1dpu

Solution NMR

SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88)

Released:

Function and Biology Details

Reaction catalysed:
Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
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):
Replication protein A 32 kDa subunit Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15927 (Residues: 172-270; Coverage: 37%)
Gene names: REPA2, RPA2, RPA32, RPA34
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Uracil-DNA glycosylase Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.83 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P13051 (Residues: 73-88; Coverage: 5%)
Gene names: DGU, UNG, UNG1, UNG15

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY SIMULATED ANNEALING
Expression systems:
  • Escherichia coli
  • Not provided