Crystal Structure of 14-3-3 epsilon with Mlf1 peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 25 Jan 2012.
Explore 3UAL in 3D Show helices and sheets RCSB PDB PDBe
3UAL 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 | 39-71 | 33 | |
| 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 | 232 | Homo sapiens | P62258 (AlphaFold model) |
| Myeloid leukemia factor 1 | P | protein | 14 | Homo sapiens | P58340 (AlphaFold model) |
>3UAL_1 14-3-3 protein epsilon (chains A) MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASW RIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVF YYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVF YYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWT
>3UAL_2 Myeloid leukemia factor 1 (chains P) MIRSFSEPFGRDLL
| ID | Name | Formula | Copies |
|---|---|---|---|
| TBU | Tertiary-butyl alcohol | C4 H10 O | 3 |
Structural insights of the MLF1/14-3-3 interaction. Molzan, M., Weyand, M., Rose, R. et al. FEBS J (2012) 279:563-571. DOI 10.1111/j.1742-4658.2011.08445.x · 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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