PPIST12474
Protein Information
| Protein_Chain | A;C;E;G;I;K |
|---|---|
| Protein_Sequence | GSKPLAEQDWYHGAIPRIEAQELLKKQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQYVDNMYRFEGTGFSNIPQLIDHHYTTKQVITKKSGVVLLNPIPK |
Peptide Information
| Peptide_Chain | B;D;F;H;J;L |
|---|---|
| Peptide_Sequence | DEYENVD |
| Peptide_Length | 7 |
| Non-standard residues | No |
Interaction Information
| PDB_ID | 6KC4 |
|---|---|
| Method | X-RAY DIFFRACTION |
| Resolution | 1.37 angstrom |
| Structure | |
| Protein-peptide residue interaction | |
| Interaction_xlsx | Download interaction table (.xlsx) |
Reference Information
| Title | High-resolution structural analysis shows how different crystallographic environments can induce alternative modes of binding of a phosphotyrosine peptide to the SH2 domain of Fer tyrosine kinase. |
|---|---|
| Release_Year | 2019 |
| PMID | 31441171 |
| DOI | 10.1002/pro.3713 |