Retinoblastoma-associated protein (RB1) is a 928-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P06400.
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The mean pLDDT of this model is 76.1 (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 | 51% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 14% |
| Below 50 | Very low: often disordered regions | 22% |
What pLDDT means and how to read it
Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed:10499802). The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes (PubMed:10499802). Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription (PubMed:10499802). Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase (PubMed:10499802). RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C (PubMed:15084261).…
The hypophosphorylated form interacts with and sequesters the E2F1 transcription factor, thereby inhibiting E2F1 transcription (PubMed:20940255, PubMed:8336704). Interacts with heterodimeric E2F/DP transcription factor complexes containing TFDP1 and either E2F1, E2F3, E2F4 or E2F5, or TFDP2 and E2F4. Interacts (when hyperphosphorylated and hypophosphorylated) with PKP3; the interaction inhibits…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2R7G | X-ray | 1.67 Å | A/C=380-787 |
| 1GUX | X-ray | 1.85 Å | A=372-589, B=636-787 |
| 4ELL | X-ray | 1.98 Å | A/B=380-787 |
| 2QDJ | X-ray | 2.0 Å | A=52-355 |
| 9DHU | X-ray | 2.16 Å | A/B=380-786 |
| 1N4M | X-ray | 2.2 Å | A/B=380-785 |
| 9DHF | X-ray | 2.26 Å | A/B=380-793 |
| 1AD6 | X-ray | 2.3 Å | A=378-562 |
| 9DHC | X-ray | 2.32 Å | A/B=380-793 |
| 4CRI | X-ray | 2.35 Å | C/D=802-817 |
| 9DGK | X-ray | 2.38 Å | A/B=380-793 |
| 1H25 | X-ray | 2.5 Å | E=868-878 |
| 1PJM | X-ray | 2.5 Å | A=858-877 |
| 3POM | X-ray | 2.5 Å | A/B=380-577, A/B=643-787 |
| 2AZE | X-ray | 2.55 Å | C=829-874 |
| 1O9K | X-ray | 2.6 Å | A/C/E/G=372-589, B/D/F/H=636-787 |
| 4ELJ | X-ray | 2.7 Å | A=53-787 |
| 1GH6 | X-ray | 3.2 Å | B=379-577, B=645-772 |
| 3N5U | X-ray | 3.2 Å | C=870-882 |
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