Crystal structure of MOZ double PHD finger mutant-S210D/N235R in complex with histone H3 crotonylation at K14. Determined by X-ray diffraction at 1.4 Å resolution. Released 26 Oct 2016.
Explore 5B78 in 3D Show helices and sheets RCSB PDB PDBe
5B78 contains 10 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 | 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 | 239-242 | 4 | |
| α-helix | 246-252 | 7 | |
| 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 | 14-16 | 3 | |
| α-helix | 17-19 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase KAT6A | A | protein | 131 | Homo sapiens | Q92794 (AlphaFold model) |
| Histone H3 | B | protein | 25 | Homo sapiens | K7EMV3 (AlphaFold model) |
>5B78_1 Histone acetyltransferase KAT6A (chains A) SLPHEKDKPVAEPIPICDFCLGTKEQNREKKPEELISCADCGRSGHPSCLKFSPELTVRV KALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWICQICRP RKKGRKLLQKK
>5B78_2 Histone H3 (chains B) ARTKQTARKSTGGXAPRKQLATKAA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
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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