5T1I: CBX3 chromo shadow domain

CBX3 chromo shadow domain in complex with histone H3 peptide. Determined by X-ray diffraction at 1.6 Å resolution. Released 14 Sept 2016.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Homo sapiens
Chains
3
Atoms
1,246
Mol. weight
17.14 kDa
Released
14 Sept 2016

Explore 5T1I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5T1I contains 9 α-helices and 11 β-strands across 3 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: 5 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix112-1143
α-helix116-1194
α-helix121-1222
β-strand123-13081
β-strand137-14261
β-strand149-15241
α-helix153-1597
α-helix161-1699
β-strand172-17432
Chain B: 4 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix116-1194
α-helix121-1222
β-strand123-13083
β-strand137-14263
β-strand149-15243
α-helix153-1597
α-helix161-17111
β-strand172-17432
Chain C: 0 helices, 3 β-strands
ElementResiduesLengthSheet
β-strand4211
β-strand44-4852
β-strand5013

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chromobox protein homolog 3A, Bprotein68Homo sapiensQ13185 (AlphaFold model)
Histone H3.1Cprotein15Homo sapiensP68431 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5T1I_1 Chromobox protein homolog 3 (chains A, B)
GAADKPRGFARGLDPERIIGATDSSGELMFLMKWKDSDEADLVLAKEANMKCPQIVIAFY
EERLTWHS
Sequence of entity 2 (C), FASTA
>5T1I_2 Histone H3.1 (chains C)
PHRYRPGTVALREIR

Primary citation

Peptide recognition by heterochromatin protein 1 (HP1) chromoshadow domains revisited: Plasticity in the pseudosymmetric histone binding site of human HP1. Liu, Y., Qin, S., Lei, M. et al. J Biol Chem (2017) 292:5655-5664. DOI 10.1074/jbc.M116.768374 · PubMed

Other PDB entries of the same protein (UniProt Q13185 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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