dHP1 Chromodomain Y24W variant bound to histone H3 peptide containing trimethyllysine. Determined by X-ray diffraction at 1.5 Å resolution. Released 25 Sept 2019.
Explore 6MHA in 3D Show helices and sheets RCSB PDB PDBe
6MHA contains 3 α-helices and 6 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 |
|---|---|---|---|
| β-strand | 23-25 | 3 | 1 |
| β-strand | 26-35 | 10 | 2 |
| β-strand | 38-45 | 8 | 2 |
| α-helix | 50-52 | 3 | |
| β-strand | 54-57 | 4 | 2 |
| α-helix | 58-60 | 3 | |
| β-strand | 61-62 | 2 | 1 |
| α-helix | 64-73 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | -2-0 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heterochromatin protein 1 | A | protein | 53 | Drosophila melanogaster | P05205 (AlphaFold model) |
| histone H3 peptide containing trimethyllysine, H3K9me3 | B | protein | 6 | Drosophila melanogaster | P02299 (AlphaFold model) |
>6MHA_1 Heterochromatin protein 1 (chains A) EEWAVEKIIDRRVRKGMVEYYLKWKGYPETENTWEPENNLDCQDLIQQYEASR
>6MHA_2 histone H3 peptide containing trimethyllysine, H3K9me3 (chains B) QTARKS
Thermodynamic consequences of Tyr to Trp mutations in the cation-pi-mediated binding of trimethyllysine by the HP1 chromodomain. Krone, M.W., Albanese, K.I., Guseman, A.J. et al. Chem Sci (2020) 11:3495-3500. DOI 10.1039/D0SC00227E
Other PDB entries of the same protein (UniProt P05205 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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