P28749: Retinoblastoma-like protein 1 (RBL1)

Retinoblastoma-like protein 1 (RBL1) is a 1068-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P28749.

Gene
RBL1
Organism
Homo sapiens
Length
1068 residues
Mean pLDDT
71.8
Model
AF-P28749-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.8 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate37%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions26%

What pLDDT means and how to read it

Function

Key regulator of entry into cell division (PubMed:17671431). Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation (By similarity). Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression (By similarity). Controls histone H4 'Lys-20' trimethylation (By similarity). Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters (By similarity). Potent inhibitor of E2F-mediated trans-activation (PubMed:8319904). May act as a tumor suppressor (PubMed:8319904)

Subunit structure

Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2 (PubMed:16360038, PubMed:17671431). The complex exists in quiescent cells where it represses cell cycle-dependent genes (PubMed:17671431). It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7SMDX-ray2.15 ÅA=391-972
4YOZX-ray2.25 ÅA=391-593, A=676-972
4YOSX-ray2.3 ÅA=391-599, A=781-972
4YOOX-ray2.4 ÅA=391-972
9C6BEM2.6 ÅD=612-687
7SMEX-ray2.64 ÅA=391-972
7SMCX-ray2.7 ÅA/C=391-972
1H28X-ray2.8 ÅE/F=653-663
5TUVX-ray2.9 ÅC/F=994-1031
7SMFX-ray3.0 ÅA/C=391-972

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