› 4lik

X-ray diffraction
1.7Å resolution

Crystal structure of the catalytic subunit of human primase

Released:
DOI: 10.2210/pdb4lik/pdb
PDB entry 4lik coloured by chain, front view.
PDB entry 4lik coloured by chain, side view.
PDB entry 4lik coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Insights into eukaryotic primer synthesis from structures of the p48 subunit of human DNA primase.
Vaithiyalingam S, Arnett DR, Aggarwal A, Eichman BF, Fanning E, Chazin WJ
J Mol Biol 426 558-69 (2014)
PMID: 24239947

Function and Biology Details

Reaction catalysed: 
SsDNA + n NTP = ssDNA/pppN(pN)(n-1) hybrid + (n-1) diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155973 (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:
Ligand ZN 1 x ZN
Ligand CIT 3 x CIT
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

Quick links

Citations

4 review citations

Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes.
Guilliam et al. (2015)
3 more

2 mentions without citation

Elaborated Action of the Human Primosome.
Baranovskiy et al. (2017)
1 more