Heat shock protein STI1 (STI1) is a 589-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15705.
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The mean pLDDT of this model is 86.1 (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 | 67% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Co-chaperone that regulates HSP70 and HSP90 chaperones (PubMed:12716905, PubMed:2674681). Functions to scaffold chaperone complexes under basal conditions and controls the ATPase activity of HSP90, but also facilitates the transfer of client proteins from HSP70 to HSP90, thus connecting these two major branches of protein quality control (PubMed:12716905, PubMed:22354036, PubMed:29930177). During high stress, forms cytoplasmic foci and operates independently to sequester soluble misfolded protein in the cytoplasm, a function typically associated with chaperones rather than co-chaperones (PubMed:39739753). Plays a role in mitochondrial function, probably as a cytosolic factors involved in…
Forms a complex with heat shock proteins HSP70 and HSP90
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3UPV | X-ray | 1.6 Å | A=395-518 |
| 3UQ3 | X-ray | 2.6 Å | A=262-515 |
| 2LLV | NMR | A=127-197 | |
| 2LLW | NMR | A=519-589 |
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