Beta sliding clamp (dnaN) is a 366-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0A988.
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The mean pLDDT of this model is 95.4 (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 | 8% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA (PubMed:2040637). DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA (PubMed:18191219). In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent (PubMed:26499492). Coordinates protein traffic at the replication fork, where it interacts with multiple DNA polymerases, repair factors and other…
Forms a ring-shaped head-to-tail homodimer (PubMed:2040637, PubMed:9927437, PubMed:1349852, PubMed:12832762, PubMed:14592985, PubMed:14729336, PubMed:18191219, PubMed:18678908) around DNA (PubMed:18191219), which can be opened by the delta subunit (PubMed:11525728, PubMed:9927437). Binds interacting factors in a hydrophobic surface cleft between domains 2 and 3, each monomer is able to bind…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8PAY | X-ray | 1.21 Å | A=1-366 |
| 8PAT | X-ray | 1.45 Å | A=1-366 |
| 4K3L | X-ray | 1.5 Å | A/B=1-366 |
| 8CIY | X-ray | 1.54 Å | A=1-366 |
| 7AZ8 | X-ray | 1.61 Å | A/B=1-366 |
| 4MJR | X-ray | 1.62 Å | A/B=1-366 |
| 6FVM | X-ray | 1.63 Å | A/B=1-366 |
| 3D1G | X-ray | 1.64 Å | A/B=1-366 |
| 1OK7 | X-ray | 1.65 Å | A/B=1-366 |
| 7AZ7 | X-ray | 1.65 Å | A=1-366 |
| 4N96 | X-ray | 1.7 Å | A/B=1-366 |
| 4N98 | X-ray | 1.7 Å | A/B=1-366 |
| 4MJQ | X-ray | 1.73 Å | A/B=1-366 |
| 4N94 | X-ray | 1.73 Å | A/B=1-366 |
| 4K3S | X-ray | 1.75 Å | A/B=1-366 |
| 8CIX | X-ray | 1.76 Å | A=1-366 |
| 3F1V | X-ray | 1.77 Å | A/B=1-366 |
| 7AZC | X-ray | 1.77 Å | A/B/C/D=1-366 |
| 4N95 | X-ray | 1.8 Å | A/B=1-366 |
| 7AZE | X-ray | 1.82 Å | A/B=1-366 |
Showing 20 of 72 experimental structures (best resolution first).
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