PDBe 2lbm

Solution NMR

Solution structure of the ADD domain of ATRX complexed with histone tail H3 1-15 K9me3

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):
Transcriptional regulator ATRX Chain: A
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 16.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P46100 (Residues: 159-296; Coverage: 6%)
  • Best match: P46100-6 (Residues: 124-257)
Gene names: ATRX, RAD54L, XH2
Histone H3.1 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: P68431 (Residues: 2-16; Coverage: 11%)
Gene names: H3FA, H3FB, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3C, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 75%
Refinement method: simulated annealing
Chemical shifts: BMR17569  
Expression systems:
  • Escherichia coli
  • Not provided