Q8BX09: Retinoblastoma-binding protein 5 (Rbbp5)

Retinoblastoma-binding protein 5 (Rbbp5) is a 538-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8BX09.

Gene
Rbbp5
Organism
Mus musculus
Length
538 residues
Mean pLDDT
77.9
Model
AF-Q8BX09-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.9 (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 right22%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (PubMed:21335234). Does not affect ES cell self-renewal (PubMed:21335234). Component or associated component of some histone methyltransferase complexes which regulates transcription through recruitment of those complexes to gene promoters (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3 (By similarity). Histone H3 'Lys-4' methylation represents a specific tag for epigenetic…

Subunit structure

Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 (By similarity). Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7 (By similarity). Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2XL2X-ray2.4 ÅC/D=369-381
5OV3X-ray2.45 ÅA/B=2-380, C=361-366
2XL3X-ray2.7 ÅC/E=369-381

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