Histone chaperone ASF1A (ASF1A) is a 204-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y294.
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The mean pLDDT of this model is 84.1 (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 | 74% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 18% |
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:10759893, PubMed:11897662, PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:16151251, PubMed:21454524). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly (PubMed:11897662, PubMed:14718166, PubMed:15664198). Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex…
Interacts with histone H3 (via C-terminus), including histone H3.1, H3.2 and H3.3, and histone H4; the interaction with H3 is direct (PubMed:10759893, PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:15840725, PubMed:17292837, PubMed:22195965, PubMed:33857403). Probably interacts with the heterodimeric form of H3-H4 taking the place of the second dimer (PubMed:17292837). Interacts with…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6ZUF | X-ray | 1.8 Å | A/B=1-156 |
| 6F0H | X-ray | 1.98 Å | A/C=1-156 |
| 6F0F | X-ray | 2.0 Å | A=1-156 |
| 7LNY | X-ray | 2.1 Å | A/B/C/D/E/F/G=1-155 |
| 8CJ2 | X-ray | 2.13 Å | A/B/C/D=1-156 |
| 6F0G | X-ray | 2.3 Å | A/B=1-156 |
| 8CJ1 | X-ray | 2.56 Å | A/B/C/D/E/F/G/H=1-156 |
| 2I32 | X-ray | 2.7 Å | A/B=1-157 |
| 2IO5 | X-ray | 2.7 Å | A=1-172 |
| 7LO0 | X-ray | 2.71 Å | A/B/C/D/E/F/G/H=1-155 |
| 8Z50 | X-ray | 2.8 Å | A=1-173 |
| 8BV1 | X-ray | 2.83 Å | A/B/C/D/E/F=1-156 |
| 7V6Q | X-ray | 3.0 Å | A/E=1-156 |
| 8CJ3 | X-ray | 3.0 Å | A=1-156 |
| 3AAD | X-ray | 3.3 Å | B/D=1-155 |
| 5C3I | X-ray | 3.5 Å | A/E/I/M/Q/U=1-175 |
| 9CVC | EM | 3.5 Å | C/D/E=1-204 |
| 9IMZ | EM | 3.75 Å | C/D/E=1-172 |
| 1TEY | NMR | A=1-156 | |
| 2IIJ | NMR | A=1-156 |
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