Lethal factor (lef) is a 809-residue protein from Bacillus anthracis. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15917.
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The mean pLDDT of this model is 89.6 (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 | 79% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages (PubMed:10475971, PubMed:11104681, PubMed:3711080, PubMed:8380282, PubMed:9563949, PubMed:9703991). Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes (PubMed:10475971, PubMed:11104681, PubMed:14718925,…
Interacts (via ATLF domain 1) with the cleaved form of protective antigen (PA-63) anthrax toxin; interaction is required for LF translocation into the host cytoplasm (PubMed:10085027, PubMed:15313199, PubMed:21037566, PubMed:32047164, PubMed:32521227, PubMed:32810181, PubMed:8942659). Interacts with PA-63 homooligomers (either homoheptamers or homooctamers): three molecules of LF bind the PA-63…
Secreted, Host cytoplasm, host cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4DV8 | X-ray | 1.63 Å | A=296-809 |
| 4PKW | X-ray | 1.75 Å | A=298-809 |
| 5D1S | X-ray | 2.1 Å | A=298-809 |
| 4PKQ | X-ray | 2.2 Å | A=298-809 |
| 4PKR | X-ray | 2.2 Å | A=298-809 |
| 5D1T | X-ray | 2.2 Å | A=298-809 |
| 1J7N | X-ray | 2.3 Å | A/B=34-809 |
| 1YQY | X-ray | 2.3 Å | A=297-809 |
| 4PKS | X-ray | 2.3 Å | A=298-809 |
| 4XM6 | X-ray | 2.35 Å | A=298-809 |
| 4PKT | X-ray | 2.4 Å | A=298-809 |
| 4PKU | X-ray | 2.4 Å | A=298-809 |
| 4PKV | X-ray | 2.5 Å | A=298-809 |
| 4WF6 | X-ray | 2.65 Å | A=298-809 |
| 1ZXV | X-ray | 2.67 Å | A/B=34-809 |
| 1PWU | X-ray | 2.7 Å | A/B=34-809 |
| 4XM7 | X-ray | 2.7 Å | A=298-809 |
| 4XM8 | X-ray | 2.7 Å | A=298-809 |
| 1PWW | X-ray | 2.8 Å | A/B=34-809 |
| 1PWV | X-ray | 2.85 Å | A/B=34-809 |
Showing 20 of 33 experimental structures (best resolution first).
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