4ba9

X-ray diffraction
2.73Å resolution

The structural basis for the coordination of Y-family Translesion DNA Polymerases by Rev1

Released:
Source organism: Homo sapiens
Entry authors: Grummitt CG, Kilkenny ML, Frey A, Roe SM, Oliver AW, Sale JE, Pearl LH

Function and Biology Details

Reaction catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-193673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA polymerase kappa; DNA repair protein REV1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 114 amino acids
Theoretical weight: 13.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UBT6 (Residues: 563-575; Coverage: 2%)
  • Canonical: Q9UBZ9 (Residues: 1158-1242; Coverage: 7%)
Gene names: DINB1, POLK, REV1, REV1L
Sequence domains: DNA repair protein REV1 C-terminal domain
Structure domains: DNA repair protein Rev1, C-terminal domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: R32
Unit cell:
a: 105.75Å b: 105.75Å c: 424.27Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.214 0.25
Expression system: Escherichia coli BL21(DE3)