Solution NMR

Solution structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase kappa

Source organism: Homo sapiens
Entry authors: Liu D, Ryu K, Ko J, Choi B

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:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA repair protein REV1 Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q9UBZ9 (Residues: 1156-1251; Coverage: 8%)
Gene names: REV1, REV1L
Sequence domains: DNA repair protein REV1 C-terminal domain
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
DNA polymerase kappa Chain: B
Molecule details ›
Chain: B
Length: 17 amino acids
Theoretical weight: 2.16 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: Q9UBT6 (Residues: 562-577; Coverage: 2%)
Gene names: DINB1, POLK

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: simulated annealing, explicit water refinement
Chemical shifts: BMR18432  
Expression systems:
  • Escherichia coli
  • Not provided