Solution structure of ASPP2 N-terminus. Determined by solution NMR. Released 10 Jul 2007.
Explore 2UWQ in 3D Show helices and sheets RCSB PDB PDBe
2UWQ contains 3 α-helices 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 | 4-9 | 6 | 1 |
| β-strand | 17-22 | 6 | 1 |
| β-strand | 27 | 1 | 2 |
| α-helix | 29-34 | 6 | |
| β-strand | 44-49 | 6 | 1 |
| β-strand | 52-56 | 5 | 1 |
| β-strand | 61 | 1 | 2 |
| α-helix | 62-69 | 8 | |
| α-helix | 73-75 | 3 | |
| β-strand | 77-81 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis-stimulating of P53 protein 2 | A | protein | 86 | HOMO SAPIENS | Q13625 (AlphaFold model) |
>2UWQ_1 APOPTOSIS-STIMULATING OF P53 PROTEIN 2 (chains A) GGSMMPMFLTVYLSNNEQHFTEVPVTPETICRDVVDLCKEPGESDCHLAEVWCGSERPVA DNERMFDVLQRFGSQRNEVRFFLRHE
Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold. Tidow, H., Andreeva, A., Rutherford, T.J. et al. J Mol Biol (2007) 371:948-958. DOI 10.1016/j.jmb.2007.05.024 · PubMed
Other PDB entries of the same protein (UniProt Q13625 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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