Bromodomain adjacent to zinc finger domain protein 2B (BAZ2B) is a 2168-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UIF8.
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The mean pLDDT of this model is 54.3 (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 | 15% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 57% |
What pLDDT means and how to read it
Regulatory subunit of the ATP-dependent BRF-1 and BRF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). The BRF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the BRF-5 ISWI chromatin remodeling complex (PubMed:28801535). Chromatin reader protein, which may play a role in transcriptional regulation via interaction with ISWI (By…
Component of the BRF-1 ISWI chromatin remodeling complex, at least composed of SMARCA1 and BAZ2B, which regulates the spacing of histone octamers on the DNA template to facilitate access to DNA (PubMed:28801535). Within the BRF-1 ISWI chromatin remodeling complex interacts with SMARCA1; the interaction is direct (PubMed:28801535). Component of the BRF-5 ISWI chromatin remodeling complex, at…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5PG1 | X-ray | 1.49 Å | A=2054-2168 |
| 5PFM | X-ray | 1.54 Å | A=2054-2168 |
| 5PGB | X-ray | 1.57 Å | A=2054-2168 |
| 5PGJ | X-ray | 1.58 Å | A=2054-2168 |
| 5PGA | X-ray | 1.59 Å | A=2054-2168 |
| 4QC3 | X-ray | 1.6 Å | A/B=2062-2166 |
| 4QF3 | X-ray | 1.6 Å | A/B=1928-1983 |
| 5PGC | X-ray | 1.61 Å | A=2054-2168 |
| 5PG9 | X-ray | 1.62 Å | A=2054-2168 |
| 5PDG | X-ray | 1.63 Å | A=2054-2168 |
| 5PFW | X-ray | 1.64 Å | A=2054-2168 |
| 5PGS | X-ray | 1.64 Å | A=2054-2168 |
| 5CQ8 | X-ray | 1.65 Å | A=2054-2168 |
| 5DYU | X-ray | 1.65 Å | A=2054-2167 |
| 5E9Y | X-ray | 1.65 Å | A=2054-2167 |
| 5PB8 | X-ray | 1.65 Å | A=2054-2168 |
| 5PBX | X-ray | 1.65 Å | A=2054-2168 |
| 5PCV | X-ray | 1.65 Å | A=2054-2168 |
| 5PE5 | X-ray | 1.65 Å | A=2054-2168 |
| 5PE8 | X-ray | 1.65 Å | A=2054-2168 |
Showing 20 of 264 experimental structures (best resolution first).
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