Histone acetyltransferase p300 (EP300) is a 2414-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q09472.
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The mean pLDDT of this model is 53.3 (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 | 20% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 61% |
What pLDDT means and how to read it
Functions as a histone acetyltransferase and regulates transcription via chromatin remodeling (PubMed:23415232, PubMed:23934153, PubMed:40240600, PubMed:8945521). Acetylates all four core histones in nucleosomes (PubMed:23415232, PubMed:23934153, PubMed:8945521). Histone acetylation gives an epigenetic tag for transcriptional activation (PubMed:23415232, PubMed:23934153, PubMed:8945521). Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (PubMed:23415232). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac,…
Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2 (PubMed:11959990, PubMed:9887100). Probably part of a complex with HIF1A and CREBBP (PubMed:8917528). Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2 (PubMed:12586840). Interacts (via CH1 domain) with CITED2 (via C-terminus) (PubMed:12586840,…
Cytoplasm, Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5BT3 | X-ray | 1.05 Å | A=1048-1161 |
| 3T92 | X-ray | 1.5 Å | A=1723-1818 |
| 5LPM | X-ray | 1.5 Å | A/B=1048-1161 |
| 5NU5 | X-ray | 1.6 Å | A/B=1048-1161 |
| 3BIY | X-ray | 1.7 Å | A=1287-1666 |
| 6PGU | X-ray | 1.72 Å | A/B=1287-1519, A/B=1582-1663 |
| 6V8K | X-ray | 1.84 Å | A=1287-1519, A=1581-1663 |
| 4PZS | X-ray | 1.94 Å | A=1287-1664 |
| 5KJ2 | X-ray | 1.95 Å | A=1287-1666 |
| 6DS6 | X-ray | 1.95 Å | A=1661-1713 |
| 7QGS | X-ray | 2.0 Å | A=330-420 |
| 7UGI | X-ray | 2.0 Å | A/B=1048-1161 |
| 7VHZ | X-ray | 2.0 Å | A/B=1159-1519, A/B=1581-1666 |
| 8GZC | X-ray | 2.0 Å | A/B=1159-1519, A/B=1581-1666 |
| 9IT5 | X-ray | 2.0 Å | A/B=1287-1666 |
| 5LKT | X-ray | 2.04 Å | A=1043-1519, A=1581-1666 |
| 6V90 | X-ray | 2.04 Å | A=1287-1666 |
| 4PZR | X-ray | 2.1 Å | A=1287-1664 |
| 5LPK | X-ray | 2.1 Å | A/B/C/D/E/F/G=1040-1161 |
| 7VI0 | X-ray | 2.1 Å | A/B=1159-1519, A/B=1581-1666 |
Showing 20 of 60 experimental structures (best resolution first).
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