5exr

X-ray diffraction
3.6Å resolution

Crystal structure of human primosome

Released:
Source organism: Homo sapiens

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-140801 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
DNA primase small subunit Chains: A, E
Molecule details ›
Chains: A, E
Length: 420 amino acids
Theoretical weight: 49.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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, F
Molecule details ›
Chains: B, F
Length: 509 amino acids
Theoretical weight: 58.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49643 (Residues: 1-509; Coverage: 100%)
Gene names: PRIM2, PRIM2A
Sequence domains: Eukaryotic and archaeal DNA primase, large subunit
DNA polymerase alpha catalytic subunit Chains: C, G
Molecule details ›
Chains: C, G
Length: 1128 amino acids
Theoretical weight: 129.31 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P09884 (Residues: 335-1462; Coverage: 77%)
Gene names: POLA, POLA1
Sequence domains:
DNA polymerase alpha subunit B Chains: D, H
Molecule details ›
Chains: D, H
Length: 597 amino acids
Theoretical weight: 65.88 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q14181 (Residues: 2-598; Coverage: 100%)
Gene name: POLA2
Sequence domains:

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: P21
Unit cell:
a: 113.096Å b: 210.164Å c: 172.565Å
α: 90° β: 93.56° γ: 90°
R-values:
R R work R free
0.268 0.268 0.326
Expression systems:
  • Escherichia coli
  • Spodoptera frugiperda