› 3qlc

X-ray diffraction
2.5Å resolution

Complex structure of ATRX ADD domain bound to unmodified H3 1-15 peptide

Released:
DOI: 10.2210/pdb3qlc/pdb
PDB entry 3qlc coloured by chain, front view.
PDB entry 3qlc coloured by chain, side view.
PDB entry 3qlc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome.
Iwase S, Xiang B, Ghosh S, Ren T, Lewis PW, Cochrane JC, Allis CD, Picketts DJ, Patel DJ, Li H, Shi Y
Nat Struct Mol Biol 18 769-76 (2011)
PMID: 21666679

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155429 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcriptional regulator ATRX Chains: A, B
Molecule details ›
Chains: A, B
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%)
Gene names: ATRX, RAD54L, XH2
Sequence domains: Cysteine Rich ADD domain
Histone H3.3 Chains: C, D
Molecule details ›
Chains: C, D
Length: 15 amino acids
Theoretical weight: 1.57 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P84243 (Residues: 2-16; Coverage: 11%)
Gene names: H3-3A, H3-3B, H3.3A, H3.3B, H3F3, H3F3A, H3F3B, PP781

Ligands and Environments

1 bound ligand:
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3221
Unit cell:
a: 80.607Å b: 80.607Å c: 136.173Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.194 0.241
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

70 review citations

Histone methylation: a dynamic mark in health, disease and inheritance.
Greer et al. (2012)
69 more

1 mention without citation

ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome.
Iwase et al. (2011)