Crystal structure of MOZ double PHD finger domain in complex with histone H3 crotonylation at K14. Determined by X-ray diffraction at 1.65 Å resolution. Released 26 Oct 2016.
Explore 5B76 in 3D Show helices and sheets RCSB PDB PDBe
5B76 contains 9 α-helices and 7 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 |
|---|---|---|---|
| α-helix | 201-206 | 6 | |
| β-strand | 209 | 1 | 1 |
| β-strand | 228-229 | 2 | 1 |
| β-strand | 236-237 | 2 | 1 |
| α-helix | 239-242 | 4 | |
| 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 | |
| α-helix | 300-302 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 2 |
| α-helix | 4-11 | 8 | |
| α-helix | 13-16 | 4 | |
| α-helix | 17-24 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase KAT6A | A | protein | 131 | Homo sapiens | Q92794 (AlphaFold model) |
| Histone H3 | B | protein | 26 | Homo sapiens | K7EMV3 (AlphaFold model) |
>5B76_1 Histone acetyltransferase KAT6A (chains A) SLPHEKDKPVAEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPELTVRV KALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWICQICRP RKKGRKLLQKK
>5B76_2 Histone H3 (chains B) ARTKQTARKSTGGXAPRKQLATKAAX
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Water and common crystallization additives (SO4) are not listed.
Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2. Xiong, X., Panchenko, T., Yang, S. et al. Nat Chem Biol (2016) 12:1111-1118. DOI 10.1038/nchembio.2218 · 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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