DNA polymerase beta (Polb) is a 335-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P06766.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 95.3 (very high 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 | 94% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as…
Monomer (By similarity). Binds single-stranded DNA (ssDNA) (By similarity). Interacts with APEX1, LIG1, LIG3, FEN1, PCNA and XRCC1 (By similarity). Interacts with HUWE1/ARF-BP1, STUB1/CHIP and USP47 (By similarity). Interacts with FAM168A (By similarity)
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2VAN | X-ray | 2.1 Å | A=91-335 |
| 3UXO | X-ray | 2.1 Å | A/B=1-335 |
| 3V7J | X-ray | 2.25 Å | A=4-335 |
| 3V7K | X-ray | 2.27 Å | A=4-335 |
| 1BPB | X-ray | 2.3 Å | A=88-335 |
| 1RPL | X-ray | 2.3 Å | A=85-335 |
| 1ZQW | X-ray | 2.3 Å | A=88-335 |
| 1ZQY | X-ray | 2.3 Å | A=88-335 |
| 1JN3 | X-ray | 2.35 Å | A=85-335 |
| 3LQC | X-ray | 2.35 Å | B=142-335 |
| 3V72 | X-ray | 2.49 Å | A=1-335 |
| 1ZQX | X-ray | 2.5 Å | A=88-335 |
| 3UXN | X-ray | 2.5 Å | A/B=1-335 |
| 1HUO | X-ray | 2.6 Å | A/B=1-335 |
| 1HUZ | X-ray | 2.6 Å | A/B=1-335 |
| 1ZQU | X-ray | 2.6 Å | A=88-335 |
| 3V7L | X-ray | 2.66 Å | A=4-335 |
| 1ZQV | X-ray | 2.7 Å | A=88-335 |
| 1ZQZ | X-ray | 2.7 Å | A=88-335 |
| 3UXP | X-ray | 2.72 Å | A/B=1-335 |
Showing 20 of 31 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.