Crystal structure of the quintuple mutant of the synaptotagmin-1 C2B domain. Determined by X-ray diffraction at 1.65 Å resolution. Released 12 Aug 2015.
Explore 5CCJ in 3D Show helices and sheets RCSB PDB PDBe
5CCJ contains 20 α-helices and 36 β-strands across 4 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 |
| 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 | 328-331 | 4 | |
| β-strand | 338-346 | 9 | 1 |
| α-helix | 349-354 | 6 | |
| 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 |
| 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 | 328-332 | 5 | |
| β-strand | 338-346 | 9 | 3 |
| α-helix | 349-351 | 3 | |
| 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 | 410-418 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 275-283 | 9 | 5 |
| β-strand | 288-297 | 10 | 5 |
| β-strand | 310-318 | 9 | 6 |
| β-strand | 321-327 | 7 | 6 |
| α-helix | 328-332 | 5 | |
| β-strand | 338-346 | 9 | 5 |
| α-helix | 349-354 | 6 | |
| β-strand | 355-363 | 9 | 6 |
| α-helix | 370 | 1 | |
| β-strand | 371-379 | 9 | 6 |
| α-helix | 384-395 | 12 | |
| β-strand | 401-406 | 6 | 5 |
| β-strand | 408 | 1 | 6 |
| α-helix | 410-417 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 275-283 | 9 | 7 |
| β-strand | 288-297 | 10 | 7 |
| β-strand | 310-318 | 9 | 8 |
| β-strand | 321-327 | 7 | 8 |
| α-helix | 328-331 | 4 | |
| β-strand | 338-346 | 9 | 7 |
| α-helix | 349-351 | 3 | |
| β-strand | 355-363 | 9 | 8 |
| α-helix | 369-370 | 2 | |
| β-strand | 371-379 | 9 | 8 |
| α-helix | 384-395 | 12 | |
| β-strand | 401-406 | 6 | 7 |
| β-strand | 408 | 1 | 8 |
| α-helix | 410-417 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Synaptotagmin-1 | A, B, C, D | protein | 152 | Rattus norvegicus | P21707 (AlphaFold model) |
>5CCJ_1 Synaptotagmin-1 (chains A, B, C, D) SEKLGDICFSLAYVPTAGKLTVVILAAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTT IKKNTLNPWYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRH WSDMLANPAAPIAQWHTLQVEEEVDAMLAVKK
Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis. Zhou, Q., Lai, Y., Bacaj, T. et al. Nature (2015) 525:62-67. DOI 10.1038/nature14975 · 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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