational analysis of monomeric Streptococcus pyogenes SpeB reveal a functional role for the glycine-rich C-terminal loop. |
| Release_Year | 2012 |
| PMID | 22645124 |
| DOI | 10.1074/jbc.M112.361576 |