PPIST09705
Protein Information
| Protein_Chain | B/A |
|---|---|
| Protein_Sequence | XDEVDX/MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIQSMLTKELYFYH |
Peptide Information
| Peptide_Chain | C[auth D] |
|---|---|
| Peptide_Sequence | DDDM |
| Peptide_Length | 4 |
| Non-standard residues | No |
Interaction Information
| PDB_ID | 5IAG |
|---|---|
| Method | X-RAY DIFFRACTION |
| Resolution | 1.98 angstrom |
| Structure | |
| Protein-peptide residue interaction | |
| Interaction_xlsx | Download interaction table (.xlsx) |
Reference Information
| Title | Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection. |
|---|---|
| Release_Year | 2016 |
| PMID | 27681633 |
| DOI | 10.1073/pnas.1603549113 |