P06400: Retinoblastoma-associated protein (RB1)

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.

Gene
RB1
Organism
Homo sapiens
Length
928 residues
Mean pLDDT
76.1
Model
AF-P06400-F1 v6
Model created
1 Aug 2025
PDB structures
19

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Model confidence (pLDDT)

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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate51%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions22%

What pLDDT means and how to read it

Function

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).…

Subunit structure

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…

Subcellular location

Nucleus, Cytoplasm

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
2R7GX-ray1.67 ÅA/C=380-787
1GUXX-ray1.85 ÅA=372-589, B=636-787
4ELLX-ray1.98 ÅA/B=380-787
2QDJX-ray2.0 ÅA=52-355
9DHUX-ray2.16 ÅA/B=380-786
1N4MX-ray2.2 ÅA/B=380-785
9DHFX-ray2.26 ÅA/B=380-793
1AD6X-ray2.3 ÅA=378-562
9DHCX-ray2.32 ÅA/B=380-793
4CRIX-ray2.35 ÅC/D=802-817
9DGKX-ray2.38 ÅA/B=380-793
1H25X-ray2.5 ÅE=868-878
1PJMX-ray2.5 ÅA=858-877
3POMX-ray2.5 ÅA/B=380-577, A/B=643-787
2AZEX-ray2.55 ÅC=829-874
1O9KX-ray2.6 ÅA/C/E/G=372-589, B/D/F/H=636-787
4ELJX-ray2.7 ÅA=53-787
1GH6X-ray3.2 ÅB=379-577, B=645-772
3N5UX-ray3.2 ÅC=870-882

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