S. Cerevisiae SWI6 ankyrin-repeat fragment. Determined by X-ray diffraction at 2.1 Å resolution. Released 15 Sept 1999.
Explore 1SW6 in 3D Show helices and sheets RCSB PDB PDBe
1SW6 contains 37 α-helices and 12 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 | 214-216 | 3 | 1 |
| α-helix | 230 | 1 | |
| β-strand | 233-234 | 2 | 2 |
| α-helix | 235 | 1 | |
| β-strand | 236 | 1 | 3 |
| α-helix | 237-239 | 3 | |
| α-helix | 244-258 | 15 | |
| α-helix | 292-302 | 11 | |
| α-helix | 321-327 | 7 | |
| α-helix | 331-339 | 9 | |
| β-strand | 346 | 1 | 3 |
| α-helix | 354-360 | 7 | |
| α-helix | 363-366 | 4 | |
| α-helix | 370-377 | 8 | |
| α-helix | 378-382 | 5 | |
| β-strand | 383-384 | 2 | 2 |
| α-helix | 391-399 | 9 | |
| α-helix | 405-421 | 17 | |
| α-helix | 422-424 | 3 | |
| β-strand | 427-429 | 3 | 1 |
| α-helix | 448-452 | 5 | |
| α-helix | 455-458 | 4 | |
| α-helix | 459-463 | 5 | |
| α-helix | 473-480 | 8 | |
| α-helix | 483-491 | 9 | |
| α-helix | 506-509 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 214-216 | 3 | 4 |
| β-strand | 233-234 | 2 | 5 |
| α-helix | 235 | 1 | |
| β-strand | 236 | 1 | 6 |
| α-helix | 237-239 | 3 | |
| α-helix | 244-257 | 14 | |
| α-helix | 292-302 | 11 | |
| α-helix | 321-327 | 7 | |
| α-helix | 331-339 | 9 | |
| β-strand | 346 | 1 | 6 |
| α-helix | 354-360 | 7 | |
| α-helix | 367-377 | 11 | |
| α-helix | 378-382 | 5 | |
| β-strand | 383-384 | 2 | 5 |
| α-helix | 391-401 | 11 | |
| α-helix | 408-421 | 14 | |
| α-helix | 422-424 | 3 | |
| β-strand | 427-429 | 3 | 4 |
| α-helix | 448-452 | 5 | |
| α-helix | 455-461 | 7 | |
| α-helix | 473-480 | 8 | |
| α-helix | 483-492 | 10 | |
| α-helix | 506-509 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulatory protein SWI6 | A, B | protein | 327 | Saccharomyces cerevisiae | P09959 (AlphaFold model) |
>1SW6_1 REGULATORY PROTEIN SWI6 (chains A, B) NDDINKGPSGDNENNGTDDNDRTAGPIITFTHDLTSDFLSSPLKIMKALPSPVVNDNEQK MKLEAFLQRLLFPEIQEMPTSLNNDSSNRNSEGGSSNQQQQHVSFDSLLQEVNDAFPNTQ LNLNIPVDEHGNTPLHWLTSIANLELVKHLVKHGSNRLYGDNMGESCLVKAVKSVNNYDS GTFEALLDYLYPCLILEDSMNRTILHHIIITSGMTGCSAAAKYYLDILMGWIVKKQNRPI QSGTNEKESKPNDKNGERKDSILENLDLKWIIANMLNAQDSNGDTCLNIAARLGNISIVD ALLDYGADPFIANKSGLRPVDFGAGLE
X-ray structural analysis of the yeast cell cycle regulator Swi6 reveals variations of the ankyrin fold and has implications for Swi6 function. Foord, R., Taylor, I.A., Sedgwick, S.G. et al. Nat Struct Biol (1999) 6:157-165. DOI 10.1038/5845 · PubMed
Other PDB entries of the same protein (UniProt P09959 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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