DNA-directed RNA polymerase I subunit RPA190 (RPA190) is a 1664-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10964.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 80.8 (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 | 33% |
| 70 to 90 | Confident: backbone generally right | 53% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. RPA190 and RPA135 both contribute to the polymerase catalytic activity and together form the Pol I active center. In addition, subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA190 and crosses the cleft near the catalytic site…
Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the…
Nucleus, nucleolus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6RUI | EM | 2.7 Å | A=1-1664 |
| 9G1V | EM | 2.7 Å | A=1-1664 |
| 4C2M | X-ray | 2.8 Å | A/P=1-1664 |
| 9G27 | EM | 2.8 Å | A=1-1664 |
| 6RQL | EM | 2.9 Å | A=1-1664 |
| 4C3I | X-ray | 3.0 Å | A=1-1664 |
| 6RWE | EM | 3.0 Å | A=1-1664 |
| 6RRD | EM | 3.1 Å | A=1-1664 |
| 6HLQ | EM | 3.18 Å | A=1-1664 |
| 6HLR | EM | 3.18 Å | A=1-1664 |
| 9G2B | EM | 3.2 Å | A=1-1664 |
| 6HLS | EM | 3.21 Å | A=1-1664 |
| 4C3H | X-ray | 3.27 Å | A=1-1664 |
| 9G29 | EM | 3.3 Å | A=1-1664 |
| 4C3J | X-ray | 3.35 Å | A=1-1664 |
| 5N61 | EM | 3.4 Å | A=1-1664 |
| 9G23 | EM | 3.4 Å | A=1-1664 |
| 9G26 | EM | 3.4 Å | A=1-1664 |
| 6HKO | EM | 3.42 Å | A=1-1664 |
| 6RUO | EM | 3.5 Å | A=1-1664 |
Showing 20 of 45 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.