CCAAT/enhancer-binding protein beta (CEBPB) is a 345-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P17676.
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The mean pLDDT of this model is 59.7 (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 | 19% |
| 70 to 90 | Confident: backbone generally right | 8% |
| 50 to 70 | Low: treat with caution | 26% |
| Below 50 | Very low: often disordered regions | 47% |
What pLDDT means and how to read it
Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC…
Binds DNA as a homodimer and as a heterodimer (PubMed:11018027, PubMed:11257229, PubMed:11792321). Interacts with ATF4. Binds DNA as a heterodimer with ATF4 (PubMed:11018027). Interacts with MYB; within the complex, MYB and CEBPB bind to different promoter regions (PubMed:11792321). Can form stable heterodimers with CEBPD (PubMed:1741402). Can form stable heterodimers with CEBPA and CEBPE (By…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6MG1 | X-ray | 1.75 Å | A/B=269-344 |
| 7L4V | X-ray | 1.75 Å | A/B=269-344 |
| 1GU4 | X-ray | 1.8 Å | A/B=259-336 |
| 2E42 | X-ray | 1.8 Å | A/B=259-336 |
| 1GTW | X-ray | 1.85 Å | A/B=259-336 |
| 6MG2 | X-ray | 1.93 Å | A/B=269-344 |
| 6MG3 | X-ray | 2.05 Å | A/B=269-344 |
| 1GU5 | X-ray | 2.1 Å | A/B=259-336 |
| 2E43 | X-ray | 2.1 Å | A/B=259-336 |
| 8K8D | X-ray | 2.2 Å | A/B=259-336 |
| 1H8A | X-ray | 2.23 Å | A/B=259-336 |
| 1H89 | X-ray | 2.45 Å | A/B=273-336 |
| 7UPZ | X-ray | 2.49 Å | A/B=257-336 |
| 1H88 | X-ray | 2.8 Å | A/B=259-336 |
| 1HJB | X-ray | 3.0 Å | A/B/D/E=259-345 |
| 1IO4 | X-ray | 3.0 Å | A/B=259-336 |
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