NMR structure of L11-C76, the C-terminal domain of 50S ribosomal protein L11, minimized average structure. Determined by solution NMR. Released 12 Mar 1997.
Explore 1FOW in 3D Show helices and sheets RCSB PDB PDBe
1FOW contains 4 α-helices and 2 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 | 10-18 | 9 | |
| β-strand | 34-36 | 3 | 1 |
| α-helix | 37-46 | 10 | |
| α-helix | 48-51 | 4 | |
| α-helix | 56-66 | 11 | |
| β-strand | 73-75 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| L11-C76 | A | protein | 76 | Geobacillus stearothermophilus | P56210 (AlphaFold model) |
>1FOW_1 L11-C76 (chains A) MTFITKTPPAAVLLKKAAGIESGSGEPNRNKVATIKRDKVREIAELKMPDLNAASIEAAM RMIEGTARSMGIVVED
High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. Markus, M.A., Hinck, A.P., Huang, S. et al. Nat Struct Biol (1997) 4:70-77. DOI 10.1038/nsb0197-70 · PubMed
Other PDB entries of the same protein (UniProt P56210 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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