X-ray diffraction
1.6Å resolution

Hexagonal complex structure of ATRX ADD bound to H3K9me3 peptide


Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcriptional regulator ATRX Chains: A, D
Molecule details ›
Chains: A, D
Length: 129 amino acids
Theoretical weight: 14.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P46100 (Residues: 167-289; Coverage: 5%)
  • Best match: P46100-2 (Residues: 1-85)
Gene names: ATRX, RAD54L, XH2
Histone H3.3 Chains: C, F
Molecule details ›
Chains: C, F
Length: 15 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P84243 (Residues: 2-16; Coverage: 11%)
Gene names: H3-3A, H3-3B, H3.3A, H3.3B, H3F3, H3F3A, H3F3B, PP781

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P65
Unit cell:
a: 66.709Å b: 66.709Å c: 131.641Å
α: 90° β: 90° γ: 120°
R R work R free
0.158 0.157 0.179
Expression systems:
  • Escherichia coli
  • Not provided