Transcription antitermination protein RfaH (rfaH) is a 162-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0AFW0.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 78.6 (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 | 40% |
| 70 to 90 | Confident: backbone generally right | 36% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components. RfaH is recruited into a multi-component RNA polymerase complex by the ops element, which is a short conserved DNA sequence located downstream of the main promoter of these operons. Once bound, RfaH suppresses pausing and inhibits Rho-dependent and intrinsic termination at a subset of sites. Termination signals are bypassed, which allows complete synthesis of long RNA chains. Enhances expression of several operons involved in synthesis of lipopolysaccharides, exopolysaccharides, hemolysin, and sex factor. Also negatively controls expression and surface presentation of…
Interacts with both the nontemplate DNA and the RNA polymerase (RNAP). Monomer in solution
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2OUG | X-ray | 2.1 Å | A/B/C/D=1-162 |
| 5OND | X-ray | 2.1 Å | A/B=1-162 |
| 8PIB | EM | 2.6 Å | P=1-162 |
| 8PID | EM | 3.0 Å | P=1-162 |
| 8PEN | EM | 3.1 Å | P=1-162 |
| 8PFG | EM | 3.1 Å | P=1-162 |
| 8PHK | EM | 3.1 Å | P=1-162 |
| 8URY | EM | 3.1 Å | AB=1-162 |
| 8PIL | EM | 3.2 Å | P=1-162 |
| 8UQL | EM | 3.2 Å | AB=1-162 |
| 8PFJ | EM | 3.4 Å | P=1-162 |
| 8PIM | EM | 3.4 Å | P=1-162 |
| 8UR0 | EM | 3.4 Å | AB=1-162 |
| 6C6T | EM | 3.5 Å | D=1-162 |
| 6C6S | EM | 3.7 Å | D=1-162 |
| 8UQP | EM | 3.8 Å | AB=1-162 |
| 8UPR | EM | 5.3 Å | AB=1-162 |
| 8UQM | EM | 5.3 Å | AB=1-162 |
| 8URI | EM | 5.3 Å | AB=1-162 |
| 8UPO | EM | 5.5 Å | AB=1-162 |
Showing 20 of 23 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.