Histone acetyltransferase ESA1 (ESA1) is a 445-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q08649.
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The mean pLDDT of this model is 81.8 (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 | 56% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
Catalytic component of the NuA4 histone acetyltransferase (HAT), a multiprotein complex involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z (PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:12379856, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:16543223, PubMed:18245364, PubMed:9520405, PubMed:9858608). Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac (PubMed:10082517,…
Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2. The complex interacts with histones H4 (HHF1 and HHF2), H3 (HHT1 and HHT2) and H2A (HTA1 and HTA2)
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3TO7 | X-ray | 1.9 Å | A=160-435 |
| 1FY7 | X-ray | 2.0 Å | A=160-435 |
| 3TO9 | X-ray | 2.0 Å | A=160-435 |
| 3TO6 | X-ray | 2.1 Å | A=160-435 |
| 1MJA | X-ray | 2.26 Å | A=160-435 |
| 1MJ9 | X-ray | 2.5 Å | A=160-435 |
| 1MJB | X-ray | 2.5 Å | A=160-435 |
| 5J9T | X-ray | 2.7 Å | A/E/I=141-445 |
| 5J9W | X-ray | 2.8 Å | A/E/I=141-445 |
| 5J9U | X-ray | 2.95 Å | A/E/I=141-445 |
| 5J9Q | X-ray | 3.25 Å | A/E/I=141-445 |
| 7VVU | EM | 3.4 Å | P=1-445 |
| 8X2X | EM | 3.8 Å | K=1-445 |
| 8X2Z | EM | 3.9 Å | K=1-445 |
| 8X2Y | EM | 4.1 Å | K=1-445 |
| 8X30 | EM | 4.3 Å | K/O=1-445 |
| 8X32 | EM | 4.4 Å | K=1-445 |
| 8X31 | EM | 6.2 Å | K=1-445 |
| 7VVZ | EM | 8.8 Å | P=1-445 |
| 2RNZ | NMR | A=17-89 |
Showing 20 of 21 experimental structures (best resolution first).
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