PDBe 3ql9

X-ray diffraction
0.93Å resolution

Monoclinic complex structure of ATRX ADD bound to histone H3K9me3 peptide

Released:

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone H3.3 Chain: C
Molecule details ›
Chain: C
Length: 15 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P84243 (Residues: 2-16; Coverage: 11%)
Gene names: H3.3A, H3.3B, H3F3, H3F3A, H3F3B, PP781
Transcriptional regulator ATRX Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P46100 (Residues: 167-289; Coverage: 5%)
  • Best match: P46100-2 (Residues: 1-83, 84-85)
Gene names: ATRX, RAD54L, XH2

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: C2
Unit cell:
a: 83.719Å b: 39.452Å c: 41.057Å
α: 90° β: 111.24° γ: 90°
R-values:
R R work R free
0.123 0.122 0.131
Expression systems:
  • Not provided
  • Escherichia coli