Heat shock cognate 71 kDa protein (HSPA8) is a 646-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P11142.
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The mean pLDDT of this model is 88.3 (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 | 64% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661, PubMed:2799391, PubMed:36586411). This is achieved through cycles of…
Component of the chaperone-assisted selective autophagy (CASA) complex consisting of BAG3, HSPA8/HSC70, HSPB8 and STUB1/CHIP (PubMed:20060297). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7. Interacts with DNAJB12 (via J domain) (PubMed:21148293,…
Cytoplasm, Melanosome, Nucleus, nucleolus, Cell membrane, Lysosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5AQM | X-ray | 1.63 Å | A/C=1-381 |
| 4H5R | X-ray | 1.64 Å | A/B=2-384 |
| 5AQL | X-ray | 1.69 Å | A/C=1-381 |
| 4H5V | X-ray | 1.75 Å | A=2-384 |
| 5AQV | X-ray | 1.75 Å | A=1-381 |
| 6B1N | X-ray | 1.8 Å | A/B=5-381 |
| 3AGY | X-ray | 1.85 Å | C/D/F=639-646 |
| 6ZYJ | X-ray | 1.85 Å | A/B=5-384 |
| 4H5N | X-ray | 1.86 Å | A/B=2-384 |
| 5AQF | X-ray | 1.88 Å | A/C=1-381 |
| 3LDQ | X-ray | 1.9 Å | A=4-381 |
| 4H5T | X-ray | 1.9 Å | A=2-384 |
| 5AQT | X-ray | 1.9 Å | A=1-381 |
| 6B1M | X-ray | 1.9 Å | A/B=5-381 |
| 5AQR | X-ray | 1.91 Å | A/C/E=1-381 |
| 5AQU | X-ray | 1.92 Å | A=1-381 |
| 4H5W | X-ray | 1.94 Å | A/B=2-384 |
| 5AQJ | X-ray | 1.96 Å | A/C/E=1-381 |
| 5AQI | X-ray | 1.98 Å | A/C=1-381 |
| 3FZH | X-ray | 2.0 Å | A=4-381 |
Showing 20 of 38 experimental structures (best resolution first).
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