Small ribosomal subunit protein eS7 (RPS7) is a 194-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62081.
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The mean pLDDT of this model is 86.9 (confident 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 | 56% |
| 70 to 90 | Confident: backbone generally right | 38% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Required for rRNA maturation (PubMed:19061985). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. 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 targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)
Component of the small ribosomal subunit (PubMed:23636399). Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). Binds IPO9 with high affinity (PubMed:11823430). Interacts with NEK6 (PubMed:20873783). Interacts with DESI2 (PubMed:28483520). Interacts with IPO5, IPO7 and KPNB1; these interactions may…
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, Nucleus, nucleolus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8GLP | EM | 1.67 Å | SH=1-194 |
| 8QOI | EM | 1.9 Å | SH=1-194 |
| 9O3W | EM | 1.9 Å | SH=1-194 |
| 8YOO | EM | 2.0 Å | SH=1-194 |
| 9C3H | EM | 2.0 Å | SH=1-194 |
| 7R4X | EM | 2.15 Å | H=1-194 |
| 9I2D | EM | 2.19 Å | SH=1-194 |
| 9PBE | EM | 2.19 Å | SH=5-193 |
| 8YOP | EM | 2.2 Å | SH=1-194 |
| 9O3Y | EM | 2.2 Å | SH=1-194 |
| 8JDK | EM | 2.26 Å | 4=1-194 |
| 8G5Y | EM | 2.29 Å | SH=1-194 |
| 9S3D | EM | 2.32 Å | SH=1-194 |
| 9RPV | EM | 2.35 Å | RH/SH=1-194 |
| 9S3B | EM | 2.38 Å | SH=1-194 |
| 8K2C | EM | 2.4 Å | SH=1-194 |
| 8XSX | EM | 2.4 Å | SH=1-194 |
| 9SPF | EM | 2.4 Å | SH=1-194 |
| 9SPI | EM | 2.4 Å | SH=1-194 |
| 8JDL | EM | 2.42 Å | 4=1-194 |
Showing 20 of 189 experimental structures (best resolution first).
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