CREB-binding protein (CREBBP) is a 2442-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92793.
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The mean pLDDT of this model is 52.5 (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 | 18% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 61% |
What pLDDT means and how to read it
Acetylates histones, giving a specific tag for transcriptional activation (PubMed:21131905, PubMed:24616510). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed:21131905). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed:10490106, PubMed:11154691, PubMed:12738767, PubMed:12929931, PubMed:24207024, PubMed:28790157, PubMed:30540930, PubMed:35675826, PubMed:9707565). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity…
Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. Interacts with GATA1; the interaction results in acetylation and enhancement of transcriptional activity of GATA1. Interacts with MAF and ZCCHC12. Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5I86 | X-ray | 1.05 Å | A/B=1082-1197 |
| 5J0D | X-ray | 1.05 Å | A=1081-1197 |
| 5I89 | X-ray | 1.07 Å | A=1082-1197 |
| 5KTW | X-ray | 1.09 Å | A/B/C=1085-1196 |
| 4NYX | X-ray | 1.1 Å | A=1081-1197 |
| 4NR7 | X-ray | 1.2 Å | A=1081-1197 |
| 5EP7 | X-ray | 1.2 Å | A=1081-1197 |
| 6YIL | X-ray | 1.22 Å | A=1081-1197 |
| 5MMG | X-ray | 1.23 Å | A=1081-1197 |
| 5MPN | X-ray | 1.23 Å | A=1081-1197 |
| 6YIM | X-ray | 1.23 Å | A=1081-1197 |
| 7WX2 | X-ray | 1.24 Å | A=1081-1197 |
| 5OWK | X-ray | 1.25 Å | A=1081-1197 |
| 5KTX | X-ray | 1.27 Å | A=1085-1196 |
| 9GET | X-ray | 1.29 Å | A=1081-1197 |
| 5ENG | X-ray | 1.3 Å | A=1081-1197 |
| 6AXQ | X-ray | 1.3 Å | A/B/C/D=1085-1196 |
| 5I83 | X-ray | 1.35 Å | A=1082-1197 |
| 5MME | X-ray | 1.35 Å | A/B=1081-1197 |
| 5MQG | X-ray | 1.35 Å | A/B=1081-1197 |
Showing 20 of 144 experimental structures (best resolution first).
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