› 2ld1

Solution NMR

Structures and chemical shift assignments for the ADD domain of the ATRX protein

Released:
DOI: 10.2210/pdb2ld1/pdb
PDB entry 2ld1 coloured by chain, ensemble of 34 models, front view.
PDB entry 2ld1 coloured by chain, ensemble of 34 models, side view.
PDB entry 2ld1 coloured by chain, ensemble of 34 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX.
Argentaro A, Yang JC, Chapman L, Kowalczyk MS, Gibbons RJ, Higgs DR, Neuhaus D, Rhodes D
Proc Natl Acad Sci U S A 104 11939-44 (2007)
PMID: 17609377

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155427 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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%)
Gene names: ATRX, RAD54L, XH2
Sequence domains: Cysteine Rich ADD domain

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 74%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

41 review citations

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers.
Taverna et al. (2007)
40 more