14-3-3 Protein Eta (Human) Complexed to Peptide. Determined by X-ray diffraction at 2.7 Å resolution. Released 2 Dec 2005.
Explore 2C74 in 3D Show helices and sheets RCSB PDB PDBe
2C74 contains 28 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 | 3-16 | 14 | |
| α-helix | 20-31 | 12 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-72 | 34 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-135 | 19 | |
| α-helix | 140-164 | 25 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 213-215 | 3 | |
| α-helix | 216-234 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein eta | A, B | protein | 247 | HOMO SAPIENS | Q04917 (AlphaFold model) |
| Consensus peptide mode 1 for 14-3-3 proteins | P, Q | protein | 7 | synthetic construct |
>2C74_1 14-3-3 PROTEIN ETA (chains A, B) SMGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSS WRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYES KVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALNF SVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQD EEAGEGN
>2C74_2 CONSENSUS PEPTIDE MODE 1 FOR 14-3-3 PROTEINS (chains P, Q) RRQRSAP
| ID | Name | Formula | Copies |
|---|---|---|---|
| CIT | Citric acid | C6 H8 O7 | 1 |
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) 103:17237-17242. DOI 10.1073/pnas.0605779103 · PubMed
Other PDB entries of the same protein (UniProt Q04917 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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