Human 14-3-3 sigma in complex with human Estrogen Receptor alpha peptide. Determined by X-ray diffraction at 1.19 Å resolution. Released 17 Feb 2021.
Explore 7NFW in 3D Show helices and sheets RCSB PDB PDBe
7NFW contains 14 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 | 167-178 | 12 | |
| α-helix | 179-183 | 5 | |
| α-helix | 187-202 | 16 | |
| α-helix | 205-207 | 3 | |
| α-helix | 210-230 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein sigma | A | protein | 276 | Homo sapiens | P31947 (AlphaFold model) |
| Estrogen receptor | B | protein | 8 | Homo sapiens | P03372 (AlphaFold model) |
>7NFW_1 14-3-3 protein sigma (chains A) MSYYHHHHHHDYDIPTTENLYFQGAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEK GEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETEL QGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQ EAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDS YKDSTLIMQLLRDNLTLWTADNAGEEGGEAPQEPQS
>7NFW_2 Estrogen receptor (chains B) AEGFPATV
Cooperative stabilisation of 14-3-3 sigma protein-protein interactions via covalent protein modification. Falcicchio, M., Ward, J.A., Chothia, S.Y. et al. Chem Sci (2021) 12:12985-12992. DOI 10.1039/d1sc02120f · 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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