3lqc

X-ray diffraction
2.35Å resolution

X-ray crystal structure of oxidized XRCC1 bound to DNA pol beta Palm thumb domain

Released:
Source organisms:
Primary publication:
Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity.
Proc Natl Acad Sci U S A 107 6805-10 (2010)
PMID: 20351257

Function and Biology Details

Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-139218 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA repair protein XRCC1 Chain: A
Molecule details ›
Chain: A
Length: 189 amino acids
Theoretical weight: 21.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18887 (Residues: 1-183; Coverage: 29%)
Gene name: XRCC1
Sequence domains: XRCC1 N terminal domain
Structure domains: Galactose-binding domain-like
DNA polymerase beta Chain: B
Molecule details ›
Chain: B
Length: 200 amino acids
Theoretical weight: 23.52 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06766 (Residues: 142-335; Coverage: 58%)
Gene name: Polb
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P3121
Unit cell:
a: 75.24Å b: 75.24Å c: 126.16Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.189 0.25
Expression system: Escherichia coli