Crystal structure of 14-3-3 sigma in complex with Tau pS214 peptide and covalent stabilizer JS17. Determined by X-ray diffraction at 1.45 Å resolution. Released 9 Jul 2025.
Explore 9FVH in 3D Show helices and sheets RCSB PDB PDBe
9FVH contains 13 α-helices and 0 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 | 3-15 | 13 | |
| α-helix | 19-30 | 12 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-69 | 32 | |
| α-helix | 80-102 | 23 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-134 | 21 | |
| α-helix | 140-161 | 22 | |
| α-helix | 167-182 | 16 | |
| α-helix | 187-204 | 18 | |
| α-helix | 205-207 | 3 | |
| α-helix | 210-230 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein sigma | A | protein | 236 | Homo sapiens | P31947 (AlphaFold model) |
| Microtubule-associated protein tau | P | protein | 13 | Homo sapiens | P10636 (AlphaFold model) |
>9FVH_1 14-3-3 protein sigma (chains A) GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQ RAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAE SRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALN FSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
>9FVH_2 Microtubule-associated protein tau (chains P) SRTPSLPTPPTRE
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1IF5 | 2-bromanyl-4-[2-(2-methylphenyl)imidazol-1-yl]benzaldehyde | C17 H13 Br N2 O | 1 |
Site-selective stabilization of the 14-3-3/tau protein-protein interaction. Oberheide, A.O., van den Oetelaar, M.C.M., Scheele, J.J.A. et al. To be published.
Other PDB entries of the same protein (UniProt P31947 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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