The Crystal Structure of Prp20p from Saccharomyces cerevisiae and Its Binding Properties to Gsp1p and Histones. Determined by X-ray diffraction at 1.9 Å resolution. Released 23 Mar 2011.
Explore 3OF7 in 3D Show helices and sheets RCSB PDB PDBe
3OF7 contains 16 α-helices and 33 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 33-36 | 4 | |
| α-helix | 37-40 | 4 | |
| β-strand | 47-53 | 7 | 1 |
| α-helix | 65-68 | 4 | |
| β-strand | 69-75 | 7 | 1 |
| β-strand | 86-91 | 6 | 2 |
| β-strand | 95-100 | 6 | 2 |
| α-helix | 104 | 1 | |
| β-strand | 105-109 | 5 | 2 |
| α-helix | 145-148 | 4 | |
| β-strand | 151-152 | 2 | 2 |
| α-helix | 153-154 | 2 | |
| α-helix | 155-157 | 3 | |
| α-helix | 159-162 | 4 | |
| β-strand | 167-172 | 6 | 3 |
| β-strand | 176-181 | 6 | 3 |
| β-strand | 186-190 | 5 | 3 |
| β-strand | 192-194 | 3 | 4 |
| β-strand | 197-200 | 4 | 4 |
| β-strand | 202 | 1 | 5 |
| β-strand | 206 | 1 | 5 |
| β-strand | 209-214 | 6 | 3 |
| α-helix | 215-217 | 3 | |
| β-strand | 223-228 | 6 | 6 |
| β-strand | 232-237 | 6 | 6 |
| β-strand | 242-246 | 5 | 6 |
| α-helix | 259-261 | 3 | |
| β-strand | 269-270 | 2 | 6 |
| β-strand | 276-281 | 6 | 7 |
| β-strand | 285-290 | 6 | 7 |
| β-strand | 295-300 | 6 | 7 |
| β-strand | 317-323 | 7 | 7 |
| α-helix | 324-325 | 2 | |
| α-helix | 330-331 | 2 | |
| β-strand | 332-337 | 6 | 8 |
| β-strand | 341-346 | 6 | 8 |
| β-strand | 351-356 | 6 | 8 |
| α-helix | 366-368 | 3 | |
| β-strand | 374-375 | 2 | 8 |
| β-strand | 381-389 | 9 | 8 |
| β-strand | 396-401 | 6 | 9 |
| β-strand | 405-410 | 6 | 9 |
| β-strand | 415-419 | 5 | 9 |
| α-helix | 434 | 1 | |
| β-strand | 435-440 | 6 | 9 |
| β-strand | 449-456 | 8 | 1 |
| β-strand | 460-467 | 8 | 1 |
| α-helix | 468-469 | 2 | |
| α-helix | 470-481 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulator of chromosome condensation | A | protein | 473 | Saccharomyces cerevisiae | P21827 (AlphaFold model) |
>3OF7_1 Regulator of chromosome condensation (chains A) MGHHHHHHMSHIINAQEDYKHMYLSVQPLDIFCWGTGSMCELGLGPLAKNKEVKRPRLNP FLPRDEAKIISFAVGGMHTLALDEESNVWSWGCNDVGALGRDTSNAKEQLKDMDADDSSD DEDGDLNELESTPAKIPRESFPPLAEGHKVVQLAATDNMSCALFSNGEVYAWGTFRCNEG ILGFYQDKIKIQKTPWKVPTFSKYNIVQLAPGKDHILFLDEEGMVFAWGNGQQNQLGRKV MERFRLKTLDPRPFGLRHVKYIASGENHCFALTKDNKLVSWGLNQFGQCGVSEDVEDGAL VTKPKRLALPDNVVIRSIAAGEHHSLILSQDGDLYSCGRLDMFEVGIPKDNLPEYTYKDV HGKARAVPLPTKLNNVPKFKSVAAGSHHSVAVAQNGIAYSWGFGETYAVGLGPFEDDTEV PTRIKNTATQDHNIILVGCGGQFSVSGGVKLSDEDAEKRADEMDDLEHHHHHH
The 1.9A crystal structure of Prp20p from Saccharomyces cerevisiae and its binding properties to Gsp1p and histones. Wu, F., Liu, Y., Zhu, Z. et al. J Struct Biol (2011) 174:213-222. DOI 10.1016/j.jsb.2010.11.016 · PubMed
Other PDB entries of the same protein (UniProt P21827 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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