Small ribosomal subunit protein uS3 (RPS3) is a 243-residue protein from Oryctolagus cuniculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: G1TNM3.
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 | 79% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 2% |
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). Has endonuclease activity and plays a role in repair of damaged DNA (By similarity). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (By similarity). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (By similarity). Has also been…
Component of the 40S small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:29856316, PubMed:30293783, PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:32286223, PubMed:33296660, PubMed:35679869, PubMed:35709277, PubMed:35822879, PubMed:36653451). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By…
Cytoplasm, Nucleus, Nucleus, nucleolus, Mitochondrion inner membrane, Cytoplasm, cytoskeleton, spindle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7O7Y | EM | 2.2 Å | Ac=1-243 |
| 7OYD | EM | 2.3 Å | DD=1-243 |
| 7O7Z | EM | 2.4 Å | Ac=1-243 |
| 8SCB | EM | 2.5 Å | DD=1-243 |
| 9MR4 | EM | 2.65 Å | w=1-243 |
| 9RHU | EM | 2.65 Å | O1=1-243 |
| 7JQB | EM | 2.7 Å | E=1-243 |
| 8VVQ | EM | 2.7 Å | DB=1-243 |
| 6SGC | EM | 2.8 Å | E1=1-243 |
| 7UCK | EM | 2.8 Å | DD=1-228 |
| 7ZJW | EM | 2.8 Å | SO=1-243 |
| 9BDL | EM | 2.8 Å | AS03=1-228 |
| 9QQA | EM | 2.8 Å | Ac=1-243 |
| 9NDP | EM | 2.82 Å | w=1-243 |
| 9Q7Q | EM | 2.86 Å | w=1-243 |
| 7O80 | EM | 2.9 Å | Ac=1-243 |
| 7TOR | EM | 2.9 Å | AS03=1-228 |
| 8P2K | EM | 2.9 Å | Ac=1-243 |
| 8VVP | EM | 2.9 Å | DB=1-243 |
| 8VVT | EM | 2.9 Å | DB=1-243 |
Showing 20 of 116 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.