Structure of human Asf1a in complex with histone H3. Determined by solution NMR. Released 13 Feb 2007.
Explore 2IIJ in 3D Show helices and sheets RCSB PDB PDBe
2IIJ contains 5 α-helices and 9 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 | 22-33 | 12 | 1 |
| β-strand | 38-44 | 7 | 2 |
| α-helix | 51-53 | 3 | |
| β-strand | 55-62 | 8 | 2 |
| β-strand | 66-76 | 11 | 1 |
| α-helix | 86-89 | 4 | |
| β-strand | 92-101 | 10 | 2 |
| β-strand | 104-117 | 14 | 2 |
| α-helix | 120-124 | 5 | |
| β-strand | 135-146 | 12 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 122-132 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ASF1A protein | A | protein | 158 | Homo sapiens | Q9Y294 (AlphaFold model) |
| Histone H3 | B | protein | 18 | Homo sapiens | Q71DI3 (AlphaFold model) |
>2IIJ_1 ASF1A protein (chains A) GAMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDN
>2IIJ_2 Histone H3 (chains B) GAMGKDIQLARRIRGERA
Structure of the histone chaperone asf1 bound to the histone h3 C-terminal helix and functional insights. Agez, M., Chen, J., Guerois, R. et al. Structure (2007) 15:191-199. DOI 10.1016/j.str.2007.01.002 · PubMed
Other PDB entries of the same protein (UniProt Q9Y294 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2IIJ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.