9SQK: Crystal structure hASF1A 156-cr17
Crystal structure hASF1A 156-cr17. Determined by X-ray diffraction at 1.7 Å resolution. Released 2 Sept 2026.
- Method
- X-ray diffraction
- Resolution
- 1.7 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 6,889
- Mol. weight
- 81.11 kDa
- Released
- 2 Sept 2026
Explore 9SQK in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9SQK contains 35 α-helices and 44 β-strands across 8 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.
Chain A: 8 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-12 | 9 | 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 |
| α-helix | 64-66 | 3 | |
| 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 |
Chain B: 8 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-12 | 9 | 3 |
| β-strand | 16-17 | 2 | 4 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 3 |
| β-strand | 38-45 | 8 | 4 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-62 | 9 | 4 |
| α-helix | 65-66 | 2 | |
| β-strand | 68-76 | 9 | 3 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-89 | 4 | |
| β-strand | 91-101 | 11 | 4 |
| β-strand | 104-117 | 14 | 4 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 4 |
| β-strand | 145-148 | 4 | 4 |
Chain C: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-11 | 8 | 5 |
| β-strand | 16-17 | 2 | 6 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 5 |
| β-strand | 38-45 | 8 | 6 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-62 | 9 | 6 |
| β-strand | 68-76 | 9 | 5 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-89 | 4 | |
| β-strand | 91-101 | 11 | 6 |
| β-strand | 104-117 | 14 | 6 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 6 |
| β-strand | 145-148 | 4 | 6 |
Chain D: 8 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-11 | 8 | 7 |
| β-strand | 16-17 | 2 | 8 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 7 |
| β-strand | 38-45 | 8 | 8 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-62 | 9 | 8 |
| α-helix | 64-66 | 3 | |
| β-strand | 68-76 | 9 | 7 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-89 | 4 | |
| β-strand | 91-101 | 11 | 8 |
| β-strand | 104-117 | 14 | 8 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 8 |
| β-strand | 145-148 | 4 | 8 |
Chains E, G and H: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-6 | 4 | |
| β-strand | 13 | 1 | 2 |
Chain F: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-6 | 5 | |
| β-strand | 13 | 1 | 6 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone chaperone ASF1A | A, B, C, D | protein | 157 | Homo sapiens | Q9Y294 (AlphaFold model) |
| cr17 | E, F, G, H | protein | 18 | Homo sapiens | |
Sequence of entity 1 (A, B, C, D), FASTA
>9SQK_1 Histone chaperone ASF1A (chains A, B, C, D)
GAMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD
SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT
ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWED
Sequence of entity 2 (E, F, G, H), FASTA
>9SQK_2 cr17 (chains E, F, G, H)
XRKXXXXRIXXXVTTXXX
Primary citation
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:
- 9SVO 1.6 Å, Crystal structure hASF1A 156-cr5
- 9TRB 1.65 Å, Crystal structure hASF1A 156-cr13
- 6ZUF 1.8 Å, Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone
- 6F0H 1.98 Å, Crystal structure ASF1-ip4
- 9SS3 2.0 Å, Crystal structure hASF1A 156-cr7
- 6F0F 2.0 Å, Crystal structure ASF1-ip2_s
- 7LNY 2.1 Å, Apo structure of the Histone chaperone ASF1A residues 1-155
- 8CJ2 2.13 Å, Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone
- 6F0G 2.3 Å, Crystal structure ASF1-ip3
- 8CJ1 2.56 Å, Urea-based foldamer inhibitor c3u_3 chimera in complex with ASF1 histone chaperone
- 2I32 2.7 Å, Structure of a human ASF1a-HIRA complex and insights into specificity of histone…
- 2IO5 2.7 Å, Crystal structure of the CIA- histone H3-H4 complex
Browse structure collections
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