Function and Biology Details
Reaction catalysed:
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Three-prime repair exonuclease 1 and DNA (preferred)
PDBe Complex ID:
PDB-CPX-115700 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Three-prime repair exonuclease 1
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 27.11 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
Length: 247 amino acids
Theoretical weight: 27.11 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q91XB0 (Residues: 9-245; Coverage: 76%)
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-3
Spacegroup:
P43212
Expression systems:
- Escherichia coli BL21
- Not provided
