Solution structure of the N-terminal domain of ribosomal protein L9. Determined by solution NMR. Released 27 Apr 2002.
Explore 1CQU in 3D Show helices and sheets RCSB PDB PDBe
1CQU contains 3 α-helices and 3 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 | 2-5 | 4 | 1 |
| β-strand | 17-20 | 4 | 1 |
| α-helix | 25 | 1 | |
| α-helix | 26-34 | 9 | |
| β-strand | 36-38 | 3 | 1 |
| α-helix | 41-49 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 50S ribosomal protein L9 | A | protein | 56 | Geobacillus stearothermophilus | P02417 (AlphaFold model) |
>1CQU_1 50S RIBOSOMAL PROTEIN L9 (chains A) MKVIFLKDVKGKGKKGEIKNVADGYANNFLFKQGLAIEATPANLKALEAQKQKEQR
Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9. Luisi, D.L., Kuhlman, B., Sideras, K. et al. J Mol Biol (1999) 289:167-174. DOI 10.1006/jmbi.1999.2742 · PubMed
Other PDB entries of the same protein (UniProt P02417 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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