PDBe 4lik

X-ray diffraction
1.7Å resolution

Crystal structure of the catalytic subunit of human primase

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA primase small subunit Chain: A
Molecule details ›
Chain: A
Length: 392 amino acids
Theoretical weight: 46.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49642 (Residues: 1-408; Coverage: 92%)
Gene name: PRIM1
Sequence domains: DNA primase small subunit
Structure domains: DNA primase, PRIM domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2
Unit cell:
a: 101.812Å b: 71.916Å c: 84.797Å
α: 90° β: 122.04° γ: 90°
R-values:
R R work R free
0.176 0.175 0.198
Expression system: Escherichia coli