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:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
DNA repair protein XRCC1 and DNA polymerase beta (preferred)
PDBe Complex ID:
PDB-CPX-139218 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA repair protein XRCC1
Molecule details ›
Chains: B, C
Length: 189 amino acids
Theoretical weight: 21.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: XRCC1 N terminal domain
Structure domains: Galactose-binding domain-like
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%)
Sequence domains: XRCC1 N terminal domain
Structure domains: Galactose-binding domain-like
DNA polymerase beta
Molecule details ›
Chains: D, E
Length: 252 amino acids
Theoretical weight: 29.34 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 252 amino acids
Theoretical weight: 29.34 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
- Canonical: P06766 (Residues: 91-335; Coverage: 73%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU MICROMAX-007 HF
Spacegroup:
C2
Expression system: Escherichia coli
