8i17

X-ray diffraction
1.98Å resolution

Structural basis for H2A-H2B recognitions by human Spt16

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for H2A-H2B recognitions by human Spt16.
Biochem Biophys Res Commun 651 85-91 (2023)
PMID: 36801613

Function and Biology Details

Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-138259 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Histone H2A type 1-B/E Chains: A, D, G
Molecule details ›
Chains: A, D, G
Length: 100 amino acids
Theoretical weight: 11.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli B
UniProt:
  • Canonical: P04908 (Residues: 14-113; Coverage: 77%)
Gene names: H2AC4, H2AC8, H2AFA, H2AFM, HIST1H2AB, HIST1H2AE
Sequence domains:
Histone H2B type 1-J Chains: B, E, H
Molecule details ›
Chains: B, E, H
Length: 100 amino acids
Theoretical weight: 11.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli B
UniProt:
  • Canonical: P06899 (Residues: 28-126; Coverage: 79%)
Gene names: H2BC11, H2BFR, HIST1H2BJ
Sequence domains: Core histone H2A/H2B/H3/H4
FACT complex subunit SPT16 Chains: C, F, I
Molecule details ›
Chains: C, F, I
Length: 42 amino acids
Theoretical weight: 4.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli B
UniProt:
  • Canonical: Q9Y5B9 (Residues: 926-965; Coverage: 4%)
Gene names: FACT140, FACTP140, SUPT16H
Sequence domains: FACT complex subunit SPT16, C-terminal domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P1
Unit cell:
a: 46.852Å b: 49.084Å c: 85.195Å
α: 85.95° β: 74.31° γ: 61.8°
R-values:
R R work R free
0.172 0.17 0.211
Expression system: Escherichia coli B