PPIST04301
Protein Information
| Protein_Chain | A[auth B] |
|---|---|
| Protein_Sequence | ITGGSSAVAGQWPWQVSITYEGVHVCGGSLVSEQWVLSAAHCFPSEHHKEAYEVKLGAHQLDSYSEDAKVSTLKDIIPHPSYLQEGSQGDIALLQLSRPITFSRYIRPISLPAAQASFPNGLHCTVTGWGHVAPSVSLLTPKPLQQLEVPLISRETCNSLYNIDAKPEEPHFVQEDMVCAGYVEGGKDACQGDSGGPLSCPVEGLWYLTGIVSWGDACGARNRPGVYTLASSYASWIQSKVTELQPRVVPQTQESQPDSNLHHHHHHHHHH |
Peptide Information
| Peptide_Chain | B[auth A] |
|---|---|
| Peptide_Sequence | FFR |
| Peptide_Length | 3 |
| Non-standard residues | No |
Interaction Information
| PDB_ID | 3E0N |
|---|---|
| Method | X-RAY DIFFRACTION |
| Resolution | 1.70 angstrom |
| Structure | |
| Protein-peptide residue interaction | |
| Interaction_xlsx | Download interaction table (.xlsx) |
Reference Information
| Title | Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations. |
|---|---|
| Release_Year | 2009 |
| PMID | 19388054 |
| DOI | 10.1002/pro.118 |