3k77

X-ray diffraction
2.6Å resolution

X-ray crystal structure of XRCC1

Released:
Source organism: Homo sapiens
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

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148463 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA repair protein XRCC1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 161 amino acids
Theoretical weight: 17.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18887 (Residues: 1-155; Coverage: 25%)
Gene name: XRCC1
Sequence domains: XRCC1 N terminal domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 64.451Å b: 89.302Å c: 93.178Å
α: 90° β: 90.03° γ: 90°
R-values:
R R work R free
0.202 0.2 0.237
Expression system: Escherichia coli