14-3-3 sigma with RelA/p65 binding site pS281. Determined by X-ray diffraction at 1.25 Å resolution. Released 13 May 2020.
Explore 6QHM in 3D Show helices and sheets RCSB PDB PDBe
6QHM 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 | 19-31 | 13 | |
| 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 | 140-161 | 22 | |
| α-helix | 167-178 | 12 | |
| α-helix | 179-183 | 5 | |
| 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 | 253 | Homo sapiens | P31947 (AlphaFold model) |
| Leu-sep-glu | P | protein | 13 | Homo sapiens | Q04206 (AlphaFold model) |
>6QHM_1 14-3-3 protein sigma (chains A) GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQ RAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAE SRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALN FSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNA GEEGGEAPQEPQS
>6QHM_2 LEU-SEP-GLU (chains P) PSDRELSEPMEFQ
Selectivity via Cooperativity: Preferential Stabilization of the p65/14-3-3 Interaction with Semisynthetic Natural Products. Wolter, M., de Vink, P., Neves, J.F. et al. J Am Chem Soc (2020) 142:11772-11783. DOI 10.1021/jacs.0c02151 · 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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