› 6hka

Solution NMR

The solution structure of the micelle-associated FATC domain of the human protein kinase ataxia telangiectasia mutated (ATM)

Released:
DOI: 10.2210/pdb6hka/pdb
PDB entry 6hka coloured by chain, ensemble of 20 models, front view.
PDB entry 6hka coloured by chain, ensemble of 20 models, side view.
PDB entry 6hka coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
NMR- and MD simulation-based structural characterization of the membrane-associating FATC domain of ataxia telangiectasia mutated.
Abd Rahim MS, Cherniavskyi YK, Tieleman DP, Dames SA
J Biol Chem 294 7098-7112 (2019)
PMID: 30867195

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148789 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Immunoglobulin G-binding protein G; Serine-protein kinase ATM Chain: A
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 11.02 KDa
Source organisms: Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P19909 (Residues: 304-357; Coverage: 10%)
  • Canonical: Q13315 (Residues: 3024-3056; Coverage: 1%)
Gene names: ATM, spg
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 89%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

2 citation in other articles

Impaired endoplasmic reticulum-mitochondrial signaling in ataxia-telangiectasia.
Yeo et al. (2021)
1 more

2 mentions without citation

A computational and structural analysis of germline and somatic variants affecting the DDR mechanism, and their impact on human diseases.
Magraner-Pardo et al. (2021)
1 more