Histone acetyltransferase RTT109 (RTT109) is a 436-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q07794.
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The mean pLDDT of this model is 88.1 (confident 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 | 72% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Histone chaperone-dependent acetylase that modifies 'Lys-9', 'Lys-14', 'Lys-23', 'Lys-27', and 'Lys-56' on histone H3 (H3K9Ac, H3K14Ac and H3K23Ac, H3K27Ac, and H3K56Ac) to promote nucleosome assembly, genomic stability, DNA repair and transcriptional regulation during mitotic S-phase (PubMed:17046836, PubMed:17272723, PubMed:17320445, PubMed:17369253, PubMed:18723682, PubMed:19172748, PubMed:19683497, PubMed:20560668, PubMed:21256037, PubMed:29300933, PubMed:31194870). Its residue selectivity is influenced by the acetylation status of histone H3, and also the presence of histone chaperone ASF1 that shifts selectivity to 'Lys-56' when H3K14Ac is already present (PubMed:31194870). H3K56…
Forms a complex composed of two RTT109 subunits and one VPS75 homodimer; each RTT109 subunit interacts predominantly with VPS75 instead of interacting with the other RTT109 subunit (PubMed:17320445, PubMed:18719104, PubMed:20560668, PubMed:21256037, PubMed:31387991). Interacts with VPS75; the interaction is direct (PubMed:17272723, PubMed:17320445, PubMed:17369253, PubMed:17690098,…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2ZFN | X-ray | 1.9 Å | A=1-436 |
| 3CZ7 | X-ray | 2.0 Å | A=1-127, A=171-403 |
| 2RIM | X-ray | 2.2 Å | A=1-436 |
| 3Q66 | X-ray | 2.7 Å | C=1-436 |
| 3Q68 | X-ray | 2.7 Å | C=1-436 |
| 3Q33 | X-ray | 2.8 Å | A=1-436 |
| 3QM0 | X-ray | 3.1 Å | A=1-436 |
| 3Q35 | X-ray | 3.3 Å | A=1-436 |
| 6F0Y | NMR | B=419-433 | |
| 6O22 | Other | C=1-436 |
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