PDBe 4bpu

X-ray diffraction
2.7Å resolution

Crystal structure of human primase in heterodimeric form, comprising PriS and truncated PriL lacking the C-terminal Fe-S domain.

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA primase large subunit Chains: B, D
Molecule details ›
Chains: B, D
Length: 253 amino acids
Theoretical weight: 29.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49643 (Residues: 1-253; Coverage: 50%)
Gene names: PRIM2, PRIM2A
DNA primase small subunit Chains: A, C
Molecule details ›
Chains: A, C
Length: 423 amino acids
Theoretical weight: 50.11 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

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 114.55Å b: 68.64Å c: 126.76Å
α: 90° β: 104.36° γ: 90°
R-values:
R R work R free
0.205 0.203 0.245
Expression system: Escherichia coli BL21(DE3)