6MHA: DHP1 Chromodomain Y24W variant

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.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Drosophila melanogaster
Chains
2
Atoms
570
Mol. weight
7.29 kDa
Released
25 Sept 2019

Explore 6MHA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 3 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand23-2531
β-strand26-35102
β-strand38-4582
α-helix50-523
β-strand54-5742
α-helix58-603
β-strand61-6221
α-helix64-7310
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand-2-031

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Heterochromatin protein 1Aprotein53Drosophila melanogasterP05205 (AlphaFold model)
histone H3 peptide containing trimethyllysine, H3K9me3Bprotein6Drosophila melanogasterP02299 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6MHA_1 Heterochromatin protein 1 (chains A)
EEWAVEKIIDRRVRKGMVEYYLKWKGYPETENTWEPENNLDCQDLIQQYEASR
Sequence of entity 2 (B), FASTA
>6MHA_2 histone H3 peptide containing trimethyllysine, H3K9me3 (chains B)
QTARKS

Primary citation

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:

Browse structure collections

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