Peregrin (BRPF1) is a 1214-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P55201.
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The mean pLDDT of this model is 67.5 (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 | 27% |
| 70 to 90 | Confident: backbone generally right | 29% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 34% |
What pLDDT means and how to read it
Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity (PubMed:16387653, PubMed:24065767, PubMed:27939640). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac) (PubMed:24065767). Some HAT complexes preferentially mediate histone H3 'Lys-23' (H3K23ac) acetylation (PubMed:27939640). Positively regulates the transcription of RUNX1 and RUNX2 (PubMed:18794358)
Component of some HBO1 complex composed of KAT7/HBO1, MEAF6, ING5, and BRPF1 (PubMed:24065767). Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 (PubMed:16387653, PubMed:18794358, PubMed:27939640). Interacts (via PHD-type zinc finger domains) with unmethylated histone H3 at 'Lys-4' (H3K4me0) (PubMed:24065767). Interacts with…
Nucleus, Chromosome, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5MWZ | X-ray | 1.25 Å | A=626-740 |
| 3L42 | X-ray | 1.3 Å | A=1079-1207 |
| 5C6S | X-ray | 1.3 Å | A=1079-1207 |
| 5FFV | X-ray | 1.3 Å | A/B=626-740 |
| 5O5F | X-ray | 1.3 Å | A=626-740 |
| 5ETB | X-ray | 1.33 Å | A=626-740 |
| 5D7X | X-ray | 1.35 Å | A=626-740 |
| 7C4I | X-ray | 1.37 Å | A=625-740 |
| 5EM3 | X-ray | 1.4 Å | A=626-740 |
| 5ETD | X-ray | 1.4 Å | A=626-740 |
| 8QAZ | X-ray | 1.4 Å | A=626-740 |
| 8QB2 | X-ray | 1.42 Å | A=626-740 |
| 5EV9 | X-ray | 1.45 Å | A=626-740 |
| 5EVA | X-ray | 1.45 Å | A=626-740 |
| 5O55 | X-ray | 1.45 Å | A=626-740 |
| 8QB0 | X-ray | 1.45 Å | A=626-740 |
| 5EPS | X-ray | 1.47 Å | A=627-740 |
| 2X4W | X-ray | 1.5 Å | A=1076-1205 |
| 5FFW | X-ray | 1.5 Å | A/B=626-740 |
| 5FG5 | X-ray | 1.5 Å | A/B=626-740 |
Showing 20 of 66 experimental structures (best resolution first).
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