5n8a

X-ray diffraction
1.28Å resolution

Structure of RPA70N in complex with PrimPol (fragment 480-560)

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA-directed primase/polymerase protein Chain: X
Molecule details ›
Chain: X
Length: 102 amino acids
Theoretical weight: 11.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96LW4 (Residues: 480-560; Coverage: 15%)
Gene names: CCDC111, PRIMPOL
Replication protein A 70 kDa DNA-binding subunit, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P27694 (Residues: 1-120; Coverage: 20%)
Gene names: REPA1, RPA1, RPA70
Sequence domains: Replication factor-A protein 1, N-terminal domain
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 38.05Å b: 53.49Å c: 53.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.154 0.178
Expression system: Escherichia coli BL21