DNA polymerase IV (dinB) is a 351-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q47155.
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The mean pLDDT of this model is 96.0 (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 | 95% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis (PubMed:10488344, PubMed:10801133). Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity (PubMed:10488344). Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long-term survival and evolutionary fitness. Not seen to be involved in translesion snythesis even…
Monomer. Interacts with beta sliding clamp, which confers increased processivity (PubMed:14592985, PubMed:14729336, PubMed:16168375)
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1OK7 | X-ray | 1.65 Å | C=336-351 |
| 5YUY | X-ray | 1.74 Å | A/F=2-351 |
| 5YUZ | X-ray | 1.83 Å | A/F=2-351 |
| 5YUU | X-ray | 1.89 Å | A/F=2-351 |
| 1UNN | X-ray | 1.9 Å | C/D=243-351 |
| 5YV2 | X-ray | 1.9 Å | A/F=2-351 |
| 5YUS | X-ray | 1.94 Å | A/F=2-351 |
| 6IG1 | X-ray | 1.97 Å | A/F=2-351 |
| 5YV3 | X-ray | 2.03 Å | A/F=2-351 |
| 5YUR | X-ray | 2.04 Å | A/F=2-351 |
| 5YUX | X-ray | 2.04 Å | A/F=2-351 |
| 5YYD | X-ray | 2.05 Å | A/F=2-351 |
| 5YUV | X-ray | 2.06 Å | A/F=2-351 |
| 5YV0 | X-ray | 2.09 Å | A/F=2-351 |
| 5YV1 | X-ray | 2.09 Å | A/F=2-351 |
| 5C5J | X-ray | 2.1 Å | A/F=2-351 |
| 5YUW | X-ray | 2.12 Å | A/F=2-351 |
| 5YUT | X-ray | 2.15 Å | A/F=2-351 |
| 4Q45 | X-ray | 2.18 Å | A/F=2-341 |
| 4R8U | X-ray | 2.3 Å | A=2-340, B=2-338 |
Showing 20 of 31 experimental structures (best resolution first).
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