› 4lil

X-ray diffraction
2.6Å resolution

Crystal structure of the catalytic subunit of human primase bound to UTP and Mn

Released:
DOI: 10.2210/pdb4lil/pdb
PDB entry 4lil coloured by chain, front view.
PDB entry 4lil coloured by chain, side view.
PDB entry 4lil 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

3 bound ligands:
Ligand ZN 1 x ZN
Ligand MN 2 x MN
Ligand UTP 1 x UTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P43212
Unit cell:
a: 79.346Å b: 79.346Å c: 148.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.214 0.248
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

3 mentions without citation

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