Small ribosomal subunit protein eS28 (RPS28) is a 69-residue protein from Oryctolagus cuniculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: G1TIB4.
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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 | 75% |
| 70 to 90 | Confident: backbone generally right | 16% |
| 50 to 70 | Low: treat with caution | 9% |
| 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. 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 to generate RNA folding, modifications, rearrangements and cleavage as well as…
Component of the 40S 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:35822879, PubMed:36653451). Part of the small subunit (SSU) processome, composed of more than 70 proteins…
Cytoplasm, cytosol, Cytoplasm, Rough endoplasmic reticulum, 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 | AB=1-69 |
| 7OYD | EM | 2.3 Å | Cc=1-69 |
| 7O7Z | EM | 2.4 Å | AB=1-69 |
| 8SCB | EM | 2.5 Å | cc=1-69 |
| 9MR4 | EM | 2.65 Å | FF=1-69 |
| 9RHU | EM | 2.65 Å | C1=1-69 |
| 7JQB | EM | 2.7 Å | d=1-69 |
| 8VVQ | EM | 2.7 Å | CC=1-69 |
| 6SGC | EM | 2.8 Å | d1=1-69 |
| 7UCK | EM | 2.8 Å | Cc=7-68 |
| 9BDL | EM | 2.8 Å | AS28=7-68 |
| 9QQA | EM | 2.8 Å | AB=1-69 |
| 9NDP | EM | 2.82 Å | FF=1-69 |
| 9Q7Q | EM | 2.86 Å | FF=1-69 |
| 7O80 | EM | 2.9 Å | AB=1-69 |
| 7TOR | EM | 2.9 Å | AS28=7-68 |
| 8P2K | EM | 2.9 Å | AB=1-69 |
| 8VVP | EM | 2.9 Å | CC=1-69 |
| 8VVT | EM | 2.9 Å | CC=1-69 |
| 9H6Y | EM | 2.9 Å | d=1-69 |
Showing 20 of 120 experimental structures (best resolution first).
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