Colicin-E9 (col) is a 582-residue protein from Escherichia coli. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P09883.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 83.4 (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 | 62% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1FR2 | X-ray | 1.6 Å | B=450-582 |
| 2GYK | X-ray | 1.6 Å | B/F=450-582 |
| 2GZJ | X-ray | 1.6 Å | B/F=450-582 |
| 2VLN | X-ray | 1.6 Å | B=450-582 |
| 2VLQ | X-ray | 1.6 Å | B=450-582 |
| 1EMV | X-ray | 1.7 Å | B=450-582 |
| 2GZG | X-ray | 1.7 Å | B=450-582 |
| 2GZI | X-ray | 1.7 Å | B=450-582 |
| 2GZF | X-ray | 1.75 Å | B=450-582 |
| 2WPT | X-ray | 1.78 Å | B=450-582 |
| 1FSJ | X-ray | 1.8 Å | B/C/D/E=450-582 |
| 2GZE | X-ray | 1.8 Å | B=450-582 |
| 2VLO | X-ray | 1.8 Å | B=450-582 |
| 1V13 | X-ray | 2.0 Å | A/B=450-582 |
| 2IVZ | X-ray | 2.0 Å | E/F/G/H=32-47 |
| 2VLP | X-ray | 2.0 Å | B=450-582 |
| 4JML | X-ray | 2.0 Å | E=32-47 |
| 1BXI | X-ray | 2.05 Å | B=449-582 |
| 1V15 | X-ray | 2.4 Å | A/B/C/D=450-582 |
| 1V14 | X-ray | 2.9 Å | A/B/C/D=450-582 |
Showing 20 of 25 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.