Trp operon repressor (trpR) is a 108-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0A881.
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The mean pLDDT of this model is 92.6 (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 | 90% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region
Homodimer
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6ENI | X-ray | 1.1 Å | A/B=1-108 |
| 6ENN | X-ray | 1.17 Å | A/B=1-108 |
| 6FAL | X-ray | 1.2 Å | A/B=2-108 |
| 1JHG | X-ray | 1.3 Å | A=8-108 |
| 6ELG | X-ray | 1.38 Å | A/B=1-108 |
| 6F9K | X-ray | 1.4 Å | A=1-107 |
| 6ELB | X-ray | 1.44 Å | A/B=1-108 |
| 6EKP | X-ray | 1.46 Å | A/B=1-108 |
| 3SSX | X-ray | 1.58 Å | N/R=2-108 |
| 2OZ9 | X-ray | 1.65 Å | R=2-108 |
| 6F7G | X-ray | 1.66 Å | A/C=4-106 |
| 3SSW | X-ray | 1.67 Å | N/R=2-108 |
| 3WRP | X-ray | 1.8 Å | A=1-108 |
| 6ELF | X-ray | 1.83 Å | A/B=1-108 |
| 1TRO | X-ray | 1.9 Å | A/C/E/G=1-108 |
| 6EJZ | X-ray | 1.9 Å | A/B/C/D=1-108 |
| 6EJW | X-ray | 1.99 Å | A/B/C/D=1-108 |
| 1ZT9 | X-ray | 2.0 Å | A/B/D/E=2-108 |
| 6ST6 | X-ray | 2.05 Å | A=1-105 |
| 6F7F | X-ray | 2.13 Å | A/B/C/D=4-106 |
Showing 20 of 29 experimental structures (best resolution first).
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