Small ribosomal subunit protein eS4 (RPS4X) is a 263-residue protein from Oryctolagus cuniculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: G1TK17.
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The mean pLDDT of this model is 94.9 (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 | 97% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 1% |
| 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). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). 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 to generate RNA folding, modifications,…
Component of the small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:29856316, PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:32286223, PubMed:33296660, PubMed:35822879, PubMed:36653451). Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:23873042,…
Cytoplasm, Nucleus, nucleolus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7OYD | EM | 2.3 Å | EE=1-263 |
| 8SCB | EM | 2.5 Å | EE=1-263 |
| 9MR4 | EM | 2.65 Å | x=1-263 |
| 9RHU | EM | 2.65 Å | P1=1-263 |
| 7JQB | EM | 2.7 Å | M=1-263 |
| 8VVQ | EM | 2.7 Å | EB=1-263 |
| 6SGC | EM | 2.8 Å | F1=1-263 |
| 9QQA | EM | 2.8 Å | Ad=1-263 |
| 9NDP | EM | 2.82 Å | x=1-263 |
| 9Q7Q | EM | 2.86 Å | x=1-263 |
| 8P2K | EM | 2.9 Å | Ad=1-263 |
| 8VVP | EM | 2.9 Å | EB=1-263 |
| 8VVT | EM | 2.9 Å | EB=1-263 |
| 9H6Y | EM | 2.9 Å | G=1-263 |
| 9H74 | EM | 2.9 Å | G=1-263 |
| 9YPW | EM | 2.9 Å | EE=1-263 |
| 9YPZ | EM | 2.9 Å | EE=1-263 |
| 9YQ0 | EM | 2.9 Å | EE=1-263 |
| 9YQ1 | EM | 2.9 Å | EE=1-263 |
| 6R5Q | EM | 3.0 Å | x=2-263 |
Showing 20 of 70 experimental structures (best resolution first).
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