2v1c

X-ray diffraction
3.8Å resolution

Crystal structure and mutational study of RecOR provide insight into its role in DNA repair

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-193314 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Recombination protein RecR Chains: A, B
Molecule details ›
Chains: A, B
Length: 220 amino acids
Theoretical weight: 23.75 KDa
Source organism: Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ZNA2 (Residues: 1-220; Coverage: 100%)
Gene names: DR_0198, recR
Sequence domains:
Structure domains:
DNA repair protein RecO Chain: C
Molecule details ›
Chain: C
Length: 244 amino acids
Theoretical weight: 26.38 KDa
Source organism: Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RW50 (Residues: 1-244; Coverage: 100%)
Gene names: DR_0819, recO
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2
Unit cell:
a: 144Å b: 83.2Å c: 66.6Å
α: 90° β: 106.9° γ: 90°
R-values:
R R work R free
0.458 0.459 0.443
Expression system: Escherichia coli BL21(DE3)