Crystal structure of renal tumor suppressor protein, folliculin. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Aug 2012.
Explore 3V42 in 3D Show helices and sheets RCSB PDB PDBe
3V42 contains 24 α-helices and 10 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 |
|---|---|---|---|
| α-helix | 349-356 | 8 | |
| α-helix | 358-370 | 13 | |
| β-strand | 373-377 | 5 | 1 |
| α-helix | 381-391 | 11 | |
| α-helix | 392-394 | 3 | |
| α-helix | 397-399 | 3 | |
| β-strand | 402-406 | 5 | 1 |
| β-strand | 417-420 | 4 | 1 |
| α-helix | 424-427 | 4 | |
| α-helix | 428-431 | 4 | |
| β-strand | 436-443 | 8 | 1 |
| β-strand | 463-469 | 7 | 1 |
| α-helix | 481-491 | 11 | |
| α-helix | 497-521 | 25 | |
| α-helix | 530-538 | 9 | |
| α-helix | 544-553 | 10 | |
| α-helix | 554-556 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 349-356 | 8 | |
| α-helix | 358-369 | 12 | |
| β-strand | 373-377 | 5 | 1 |
| α-helix | 381-391 | 11 | |
| α-helix | 392-394 | 3 | |
| α-helix | 397-399 | 3 | |
| β-strand | 402-406 | 5 | 1 |
| β-strand | 417-420 | 4 | 1 |
| α-helix | 428-431 | 4 | |
| β-strand | 436-442 | 7 | 1 |
| β-strand | 464-469 | 6 | 1 |
| α-helix | 472 | 1 | |
| α-helix | 481-491 | 11 | |
| α-helix | 497-521 | 25 | |
| α-helix | 529-538 | 10 | |
| α-helix | 544-553 | 10 | |
| α-helix | 554-556 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Folliculin | A, B | protein | 226 | Homo sapiens | Q8NFG4 (AlphaFold model) |
>3V42_1 Folliculin (chains A, B) RKLPVFKSLRHMRQVLGAPSFRMLAWHVLMGNQVIWKSRDVDLVQSAFEVLRTMLPVGCV RIIPYSSQYEEAYRCNFLGLSPHVQIPPHVLSSEFAVIVEVHAAARSTLHPVGAEDDQSL SKYEFVVTSGSPVAADRVGPTILNKIEAALTNQNLSVDVVDQALVALKEEWMNKVKVLFK FTKVDSRPKEDTQKLLSILGASEEDNVKLLKFWMTGLSKTYKSHLM
Crystal structure of folliculin reveals a hidDENN function in genetically inherited renal cancer. Nookala, R.K., Langemeyer, L., Pacitto, A. et al. Open Biol (2012) 2:120071-120071. DOI 10.1098/rsob.120071 · PubMed
Other PDB entries of the same protein (UniProt Q8NFG4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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