Crystal Structure of MOZ double PHD finger histone H3K14ac complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 16 Oct 2013.
Explore 4LLB in 3D Show helices and sheets RCSB PDB PDBe
4LLB contains 12 α-helices and 14 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 195-197 | 3 | |
| α-helix | 203-206 | 4 | |
| β-strand | 209 | 1 | 1 |
| β-strand | 228-229 | 2 | 1 |
| β-strand | 236-237 | 2 | 1 |
| α-helix | 246-253 | 8 | |
| β-strand | 265 | 1 | 2 |
| α-helix | 275-277 | 3 | |
| β-strand | 279-280 | 2 | 2 |
| β-strand | 287-288 | 2 | 2 |
| α-helix | 290-292 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 2 |
| α-helix | 4-11 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase KAT6A | A, B | protein | 136 | Homo sapiens | Q92794 (AlphaFold model) |
| Histone H3.1 | C, D | protein | 21 | Homo sapiens | P68431 (AlphaFold model) |
>4LLB_1 Histone acetyltransferase KAT6A (chains A, B) GSHMLELPHEKDKPVAEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPE LTVRVKALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWIC QICRPRKKGRKLLQKK
>4LLB_2 Histone H3.1 (chains C, D) ARTKQTARKSTGGKAPRKQLA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 8 |
The double PHD finger domain of MOZ/MYST3 induces alpha-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification. Dreveny, I., Deeves, S.E., Fulton, J. et al. Nucleic Acids Res (2014) 42:822-835. DOI 10.1093/nar/gkt931 · PubMed
Other PDB entries of the same protein (UniProt Q92794 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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