Histone lysine acetyltransferase CREBBP (Crebbp) is a 2441-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P45481.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 52.2 (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 | 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:11115394). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (By similarity). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed:10207073, PubMed:11701890, PubMed:15220471, PubMed:16287980). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes (By similarity). Acts as a coactivator of ALX1 (By similarity). Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-BMAL1 and CLOCK-BMAL1…
Part of a complex composed of MSX3, CREBBP/CBP AND EP300/p300; the interaction with MSX3 decreases histone acetylation activity (PubMed:11115394). Interacts with DHX9 (via N-terminus); this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation (By similarity). Interacts (via transactivation domain and C-terminus) with PCNA;…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5W0I | X-ray | 1.43 Å | A=1083-1198 |
| 8CNB | X-ray | 1.99 Å | A=1079-1555, A=1620-1751 |
| 4I9O | X-ray | 2.0 Å | A=586-672 |
| 7LVS | X-ray | 2.02 Å | B=340-439 |
| 8CMZ | X-ray | 2.25 Å | A=1079-1556, A=1619-1751 |
| 6DNQ | X-ray | 2.35 Å | B/D=586-672 |
| 5U7G | X-ray | 2.4 Å | A/B=1079-1556 |
| 8CN0 | X-ray | 2.44 Å | A=1086-1556, A=1619-1751 |
| 8CNA | X-ray | 2.46 Å | A=1082-1556, A=1619-1751 |
| 8OG2 | X-ray | 2.47 Å | A=1079-1556, A=1620-1751 |
| 6DMX | X-ray | 2.8 Å | B/D/G/I=586-672 |
| 8CND | X-ray | 2.97 Å | A=1086-1556, A=1619-1751 |
| 1F81 | NMR | A=1764-1849 | |
| 1JJS | NMR | A=2067-2112 | |
| 1KBH | NMR | B=2059-2117 | |
| 1KDX | NMR | A=586-666 | |
| 1L8C | NMR | A=345-439 | |
| 1R8U | NMR | B=340-439 | |
| 1SB0 | NMR | A=586-672 | |
| 1TOT | NMR | A=1700-1751 |
Showing 20 of 34 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.