PPIST17886
Protein Information
| Protein_Chain | A;B;C;D;E;F |
|---|---|
| Protein_Sequence | DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF |
Peptide Information
| Peptide_Chain | G[auth M];H[auth N];I[auth O];J[auth P];K[auth Q];L[auth R];M[auth S] |
|---|---|
| Peptide_Sequence | WXATCPA |
| Peptide_Length | 7 |
| Non-standard residues | Yes |
Interaction Information
| PDB_ID | 9DUU |
|---|---|
| Method | ELECTRON MICROSCOPY |
| Resolution | 3.40 angstrom |
| Structure | |
| Protein-peptide residue interaction | |
| Interaction_xlsx | Download interaction table (.xlsx) |
Reference Information
| Title | Dilated cardiomyopathy-associated skeletal muscle actin (ACTA1) mutation R256H disrupts actin structure and function and causes cardiomyocyte hypocontractility. |
|---|---|
| Release_Year | 2024 |
| PMID | 39503885 |
| DOI | 10.1073/pnas.2405020121 |