Histone chaperone ASF1 (ASF1) is a 279-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P32447.
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The mean pLDDT of this model is 72.2 (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 | 54% |
| 70 to 90 | Confident: backbone generally right | 1% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 38% |
What pLDDT means and how to read it
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed:11172707, PubMed:11331602, PubMed:11404324, PubMed:11856374, PubMed:14680630, PubMed:15071494, PubMed:15175160, PubMed:15452122, PubMed:15542829, PubMed:15766286, PubMed:15891116, PubMed:16039596, PubMed:16303565, PubMed:16407267, PubMed:16678113, PubMed:16936140). Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways (PubMed:14585955, PubMed:15632066, PubMed:16678113). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the…
Interacts with histone H3/H4 heterodimers via both histone H3 and histone H4 (PubMed:11172707, PubMed:11412995, PubMed:11756556, PubMed:11856374, PubMed:12626510, PubMed:14680630, PubMed:15840725, PubMed:16303565, PubMed:16582440, PubMed:17081973, PubMed:27036862, PubMed:29300933, PubMed:31387991). Binds with higher affinity to H3/H4 heterodimers where histone H3 has been pre-acetylated on…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1ROC | X-ray | 1.5 Å | A=2-154 |
| 5UCB | X-ray | 1.52 Å | B=2-154 |
| 2HUE | X-ray | 1.7 Å | A=2-169 |
| 5UEA | X-ray | 1.7 Å | D/X=2-154 |
| 5UEK | X-ray | 1.7 Å | A=2-154 |
| 6AYZ | X-ray | 2.1 Å | A/M=2-154 |
| 2IDC | X-ray | 2.2 Å | A=2-155 |
| 4ZBJ | X-ray | 2.25 Å | A=2-169 |
| 4EO5 | X-ray | 2.35 Å | A=2-169 |
| 5EII | X-ray | 2.44 Å | G/I=1-156 |
| 6AZ2 | X-ray | 2.48 Å | B/D=2-154 |
| 9AWE | X-ray | 2.8 Å | A=2-159 |
| 2YGV | X-ray | 2.94 Å | A/B/C/D=1-156 |
| 8GHN | EM | 2.96 Å | O=1-279 |
| 1WG3 | X-ray | 3.0 Å | A=1-169 |
| 9AVO | X-ray | 3.0 Å | A=2-159 |
| 7UNK | EM | 3.45 Å | D=1-279 |
| 8GHM | EM | 12.0 Å | O=1-279 |
| 6F0Y | NMR | A=2-169 | |
| 6O22 | Other | D=2-279 |
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