Bromodomain-containing protein 3 (BRD3) is a 726-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15059.
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The mean pLDDT of this model is 66.9 (low 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 | 33% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 42% |
What pLDDT means and how to read it
Chromatin reader that recognizes and binds acetylated histones, thereby controlling gene expression and remodeling chromatin structures (PubMed:18406326, PubMed:22464331, PubMed:27105114, PubMed:32895492). Recruits transcription factors and coactivators to target gene sites, and activates RNA polymerase II machinery for transcriptional elongation (PubMed:29567837, PubMed:32895492). In vitro, binds acetylated lysine residues on the N-terminus of histone H2A, H2B, H3 and H4 (PubMed:18406326). Involved in endoderm differentiation via its association with long non-coding RNA (lncRNA) DIGIT: BRD3 undergoes liquid-liquid phase separation upon binding to lncRNA DIGIT, promoting binding to histone…
Interacts (via bromo domain 1) with GATA1 acetylated at 'Lys-312' and 'Lys-315' (By similarity). Interacts (via bromo domain 1) with GATA2 acetylated on lysine residues (By similarity). Interacts (via NET domain) with CHD4 (via KIKL motif) (PubMed:29567837). Interacts (via NET domain) with SMARCA4 (via KIKL motif) (PubMed:29567837). Interacts (via NET domain) with NSD3 (via KIKL motif)…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6QJU | X-ray | 1.2 Å | A/B=24-144 |
| 3S92 | X-ray | 1.36 Å | A=306-416 |
| 9NN4 | X-ray | 1.37 Å | A/B=28-147 |
| 2NXB | X-ray | 1.4 Å | A/B=24-144 |
| 7TOA | X-ray | 1.41 Å | A/B=32-147 |
| 7LAY | X-ray | 1.45 Å | A/B=24-144 |
| 8CV5 | X-ray | 1.47 Å | A=307-419 |
| 7L72 | X-ray | 1.5 Å | A=306-416 |
| 7RJL | X-ray | 1.5 Å | A/B=24-144 |
| 7TO8 | X-ray | 1.5 Å | A/B=25-147 |
| 7L9L | X-ray | 1.55 Å | A=306-416 |
| 7TO9 | X-ray | 1.6 Å | A/B=25-147 |
| 9MPN | X-ray | 1.6 Å | A/B/C/D=25-147 |
| 2OO1 | X-ray | 1.7 Å | A/B/C/D=307-416 |
| 5HFR | X-ray | 1.7 Å | A/B/C/D=306-416 |
| 7R8R | X-ray | 1.8 Å | A=24-144 |
| 7UG5 | X-ray | 1.8 Å | A/B/C/D=306-416 |
| 6I5P | X-ray | 1.81 Å | B/D/F/H=245-253 |
| 24OS | X-ray | 1.83 Å | A/B=24-143 |
| 6I68 | X-ray | 1.85 Å | B/D/F/H=245-253 |
Showing 20 of 48 experimental structures (best resolution first).
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