Histone H3.2 (H3C15) is a 136-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q71DI3.
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The mean pLDDT of this model is 86.0 (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 | 68% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 25% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer (via C-terminus of H3); this interaction is direct (PubMed:17292837). Interacts with DNAJC9, CHAF1A…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2X4W | X-ray | 1.5 Å | B=23-43 |
| 3MO8 | X-ray | 1.69 Å | B=31-42 |
| 2X4Y | X-ray | 1.7 Å | B/D/F/H/J/L/N/P=23-43 |
| 4MZG | X-ray | 1.7 Å | A/C=2-21 |
| 2X4X | X-ray | 1.85 Å | B/D/F/H=23-43 |
| 4OUC | X-ray | 1.9 Å | B=2-13 |
| 5VAC | X-ray | 1.95 Å | C=19-37 |
| 6ACE | X-ray | 1.98 Å | B=119-126 |
| 7UVA | X-ray | 1.98 Å | C/F=30-42 |
| 5B0Z | X-ray | 1.99 Å | A/E=1-136 |
| 3R93 | X-ray | 2.06 Å | E/F/G/H=2-16 |
| 4MZF | X-ray | 2.1 Å | A=2-10 |
| 4MZH | X-ray | 2.2 Å | B=2-10 |
| 5CIU | X-ray | 2.24 Å | C/D=29-43 |
| 8JLB | EM | 2.36 Å | A/E=2-136 |
| 3DB3 | X-ray | 2.4 Å | B=7-12 |
| 8JLD | EM | 2.48 Å | A/E=2-136 |
| 3QO2 | X-ray | 2.49 Å | P/Q/R/S=2-16 |
| 10YE | EM | 2.5 Å | A/E=39-135 |
| 3AV1 | X-ray | 2.5 Å | A/E=1-136 |
Showing 20 of 153 experimental structures (best resolution first).
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