B-cell lymphoma 6 protein (BCL6) is a 706-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P41182.
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The mean pLDDT of this model is 52.1 (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 | 1% |
| 70 to 90 | Confident: backbone generally right | 37% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 58% |
What pLDDT means and how to read it
Transcriptional repressor mainly required for germinal center (GC) formation and antibody affinity maturation which has different mechanisms of action specific to the lineage and biological functions. Forms complexes with different corepressors and histone deacetylases to repress the transcriptional expression of different subsets of target genes. Represses its target genes by binding directly to the DNA sequence 5'-TTCCTAGAA-3' (BCL6-binding site) or indirectly by repressing the transcriptional activity of transcription factors. In GC B-cells, represses genes that function in differentiation, inflammation, apoptosis and cell cycle control, also autoregulates its transcriptional expression…
Homodimer. Interacts (via BTB domain) with the corepressors BCOR, NCOR1 and SMRT/NCOR2; the interactions are direct. Forms preferably ternary complexes with BCOR and SMRT/NCOR2 on target gene promoters but, on enhancer elements, interacts with SMRT/NCOR2 and HDAC3 to repress proximal gene expression. Interacts with histone deacetylases HDAC2, HDAC5 and HDAC9 (via the catalytic domain). Interacts…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7LWE | X-ray | 1.17 Å | A=1-129 |
| 7RV1 | X-ray | 1.17 Å | A=5-129 |
| 7OKL | X-ray | 1.2 Å | A=5-129 |
| 7LWF | X-ray | 1.22 Å | A=5-129 |
| 7RV4 | X-ray | 1.25 Å | A=5-129 |
| 7RV8 | X-ray | 1.25 Å | A=5-129 |
| 7RUY | X-ray | 1.27 Å | A=5-129 |
| 7RV2 | X-ray | 1.29 Å | A=5-129 |
| 1R29 | X-ray | 1.3 Å | A=5-129 |
| 7LWG | X-ray | 1.3 Å | A/B=5-129 |
| 7RUW | X-ray | 1.3 Å | A=5-129 |
| 7RUX | X-ray | 1.3 Å | A=5-129 |
| 7OKG | X-ray | 1.32 Å | A=5-129 |
| 7LZR | X-ray | 1.34 Å | A/B/C/D=5-129 |
| 7RV3 | X-ray | 1.35 Å | A=5-129 |
| 5N20 | X-ray | 1.38 Å | A=6-128 |
| 7ZWX | X-ray | 1.38 Å | A=5-129 |
| 6EW6 | X-ray | 1.39 Å | A=6-128 |
| 6XZZ | X-ray | 1.39 Å | A=6-129 |
| 7ZWO | X-ray | 1.39 Å | A=5-129 |
Showing 20 of 246 experimental structures (best resolution first).
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