AF9 YEATS in complex with histone H3 Crotonylation at K9. Determined by X-ray diffraction at 2.7 Å resolution. Released 20 Apr 2016.
Explore 5HJB in 3D Show helices and sheets RCSB PDB PDBe
5HJB contains 4 α-helices and 12 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 | 6-19 | 14 | 1 |
| β-strand | 30-37 | 8 | 1 |
| α-helix | 39-41 | 3 | |
| β-strand | 48-54 | 7 | 2 |
| β-strand | 63-66 | 4 | 2 |
| β-strand | 71-77 | 7 | 1 |
| β-strand | 80 | 1 | 3 |
| β-strand | 81-89 | 9 | 2 |
| β-strand | 97-104 | 8 | 2 |
| β-strand | 107 | 1 | 4 |
| α-helix | 108 | 1 | |
| α-helix | 112-113 | 2 | |
| β-strand | 114-125 | 12 | 1 |
| α-helix | 129-136 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 4 |
| β-strand | 8 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein AF-9 | A | protein | 140 | Homo sapiens | P42568 (AlphaFold model) |
| peptide of Histone H3.1 | B | protein | 8 | Homo sapiens | P68431 (AlphaFold model) |
>5HJB_1 Protein AF-9 (chains A) SHMASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHES FPRPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLR CEKLTFNNPTEDFRRKLLKA
>5HJB_2 peptide of Histone H3.1 (chains B) TKQTARXS
Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain. Li, Y.Y., Sabari, B.R., Panchenko, T. et al. Mol Cell (2016) 62:181-193. DOI 10.1016/j.molcel.2016.03.028 · PubMed
Other PDB entries of the same protein (UniProt P42568 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 5HJB 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.