Crystal structure of MOZ. Determined by X-ray diffraction at 1.47 Å resolution. Released 27 Jun 2012.
Explore 3V43 in 3D Show helices and sheets RCSB PDB PDBe
3V43 contains 5 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 | 203-206 | 4 | |
| β-strand | 209 | 1 | 1 |
| α-helix | 226-227 | 2 | |
| 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 |
| β-strand | 279-280 | 2 | 2 |
| β-strand | 287-288 | 2 | 2 |
| α-helix | 290-292 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase KAT6A | A | protein | 112 | Homo sapiens | Q92794 (AlphaFold model) |
| Histone H3.1 | Q | protein | 18 | Homo sapiens | P68431 (AlphaFold model) |
>3V43_1 Histone acetyltransferase KAT6A (chains A) HMEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPELTVRVKALRWQCIE CKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWICQICRPR
>3V43_2 Histone H3.1 (chains Q) ARTKQTARKSTGGKAPRK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Water and common crystallization additives (ACT) are not listed.
Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription. Qiu, Y., Liu, L., Zhao, C. et al. Genes Dev (2012) 26:1376-1391. DOI 10.1101/gad.188359.112 · 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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