› 2aq0

Solution NMR

Solution structure of the human homodimeric dna repair protein XPF

Released:
DOI: 10.2210/pdb2aq0/pdb
PDB entry 2aq0 coloured by chain, ensemble of 20 models, front view.
PDB entry 2aq0 coloured by chain, ensemble of 20 models, side view.
PDB entry 2aq0 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The HhH domain of the human DNA repair protein XPF forms stable homodimers.
Das D, Tripsianes K, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R, Folkers GE
Proteins 70 1551-63 (2008)
PMID: 17912758

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187800 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA repair endonuclease XPF Chains: A, B
Molecule details ›
Chains: A, B
Length: 84 amino acids
Theoretical weight: 9.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92889 (Residues: 834-916; Coverage: 9%)
Gene names: ERCC11, ERCC4, XPF
Structure domains: 5' to 3' exonuclease, C-terminal subdomain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics; simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

DNA repair endonuclease ERCC1-XPF as a novel therapeutic target to overcome chemoresistance in cancer therapy.
McNeil et al. (2012)
13 other articles

3 mentions without citation

DNA repair gets physical: mapping an XPA-binding site on ERCC1.
Croteau et al. (2008)
2 more