NMR structure of L11-C76, the C-terminal domain of 50S ribosomal protein L11, 33 structures. Determined by solution NMR. Released 12 Mar 1997.
Explore 1FOX in 3D Show helices and sheets RCSB PDB PDBe
1FOX contains 3 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 | 56-69 | 14 | |
| β-strand | 73-75 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| L11-C76 | A | protein | 76 | Geobacillus stearothermophilus | P56210 (AlphaFold model) |
>1FOX_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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