Synaptotagmin-1 C2B domain with phosphoserine. Determined by X-ray diffraction at 1.5 Å resolution. Released 20 Mar 2013.
Explore 2YOA in 3D Show helices and sheets RCSB PDB PDBe
2YOA contains 12 α-helices and 18 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 275-283 | 9 | 1 |
| α-helix | 284-286 | 3 | |
| β-strand | 288-297 | 10 | 1 |
| α-helix | 299-301 | 3 | |
| β-strand | 310-318 | 9 | 2 |
| β-strand | 321-327 | 7 | 2 |
| α-helix | 328-330 | 3 | |
| β-strand | 338-346 | 9 | 1 |
| α-helix | 349-352 | 4 | |
| β-strand | 355-363 | 9 | 2 |
| β-strand | 371-379 | 9 | 2 |
| α-helix | 384-395 | 12 | |
| β-strand | 401-406 | 6 | 1 |
| β-strand | 408 | 1 | 2 |
| α-helix | 410-417 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 275-283 | 9 | 3 |
| α-helix | 284-286 | 3 | |
| β-strand | 288-297 | 10 | 3 |
| α-helix | 299-301 | 3 | |
| β-strand | 310-318 | 9 | 4 |
| β-strand | 321-327 | 7 | 4 |
| α-helix | 328-330 | 3 | |
| β-strand | 338-346 | 9 | 3 |
| α-helix | 349-354 | 6 | |
| β-strand | 355-363 | 9 | 4 |
| β-strand | 371-379 | 9 | 4 |
| α-helix | 384-395 | 12 | |
| β-strand | 401-406 | 6 | 3 |
| β-strand | 408 | 1 | 4 |
| α-helix | 410-417 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Synaptotagmin-1 | A, B | protein | 152 | RATTUS NORVEGICUS | P21707 (AlphaFold model) |
>2YOA_1 SYNAPTOTAGMIN-1 (chains A, B) MEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTT IKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRH WSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK
Phosphatidylinositol 4,5-Bisphosphate Clusters Act as Molecular Beacons for Vesicle Recruitment. Honigmann, A., Van Den Bogaart, G., Iraheta, E. et al. Nat Struct Mol Biol (2013) 20:679. DOI 10.1038/NSMB.2570 · PubMed
Other PDB entries of the same protein (UniProt P21707 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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