PDBe 4rr2

X-ray diffraction
2.65Å resolution

Crystal structure of human primase

Released:
Source organism: Homo sapiens
Primary publication:
Crystal Structure of the Human Primase.
J. Biol. Chem. (2014)
PMID: 25550159

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA primase small subunit Chains: A, C
Molecule details ›
Chains: A, C
Length: 420 amino acids
Theoretical weight: 49.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49642 (Residues: 1-420; Coverage: 100%)
Gene name: PRIM1
Sequence domains: DNA primase small subunit
Structure domains: DNA primase, PRIM domain
DNA primase large subunit Chains: B, D
Molecule details ›
Chains: B, D
Length: 509 amino acids
Theoretical weight: 58.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49643 (Residues: 1-509; Coverage: 100%)
Gene names: PRIM2, PRIM2A
Sequence domains: Eukaryotic and archaeal DNA primase, large subunit
Structure domains: Transcription Elongation Factor S-II; Chain A

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P1
Unit cell:
a: 86.195Å b: 88.899Å c: 94.682Å
α: 93.82° β: 96.57° γ: 111.72°
R-values:
R R work R free
0.229 0.229 0.271
Expression system: Escherichia coli BL21(DE3)