X-ray diffraction
1.39Å resolution

Crystal structure of eukaryotic DNA primase large subunit iron-sulfur cluster domain

Primary publication:
Yeast require redox switching in DNA primase.
Proc Natl Acad Sci U S A 115 13186-13191 (2018)
PMID: 30541886

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
DNA primase large subunit Chain: A
Molecule details ›
Chain: A
Length: 201 amino acids
Theoretical weight: 23.36 KDa
Source organism: Saccharomyces cerevisiae JAY291
Expression system: Escherichia coli
  • Canonical: C7GP29 (Residues: 316-512; Coverage: 37%)
Gene names: C1Q_02024, PRI2
Sequence domains: Eukaryotic and archaeal DNA primase, large subunit

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 41.085Å b: 50.769Å c: 89.832Å
α: 90° β: 90° γ: 90°
R R work R free
0.126 0.124 0.146
Expression system: Escherichia coli