Retinoblastoma-binding protein 5 (RBBP5) is a 538-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15291.
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The mean pLDDT of this model is 77.8 (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 | 55% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 19% |
What pLDDT means and how to read it
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 (By similarity). Does not affect ES cell self-renewal (By similarity). Component or associated component of some histone methyltransferase complexes which regulates transcription through recruitment of those complexes to gene promoters (PubMed:19131338). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3 (PubMed:19556245). Histone H3 'Lys-4' methylation represents a specific tag for epigenetic…
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 (PubMed:16253997, PubMed:17355966, PubMed:17998332, PubMed:18838538). Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7 (PubMed:15199122, PubMed:15960975,…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6KM7 | X-ray | 1.8 Å | A/B=10-325, C/D=390-480 |
| 5F6L | X-ray | 1.9 Å | J=330-356 |
| 4X8N | X-ray | 2.1 Å | B=347-356 |
| 7W67 | X-ray | 2.19 Å | F=330-356 |
| 4X8P | X-ray | 2.2 Å | B=344-355 |
| 7W6A | X-ray | 2.21 Å | F=330-356 |
| 7W6L | X-ray | 2.26 Å | D/F=330-356 |
| 3P4F | X-ray | 2.35 Å | B=371-381 |
| 5F6K | X-ray | 2.41 Å | D/F=330-356 |
| 7W6I | X-ray | 2.56 Å | F=330-356 |
| 7W6J | X-ray | 2.68 Å | F=330-356 |
| 7BRE | X-ray | 2.8 Å | C/F=330-356 |
| 6KIU | EM | 3.2 Å | N=1-538 |
| 8DU4 | EM | 3.55 Å | N=1-538 |
| 6KIV | EM | 4.0 Å | N=1-538 |
| 6KIW | EM | 4.0 Å | N=1-538 |
| 6KIX | EM | 4.1 Å | N=1-538 |
| 6PWX | EM | 4.2 Å | A=2-538 |
| 7UD5 | EM | 4.25 Å | N=1-538 |
| 6PWW | EM | 4.4 Å | A=2-538 |
Showing 20 of 27 experimental structures (best resolution first).
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