Crystal structure of C-terminal modified Tau peptide-hybrid 126B with 14-3-3sigma. Determined by X-ray diffraction at 1.4 Å resolution. Released 13 Jan 2016.
Explore 4Y5I in 3D Show helices and sheets RCSB PDB PDBe
4Y5I contains 26 α-helices and 0 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 | 3-15 | 13 | |
| α-helix | 19-30 | 12 | |
| α-helix | 34-37 | 4 | |
| α-helix | 38-69 | 32 | |
| α-helix | 80-102 | 23 | |
| α-helix | 103-107 | 5 | |
| α-helix | 114-134 | 21 | |
| α-helix | 138-161 | 24 | |
| α-helix | 167-182 | 16 | |
| α-helix | 187-204 | 18 | |
| α-helix | 205-207 | 3 | |
| α-helix | 210-230 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-30 | 12 | |
| α-helix | 34-37 | 4 | |
| α-helix | 38-68 | 31 | |
| α-helix | 80-102 | 23 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-134 | 21 | |
| α-helix | 138-161 | 24 | |
| α-helix | 167-178 | 12 | |
| α-helix | 179-183 | 5 | |
| α-helix | 187-202 | 16 | |
| α-helix | 205-207 | 3 | |
| α-helix | 210-229 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein sigma | A, B | protein | 236 | Homo sapiens | P31947 (AlphaFold model) |
| Microtubule-associated protein tau | F, G | protein | 9 | Homo sapiens | P10636 (AlphaFold model) |
>4Y5I_1 14-3-3 protein sigma (chains A, B) GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQ RAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAE SRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALN FSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
>4Y5I_2 Microtubule-associated protein tau (chains F, G) XRTPSLPTX
Stabilizer-Guided Inhibition of Protein-Protein Interactions. Milroy, L.G., Bartel, M., Henen, M.A. et al. Angew Chem Int Ed Engl (2015) 54:15720-15724. DOI 10.1002/anie.201507976 · PubMed
Other PDB entries of the same protein (UniProt P31947 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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