Ribosome-associated molecular chaperone SSB1 (SSB1) is a 614-residue protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: G0SCU5.
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The mean pLDDT of this model is 93.0 (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 | 77% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high…
Binds to ribosomes. Binds close to the ribosomal tunnel exit via contacts with both ribosomal proteins and rRNA. Directly interacts with nascent polypeptides. This interaction is dependent on the ribosome-associated complex (RAC). Interacts with SSE1. Interacts with FES1
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5TKY | X-ray | 2.6 Å | A/B=4-613 |
| 7OLC | EM | 2.9 Å | C=1-614 |
| 8OO0 | EM | 3.1 Å | C=1-614 |
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