DNA polymerase lambda (POLL) is a 575-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UGP5.
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The mean pLDDT of this model is 80.4 (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 | 58% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 19% |
What pLDDT means and how to read it
DNA polymerase that functions in several pathways of DNA repair (PubMed:11457865, PubMed:19806195, PubMed:20693240, PubMed:30250067). Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA (PubMed:11457865, PubMed:19806195). Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination (PubMed:19806195, PubMed:20693240, PubMed:30250067). Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities (PubMed:10887191, PubMed:10982892, PubMed:12809503, PubMed:14627824, PubMed:15537631, PubMed:19806195). Also has a 5'-deoxyribose-5-phosphate lyase…
Interacts with PCNA (PubMed:14992725). Interacts with PAXX; promoting POLL recruitment to double-strand breaks (DSBs) and stimulation of the end-filling activity of POLL (PubMed:30250067). Interacts with XRCC4; promoting POLL recruitment to double-strand breaks (DSBs) and stimulation of the end-filling activity of POLL (PubMed:30250067). Interacts with NHEJ1/XLF; promoting POLL recruitment to…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7M07 | X-ray | 1.57 Å | A=234-575 |
| 7M49 | X-ray | 1.6 Å | A=242-575 |
| 9NPU | X-ray | 1.63 Å | A=234-575 |
| 2BCQ | X-ray | 1.65 Å | A=242-575 |
| 7M09 | X-ray | 1.65 Å | A=234-575 |
| 7M47 | X-ray | 1.65 Å | A=242-575 |
| 7M4B | X-ray | 1.66 Å | A=242-575 |
| 7M08 | X-ray | 1.7 Å | A=234-575 |
| 7M4L | X-ray | 1.7 Å | A=242-575 |
| 5IIJ | X-ray | 1.72 Å | A=242-575 |
| 7M4K | X-ray | 1.72 Å | A=242-575 |
| 2BCR | X-ray | 1.75 Å | A=242-575 |
| 5III | X-ray | 1.8 Å | A=242-575 |
| 7M0D | X-ray | 1.8 Å | A/B=234-575 |
| 7M4D | X-ray | 1.82 Å | A=242-575 |
| 7M0A | X-ray | 1.83 Å | A=234-575 |
| 7M4A | X-ray | 1.87 Å | A=242-575 |
| 7M4G | X-ray | 1.88 Å | A=242-575 |
| 7M45 | X-ray | 1.89 Å | A=242-575 |
| 2PFN | X-ray | 1.9 Å | A=242-575 |
Showing 20 of 96 experimental structures (best resolution first).
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