Small ribosomal subunit protein eS17 (RPS17) is a 135-residue protein from Oryctolagus cuniculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: G1TU13.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 90.4 (very high overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 58% |
| 70 to 90 | Confident: backbone generally right | 40% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Component of the small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert…
Component of the small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:29856316, PubMed:30293783, PubMed:30355441, PubMed:30517857, PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:32286223, PubMed:33296660, PubMed:35679869, PubMed:35709277, PubMed:35822879, PubMed:36653451). Part of the small subunit (SSU) processome, composed of more than…
Cytoplasm, Nucleus, nucleolus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7O7Y | EM | 2.2 Å | Aq=1-135 |
| 7OYD | EM | 2.3 Å | RR=1-135 |
| 7O7Z | EM | 2.4 Å | Aq=1-135 |
| 8SCB | EM | 2.5 Å | RR=1-135 |
| 9MR4 | EM | 2.65 Å | KK=1-135 |
| 9RHU | EM | 2.65 Å | c1=1-135 |
| 7JQB | EM | 2.7 Å | S=1-135 |
| 8VVQ | EM | 2.7 Å | RB=1-135 |
| 6SGC | EM | 2.8 Å | S1=1-135 |
| 7UCK | EM | 2.8 Å | RR=2-133 |
| 7ZJW | EM | 2.8 Å | Sc=1-135 |
| 9BDL | EM | 2.8 Å | AS17=2-133 |
| 9QQA | EM | 2.8 Å | Aq=1-135 |
| 9NDP | EM | 2.82 Å | KK=1-135 |
| 9Q7Q | EM | 2.86 Å | KK=2-135 |
| 7O80 | EM | 2.9 Å | Aq=1-135 |
| 7TOR | EM | 2.9 Å | AS17=2-133 |
| 8P2K | EM | 2.9 Å | Aq=1-135 |
| 8VVP | EM | 2.9 Å | RB=1-135 |
| 8VVT | EM | 2.9 Å | RB=1-135 |
Showing 20 of 120 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.