5bs7

X-ray diffraction
3.3Å resolution

Structure of histone H3/H4 in complex with Spt2

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-158671 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Histone H3.2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 111 amino acids
Theoretical weight: 12.74 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P84233 (Residues: 26-136; Coverage: 82%)
Sequence domains: Core histone H2A/H2B/H3/H4
Structure domains: Histone, subunit A
Histone H4 Chains: C, D
Molecule details ›
Chains: C, D
Length: 102 amino acids
Theoretical weight: 11.26 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P62799 (Residues: 2-103; Coverage: 99%)
Sequence domains: Centromere kinetochore component CENP-T histone fold
Structure domains: Histone, subunit A
Protein SPT2 homolog Chains: E, F
Molecule details ›
Chains: E, F
Length: 115 amino acids
Theoretical weight: 14.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q68D10 (Residues: 571-685; Coverage: 17%)
Gene name: SPTY2D1
Sequence domains: SPT2 chromatin protein

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P4322
Unit cell:
a: 121.205Å b: 121.205Å c: 118.503Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.23 0.29
Expression system: Escherichia coli