14-3-3 Protein Epsilon (Human) Complexed to Peptide. Determined by X-ray diffraction at 1.75 Å resolution. Released 12 May 2005.
Explore 2BR9 in 3D Show helices and sheets RCSB PDB PDBe
2BR9 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 | 4-17 | 14 | |
| α-helix | 20-31 | 12 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-73 | 35 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-111 | 3 | |
| α-helix | 115-135 | 21 | |
| α-helix | 138-162 | 25 | |
| α-helix | 168-179 | 12 | |
| α-helix | 180-184 | 5 | |
| α-helix | 188-204 | 17 | |
| α-helix | 206-208 | 3 | |
| α-helix | 214-231 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein epsilon | A | protein | 234 | HOMO SAPIENS | P62258 (AlphaFold model) |
| Consensus peptide for 14-3-3 proteins | P | protein | 7 | HOMO SAPIENS |
>2BR9_1 14-3-3 PROTEIN EPSILON (chains A) SMDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRAS WRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKV FYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSV FYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS
>2BR9_2 CONSENSUS PEPTIDE FOR 14-3-3 PROTEINS (chains P) RRQRSAP
Structural Basis for Protein-Protein Interactions in the 14-3-3 Protein Family. Yang, X., Lee, W.H., Sobott, F. et al. Proc Natl Acad Sci U S A (2006) 103:17237. DOI 10.1073/PNAS.0605779103 · PubMed
Other PDB entries of the same protein (UniProt P62258 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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