NMR structure of dimerization domain of human ribosomal protein P2. Determined by solution NMR. Released 17 Nov 2009.
Explore 2W1O in 3D Show helices and sheets RCSB PDB PDBe
2W1O contains 10 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 | 2-12 | 11 | |
| α-helix | 20-30 | 11 | |
| α-helix | 37-48 | 12 | |
| α-helix | 51-58 | 8 | |
| α-helix | 60-62 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 60S acidic ribosomal protein P2 | A, B | protein | 70 | HOMO SAPIENS | P05387 (AlphaFold model) |
>2W1O_1 60S ACIDIC RIBOSOMAL PROTEIN P2 (chains A, B) AMRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGI GKLASVPAGG
Solution Structure of the Dimerization Domain of Ribosomal Protein P2 Provides Insights for the Structural Organization of Eukaryotic Stalk. Lee, K.M., Yu, C.W., Chan, D.S. et al. Nucleic Acids Res (2010) 38:5206. DOI 10.1093/NAR/GKQ231 · PubMed
Other PDB entries of the same protein (UniProt P05387 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2W1O directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.