14-3-3 isoform sigma in complex with a phosphorylated C-RAF peptide. Determined by X-ray diffraction at 1.7 Å resolution. Released 25 Sept 2013.
Explore 4IEA in 3D Show helices and sheets RCSB PDB PDBe
4IEA 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 | 19-31 | 13 | |
| α-helix | 35-36 | 2 | |
| 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 | 139-161 | 23 | |
| 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 | 236 | Homo sapiens | P31947 (AlphaFold model) |
| RAF proto-oncogene serine/threonine-protein kinase | P | protein | 8 | Homo sapiens | P04049 (AlphaFold model) |
>4IEA_1 14-3-3 protein sigma (chains A) GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQ RAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAE SRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALN FSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
>4IEA_2 RAF proto-oncogene serine/threonine-protein kinase (chains P) RSASEPSL
Stabilization of Physical RAF/14-3-3 Interaction by Cotylenin A as Treatment Strategy for RAS Mutant Cancers. Molzan, M., Kasper, S., Roglin, L. et al. ACS Chem Biol (2013) 8:1869-1875. DOI 10.1021/cb4003464 · 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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