› 3nqu

X-ray diffraction
2.5Å resolution

Crystal structure of partially trypsinized (CENP-A/H4)2 heterotetramer

Released:
DOI: 10.2210/pdb3nqu/pdb
PDB entry 3nqu coloured by chain, front view.
PDB entry 3nqu coloured by chain, side view.
PDB entry 3nqu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres.
Sekulic N, Bassett EA, Rogers DJ, Black BE
Nature 467 347-51 (2010)
PMID: 20739937

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155957 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone H3-like centromeric protein A Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 16.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49450 (Residues: 1-140; Coverage: 100%)
Gene name: CENPA
Sequence domains: Core histone H2A/H2B/H3/H4
Structure domains: Histone, subunit A
Histone H4 Chain: B
Molecule details ›
Chain: B
Length: 103 amino acids
Theoretical weight: 11.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62805 (Residues: 1-103; Coverage: 100%)
Gene names: H4-16, H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4C1, H4C11, H4C12, H4C13, H4C14, H4C15, H4C16, H4C2, H4C3, H4C4, H4C5, H4C6, H4C8, H4C9, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4
Sequence domains: Centromere kinetochore component CENP-T histone fold
Structure domains: Histone, subunit A

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P6522
Unit cell:
a: 61.457Å b: 61.457Å c: 185.619Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.236 0.302
Expression system: Escherichia coli

Quick links

Citations

40 review citations

The molecular basis for centromere identity and function.
McKinley et al. (2016)
39 more

3 mentions without citation

HLA and autoantibodies define scleroderma subtypes and risk in African and European Americans and suggest a role for molecular mimicry.
Gourh et al. (2020)
2 more