› 2htf

Solution NMR

The solution structure of the BRCT domain from human polymerase reveals homology with the TdT BRCT domain

Released:
DOI: 10.2210/pdb2htf/pdb
PDB entry 2htf coloured by chain, ensemble of 11 models, front view.
PDB entry 2htf coloured by chain, ensemble of 11 models, side view.
PDB entry 2htf coloured by chain, ensemble of 11 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of polymerase mu's BRCT Domain reveals an element essential for its role in nonhomologous end joining.
DeRose EF, Clarkson MW, Gilmore SA, Galban CJ, Tripathy A, Havener JM, Mueller GA, Ramsden DA, London RE, Lee AL
Biochemistry 46 12100-10 (2007)
PMID: 17915942

Function and Biology Details

Reaction catalysed: 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA-directed DNA/RNA polymerase mu Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NP87 (Residues: 21-124; Coverage: 21%)
Gene names: POLM, polmu
Structure domains: BRCT domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Torsion angle dynamics followed by molecular dynamics refinement in explicit water solvent
Expression system: Escherichia coli

Quick links

Citations

6 review citations

One ring to bring them all--the role of Ku in mammalian non-homologous end joining.
Grundy et al. (2014)
5 more

5 mentions without citation

Repair of double-strand breaks by end joining.
Chiruvella et al. (2013)
4 more