ATP-dependent molecular chaperone HSP82 (HSP82) is a 709-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02829.
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The mean pLDDT of this model is 84.9 (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 | 31% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as…
Homodimer. Interacts with the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1. Interacts directly with the substrates GCN2, HAP1 and STE11
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2IWX | X-ray | 1.5 Å | A=1-214 |
| 2BRC | X-ray | 1.6 Å | A=1-214 |
| 2WER | X-ray | 1.6 Å | A/B=1-220 |
| 3C11 | X-ray | 1.6 Å | A=1-220 |
| 1ZWH | X-ray | 1.65 Å | A=1-220 |
| 1AH6 | X-ray | 1.8 Å | A=1-220 |
| 1AMW | X-ray | 1.85 Å | A=1-214 |
| 2XX2 | X-ray | 1.85 Å | A/B/C/D=1-214 |
| 1ZW9 | X-ray | 1.9 Å | A=1-220 |
| 2VW5 | X-ray | 1.9 Å | A/B/C/D=1-214 |
| 3C0E | X-ray | 1.9 Å | A=1-220 |
| 2AKP | X-ray | 1.94 Å | A/B=25-210 |
| 2YGE | X-ray | 1.96 Å | A=1-220 |
| 3FP2 | X-ray | 1.98 Å | Q=698-709 |
| 1AM1 | X-ray | 2.0 Å | A=2-214 |
| 2BRE | X-ray | 2.0 Å | A/B=1-219 |
| 2FXS | X-ray | 2.0 Å | A=1-220 |
| 2WEP | X-ray | 2.0 Å | A=1-220 |
| 2XX5 | X-ray | 2.0 Å | A=1-214 |
| 2YGF | X-ray | 2.0 Å | A=1-220 |
Showing 20 of 49 experimental structures (best resolution first).
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