26S proteasome regulatory subunit RPN13 (RPN13) is a 156-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O13563.
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The mean pLDDT of this model is 67.5 (low 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 | 0% |
| 70 to 90 | Confident: backbone generally right | 55% |
| 50 to 70 | Low: treat with caution | 30% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
Component of the 19S cap proteasome complex which acts as a regulatory subunit of the 26S proteasome, involved in the ATP-dependent degradation of ubiquitinated proteins
Component of the 19S cap proteasome complex composed of at least RPN1, RPN2, RPN3, RPN4, RPN5, RPN6, RPN7, RPN8, RPN9, RPN10, RPN11, RPN12, RPN13, RPT1, RPT2, RPT3, RPT4, RPT5, and RPT6. The 19S subcomplex associates with the 20S proteasome subcomplex to form the functional 26S proteasome
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6J2Q | EM | 3.8 Å | X=1-156 |
| 6J2X | EM | 3.8 Å | X=1-156 |
| 5MPD | EM | 4.1 Å | X=1-156 |
| 6FVT | EM | 4.1 Å | X=7-133 |
| 5WVK | EM | 4.2 Å | X=1-156 |
| 5MPE | EM | 4.5 Å | X=1-156 |
| 6FVU | EM | 4.5 Å | X=7-133 |
| 6FVW | EM | 4.5 Å | X=7-133 |
| 6J30 | EM | 4.5 Å | X=1-156 |
| 3JCP | EM | 4.6 Å | X=1-156 |
| 3JCO | EM | 4.8 Å | X=1-156 |
| 6FVX | EM | 4.9 Å | X=7-133 |
| 6FVV | EM | 5.4 Å | X=7-133 |
| 7QO5 | EM | 6.0 Å | X=1-156 |
| 6FVY | EM | 6.1 Å | X=7-133 |
| 7QO3 | EM | 6.1 Å | X=1-156 |
| 5WVI | EM | 6.3 Å | X=1-156 |
| 6J2C | EM | 7.0 Å | X=1-156 |
| 6J2N | EM | 7.5 Å | X=1-156 |
| 4CR2 | EM | 7.7 Å | X=1-156 |
Showing 20 of 27 experimental structures (best resolution first).
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