Crystal structure of AF9 YEATS domain in complex with dicrotonylated at K1007 and K1014 MOZ. Determined by X-ray diffraction at 2.1 Å resolution. Released 22 Jan 2025.
Explore 9ARR in 3D Show helices and sheets RCSB PDB PDBe
9ARR contains 10 α-helices and 17 β-strands across 3 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 | 3-19 | 17 | 1 |
| β-strand | 30-37 | 8 | 1 |
| α-helix | 39-41 | 3 | |
| α-helix | 44-46 | 3 | |
| β-strand | 48-54 | 7 | 2 |
| β-strand | 63-66 | 4 | 2 |
| β-strand | 71-77 | 7 | 1 |
| β-strand | 81-89 | 9 | 2 |
| β-strand | 97-104 | 8 | 2 |
| α-helix | 107-108 | 2 | |
| α-helix | 112-113 | 2 | |
| β-strand | 114-125 | 12 | 1 |
| α-helix | 129-137 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-19 | 17 | 1 |
| β-strand | 30-37 | 8 | 1 |
| α-helix | 39-41 | 3 | |
| α-helix | 44-46 | 3 | |
| β-strand | 48-54 | 7 | 3 |
| β-strand | 63-66 | 4 | 3 |
| β-strand | 71-77 | 7 | 1 |
| β-strand | 81-89 | 9 | 3 |
| β-strand | 97-104 | 8 | 3 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-125 | 12 | 1 |
| α-helix | 129-136 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 2 |
| α-helix | 3-5 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein AF-9 | A, B | protein | 138 | Homo sapiens | P42568 (AlphaFold model) |
| Histone acetyltransferase KAT6A | C | protein | 13 | Homo sapiens | Q92794 (AlphaFold model) |
>9ARR_1 Protein AF-9 (chains A, B) MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFP RPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCE KLTFNNPTEDFRRKLLKA
>9ARR_2 Histone acetyltransferase KAT6A (chains C) LTXPTLKRKXPFL
| ID | Name | Formula | Copies |
|---|---|---|---|
| LI | Lithium ion | Li | 2 |
Water and common crystallization additives (NO3, PEG, GOL) are not listed.
A multivalent engagement of ENL with MOZ. Becht, D.C., Selvam, K., Lachance, C. et al. Nat Struct Mol Biol (2025) 32:709-718. DOI 10.1038/s41594-024-01455-8 · PubMed
Other PDB entries of the same protein (UniProt P42568 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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