PDBe 4bpx

X-ray diffraction
3.4Å resolution

Crystal structure of human primase in complex with the primase- binding motif of DNA polymerase alpha

Released:

Function and Biology Details

Reaction catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). 
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
DNA primase large subunit Chains: B, D
Molecule details ›
Chains: B, D
Length: 269 amino acids
Theoretical weight: 30.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49643 (Residues: 19-253; Coverage: 46%)
Gene names: PRIM2, PRIM2A

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 120.68Å b: 70.701Å c: 127.16Å
α: 90° β: 105.83° γ: 90°
R-values:
R R work R free
0.236 0.234 0.267
Expression system: Escherichia coli BL21(DE3)