1PDQ: Polycomb chromodomain

Polycomb chromodomain complexed with the histone H3 tail containing trimethyllysine 27. Determined by X-ray diffraction at 1.76 Å resolution. Released 26 Aug 2003.

Method
X-ray diffraction
Resolution
1.76 Å
Organism
Drosophila melanogaster
Chains
2
Atoms
710
Mol. weight
10.78 kDa
Released
26 Aug 2003

Explore 1PDQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1PDQ contains 3 α-helices and 4 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, 3 β-strands

ElementResiduesLengthSheet
β-strand24-37141
β-strand40-4781
α-helix52-543
β-strand56-5941
α-helix60-623
α-helix67-726
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand23-2751

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Polycomb proteinAprotein72Drosophila melanogasterP26017 (AlphaFold model)
Histone H3.3Bprotein18P84243 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1PDQ_1 Polycomb protein (chains A)
MKKHHHHHHDNATDDPVDLVYAAEKIIQKRVKKGVVEYRVKWKGWNQRYNTWEPEVNILD
RRLIDIYEQTNK
Sequence of entity 2 (B), FASTA
>1PDQ_2 Histone H3.3 (chains B)
APRKQLATKAARKSAPST

Primary citation

Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Fischle, W., Wang, Y., Jacobs, S.A. et al. Genes Dev (2003) 17:1870-1881. DOI 10.1101/gad.1110503 · PubMed

Other PDB entries of the same protein (UniProt P26017 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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