Heat shock cognate 71 kDa protein (HSPA8) is a 650-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19120.
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The mean pLDDT of this model is 88.2 (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 | 66% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 6% |
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. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only…
Component of the chaperone-assisted selective autophagy (CASA) complex consisting of BAG3, HSPA8/HSC70, HSPB8 and STUB1/CHIP (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). Interacts with PACRG (By similarity). Interacts with HSPH1/HSP105 (By similarity). Interacts with IRAK1BP1 and BAG1 (By similarity). Interacts with DNAJC7…
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 |
|---|---|---|---|
| 7ODB | X-ray | 1.66 Å | A=1-554 |
| 1BA1 | X-ray | 1.7 Å | A=1-386 |
| 1BUP | X-ray | 1.7 Å | A=1-386 |
| 1HPM | X-ray | 1.7 Å | A=1-386 |
| 1KAX | X-ray | 1.7 Å | A=1-381 |
| 1KAY | X-ray | 1.7 Å | A=1-381 |
| 1KAZ | X-ray | 1.7 Å | A=1-381 |
| 2BUP | X-ray | 1.7 Å | A=1-381 |
| 2QWO | X-ray | 1.7 Å | A=1-394 |
| 2QWL | X-ray | 1.75 Å | A/B=1-394 |
| 2QWP | X-ray | 1.75 Å | A=1-394 |
| 7ODI | X-ray | 1.83 Å | A=1-554 |
| 2QW9 | X-ray | 1.85 Å | A/B=1-394 |
| 2QWM | X-ray | 1.86 Å | A/B=1-394 |
| 1BA0 | X-ray | 1.9 Å | A=1-386 |
| 1HX1 | X-ray | 1.9 Å | A=4-381 |
| 1QQM | X-ray | 1.9 Å | A=4-381 |
| 1QQN | X-ray | 1.9 Å | A=4-381 |
| 1QQO | X-ray | 1.9 Å | A=4-381 |
| 4FL9 | X-ray | 1.9 Å | A=1-554 |
Showing 20 of 42 experimental structures (best resolution first).
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