26S proteasome regulatory subunit 8 homolog (RPT6) is a 405-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q01939.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 81.6 (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 | 22% |
| 70 to 90 | Confident: backbone generally right | 64% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity)
May form a homodimer or a heterodimer with a related family member. Interacts with OLA1, TMA17, and UBR1
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9CGC | EM | 3.61 Å | J=1-405 |
| 6J2Q | EM | 3.8 Å | J=1-405 |
| 6J2X | EM | 3.8 Å | J=1-405 |
| 5MP9 | EM | 4.1 Å | J=1-405 |
| 6FVT | EM | 4.1 Å | J=1-405 |
| 6EF3 | EM | 4.17 Å | J=1-405 |
| 5WVK | EM | 4.2 Å | J=1-405 |
| 6EF2 | EM | 4.27 Å | J=144-405 |
| 6EF0 | EM | 4.43 Å | J=130-405 |
| 5MPA | EM | 4.5 Å | J=1-405 |
| 6FVU | EM | 4.5 Å | J=1-405 |
| 6FVW | EM | 4.5 Å | J=3-405 |
| 6J30 | EM | 4.5 Å | J=1-405 |
| 3JCP | EM | 4.6 Å | J=1-405 |
| 6EF1 | EM | 4.73 Å | J=133-405 |
| 3JCO | EM | 4.8 Å | J=1-405 |
| 6FVX | EM | 4.9 Å | J=1-405 |
| 6FVV | EM | 5.4 Å | J=1-405 |
| 7QO5 | EM | 6.0 Å | J=1-405 |
| 6FVY | EM | 6.1 Å | J=1-405 |
Showing 20 of 31 experimental structures (best resolution first).
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