The crystal structure of p18, human translation elongation factor 1 epsilon 1. Determined by X-ray diffraction at 2.0 Å resolution. Released 25 Mar 2008.
Explore 2UZ8 in 3D Show helices and sheets RCSB PDB PDBe
2UZ8 contains 24 α-helices and 6 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 | 2-13 | 12 | |
| α-helix | 19-21 | 3 | |
| β-strand | 23-25 | 3 | 1 |
| β-strand | 30-34 | 5 | 1 |
| β-strand | 40-42 | 3 | 1 |
| α-helix | 44-54 | 11 | |
| α-helix | 58-61 | 4 | |
| α-helix | 65-77 | 13 | |
| α-helix | 78-82 | 5 | |
| α-helix | 90-101 | 12 | |
| α-helix | 102-104 | 3 | |
| α-helix | 115-128 | 14 | |
| α-helix | 133-138 | 6 | |
| α-helix | 140-151 | 12 | |
| α-helix | 160-163 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-13 | 11 | |
| α-helix | 19-21 | 3 | |
| β-strand | 22-25 | 4 | 2 |
| β-strand | 30-34 | 5 | 2 |
| β-strand | 40-42 | 3 | 2 |
| α-helix | 44-54 | 11 | |
| α-helix | 58-61 | 4 | |
| α-helix | 65-77 | 13 | |
| α-helix | 78-82 | 5 | |
| α-helix | 91-101 | 11 | |
| α-helix | 102-104 | 3 | |
| α-helix | 115-129 | 15 | |
| α-helix | 133-138 | 6 | |
| α-helix | 140-151 | 12 | |
| α-helix | 160-163 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic translation elongation factor 1 epsilon-1 | A, B | protein | 174 | HOMO SAPIENS | O43324 (AlphaFold model) |
>2UZ8_1 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1 EPSILON-1 (chains A, B) MAAAAELSLLEKSLGLSKGNKYSAQGERQIPVLQTNNGPSLMGLTTIAAHLVKQANKEYL LGSTAEEKAMVQQWLEYRVTQVDGHSSKNDIHTLLMDLNSYLEDKVYLTGYNFTLADILL YYGLHRFIVDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRLYTNSH
Determination of Three-Dimensional Structure and Residues of the Novel Tumor Suppressor Aimp3/P18 Required for the Interaction with Atm. Kim, K.J., Park, M.C., Choi, S.J. et al. J Biol Chem (2008) 283:14032. DOI 10.1074/JBC.M800859200 · PubMed
Other PDB entries of the same protein (UniProt O43324 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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