A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K). Determined by X-ray diffraction at 1.94 Å resolution. Released 17 Jul 2007.
Explore 2UZR in 3D Show helices and sheets RCSB PDB PDBe
2UZR contains 1 α-helix and 7 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 |
|---|---|---|---|
| β-strand | 6-15 | 10 | 1 |
| β-strand | 22-30 | 9 | 1 |
| β-strand | 34-38 | 5 | 1 |
| β-strand | 53-56 | 4 | 1 |
| β-strand | 60-65 | 6 | 1 |
| β-strand | 72-79 | 8 | 1 |
| β-strand | 82-89 | 8 | 1 |
| α-helix | 93-118 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RAC-alpha serine/threonine-protein kinase | A | protein | 124 | Homo sapiens | P31749 (AlphaFold model) |
>2UZR_1 RAC-alpha serine/threonine-protein kinase (chains A) SMSDVAIVKEGWLHKRGKYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQ CQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMD FRSG
A transforming mutation in the pleckstrin homology domain of AKT1 in cancer. Carpten, J.D., Faber, A.L., Horn, C. et al. Nature (2007) 448:439-444. DOI 10.1038/nature05933 · PubMed
Other PDB entries of the same protein (UniProt P31749 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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