Bromodomain-containing protein 2 (BRD2) is a 801-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P25440.
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The mean pLDDT of this model is 64.1 (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 | 32% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 50% |
What pLDDT means and how to read it
Chromatin reader protein that specifically recognizes and binds histone H4 acetylated at 'Lys-5' and 'Lys-12' (H4K5ac and H4K12ac, respectively), thereby controlling gene expression and remodeling chromatin structures (PubMed:17148447, PubMed:17848202, PubMed:18406326, PubMed:20048151, PubMed:20709061, PubMed:20871596). Recruits transcription factors and coactivators to target gene sites, and activates RNA polymerase II machinery for transcriptional elongation (PubMed:28262505). Plays a key role in genome compartmentalization via its association with CTCF and cohesin: recruited to chromatin by CTCF and promotes formation of topologically associating domains (TADs) via its ability to bind…
Homodimer (PubMed:17148447, PubMed:17848202, PubMed:20048151, PubMed:20709061). Interacts with E2F1 (PubMed:17148447). Interacts with (acetylated) STAT3; promoting STAT3 recruitment to chromatin (PubMed:28262505). Interacts with CTCF; promoting BRD2 recruitment to chromatin (By similarity)
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5IG6 | X-ray | 0.91 Å | A=348-454 |
| 5IBN | X-ray | 0.94 Å | A=348-455 |
| 6DBC | X-ray | 1.05 Å | A=348-455 |
| 6DDJ | X-ray | 1.05 Å | A=348-455 |
| 4J1P | X-ray | 1.08 Å | A=344-455 |
| 7VRM | X-ray | 1.1 Å | A=348-455 |
| 6I80 | X-ray | 1.14 Å | A/B=348-455 |
| 7VRQ | X-ray | 1.15 Å | A=348-455 |
| 5O38 | X-ray | 1.2 Å | A=344-455 |
| 5O3I | X-ray | 1.2 Å | A=344-455 |
| 7USG | X-ray | 1.2 Å | A=348-455 |
| 6K04 | X-ray | 1.25 Å | A=344-455 |
| 7VS0 | X-ray | 1.25 Å | A=348-455 |
| 7VS1 | X-ray | 1.25 Å | A=348-455 |
| 6MOA | X-ray | 1.27 Å | A=346-455 |
| 7USH | X-ray | 1.27 Å | A=348-455 |
| 5XHK | X-ray | 1.28 Å | A=348-455 |
| 7NPZ | X-ray | 1.28 Å | AAA=344-455 |
| 7NQ0 | X-ray | 1.3 Å | AAA=344-455 |
| 7OE8 | X-ray | 1.3 Å | A=344-455 |
Showing 20 of 174 experimental structures (best resolution first).
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