UV excision repair protein RAD23 (RAD23) is a 398-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P32628.
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The mean pLDDT of this model is 67.8 (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 | 13% |
| 70 to 90 | Confident: backbone generally right | 42% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 34% |
What pLDDT means and how to read it
Plays a central role both in proteasomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes
Interacts directly with PNG1
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2QSF | X-ray | 2.35 Å | X=230-398 |
| 3M62 | X-ray | 2.4 Å | B=1-84 |
| 1X3Z | X-ray | 2.8 Å | B=238-309 |
| 2QSH | X-ray | 2.81 Å | X=230-398 |
| 6UG1 | X-ray | 2.83 Å | X=256-311 |
| 1X3W | X-ray | 3.0 Å | B=238-309 |
| 4YIR | X-ray | 3.05 Å | X=230-398 |
| 2QSG | X-ray | 3.1 Å | X=230-398 |
| 6UIN | X-ray | 3.35 Å | X=230-398 |
| 6CFI | X-ray | 3.36 Å | X=230-398 |
| 3ESW | X-ray | 3.4 Å | B=254-308 |
| 6UBF | X-ray | 4.6 Å | X=230-398 |
| 2NBU | NMR | A=1-78 | |
| 2NBW | NMR | B=1-78 |
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