Crystal structure hASF1A 156-cr7. Determined by X-ray diffraction at 2.0 Å resolution. Released 2 Sept 2026.
Explore 9SS3 in 3D Show helices and sheets RCSB PDB PDBe
9SS3 contains 8 α-helices and 11 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-11 | 8 | 1 |
| β-strand | 16-17 | 2 | 2 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 1 |
| β-strand | 38-45 | 8 | 2 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-62 | 9 | 2 |
| β-strand | 68-76 | 9 | 1 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-89 | 4 | |
| β-strand | 91-101 | 11 | 2 |
| β-strand | 104-117 | 14 | 2 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 2 |
| β-strand | 145-148 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-6 | 5 | |
| β-strand | 13-15 | 3 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone chaperone ASF1A | A | protein | 157 | Homo sapiens | Q9Y294 (AlphaFold model) |
| cr7 | B | protein | 20 | Homo sapiens |
>9SS3_1 Histone chaperone ASF1A (chains A) GAMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWED
>9SS3_2 cr7 (chains B) XRKXXXXRIXXXVTLDGFGX
Downsizing the Histone H3-H4 Quaternary Structure Into Foldamer Mimetics Yields High-Affinity and Cell-Permeable Ligands of ASF1. Li, B., Perrin, M.E., Maillard, E. et al. Angew Chem Int Ed Engl (2026):e4112426-e4112426. DOI 10.1002/anie.4112426 · PubMed
Other PDB entries of the same protein (UniProt Q9Y294 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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