5T1G: Chromo shadow domain of CBX1

chromo shadow domain of CBX1 in complex with a histone peptide. Determined by X-ray diffraction at 1.9 Å resolution. Released 14 Sept 2016.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
2
Atoms
533
Mol. weight
10.9 kDa
Released
14 Sept 2016

Explore 5T1G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5T1G 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
α-helix112-1154
β-strand119-12681
β-strand133-13861
β-strand145-14841
α-helix149-1557
α-helix157-16610
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand47-4821

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chromobox protein homolog 1Aprotein79Homo sapiensP83916 (AlphaFold model)
Histone H3.1Bprotein15Homo sapiensP68431 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5T1G_1 Chromobox protein homolog 1 (chains A)
GEKPRGFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEE
RLTWHSYPSEDDDKKDDKN
Sequence of entity 2 (B), FASTA
>5T1G_2 Histone H3.1 (chains B)
PHRYRPGTVALREIR

Primary citation

chromo shadow domain of CBX1 in complex with a histone peptide. Liu, Y., Tempel, W., Bountra, C. et al. To be published.

Other PDB entries of the same protein (UniProt P83916 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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