Proliferating cell nuclear antigen (POL30) is a 258-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15873.
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The mean pLDDT of this model is 95.1 (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 | 92% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Confers DNA tethering and processivity to DNA polymerases and other proteins (PubMed:9343398, PubMed:11545742, PubMed:12226657, PubMed:23747975). Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of DNA replication by increasing the polymerases' processivity during elongation of the leading strand (PubMed:9343398, PubMed:11545742). Additionally, acts as a molecular switch to control the choice of two parallel branches of the DNA damage tolerance (DDT) pathway (also known as the post-replication repair (PRR) pathway) that bypasses replication-blocking lesions without removing them; the translesion DNA synthesis (TLS) branch, and the template-switching (TS)…
Homotrimer (PubMed:15201901). Interacts with RAD30/POLH/DNA polymerase eta (via PIP-box motif); the interaction is direct and is essential for the polymerase eta function (PubMed:11545742, PubMed:23747975). Interacts with REV1 (via BRCT domain); the interaction is direct (PubMed:23747975). Interacts with MCM10 (PubMed:16782870). Interacts with UBP10 (PubMed:22829782)
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5V7M | X-ray | 1.93 Å | A=1-258 |
| 8DQX | EM | 2.1 Å | F/G/H=1-258 |
| 8DR1 | EM | 2.14 Å | F/G/H=1-258 |
| 8DR3 | EM | 2.2 Å | F/G/H=1-258 |
| 1PLQ | X-ray | 2.3 Å | A=1-258 |
| 8DR6 | EM | 2.39 Å | F/G/H=1-258 |
| 8DR0 | EM | 2.42 Å | F/G/H=1-258 |
| 8DR4 | EM | 2.45 Å | F/G/H=1-258 |
| 3GPN | X-ray | 2.5 Å | A=1-258 |
| 3V60 | X-ray | 2.6 Å | B=1-258 |
| 8THW | X-ray | 2.6 Å | A/B/C=1-258 |
| 6W9W | X-ray | 2.65 Å | A=1-254 |
| 4L6P | X-ray | 2.68 Å | A/B/C=1-258 |
| 8DR7 | EM | 2.7 Å | F/G/H=1-258 |
| 8DR5 | EM | 2.76 Å | F/G/H=1-258 |
| 2OD8 | X-ray | 2.8 Å | A=1-258 |
| 3L0W | X-ray | 2.8 Å | A=1-163 |
| 3L10 | X-ray | 2.8 Å | A=1-163 |
| 3PGE | X-ray | 2.8 Å | A=165-258, B=1-163 |
| 3V61 | X-ray | 2.8 Å | B=1-258 |
Showing 20 of 61 experimental structures (best resolution first).
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