PDBe 1q57

X-ray diffraction
3.45Å resolution

The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7

Released:

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA primase/helicase Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 503 amino acids
Theoretical weight: 55.86 KDa
Source organism: Enterobacteria phage T7
Expression system: Escherichia coli
UniProt:
  • Canonical: P03692 (Residues: 64-566; Coverage: 89%)
Gene name: 4
Sequence domains: DnaB-like helicase C terminal domain
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 117.179Å b: 171.567Å c: 118.581Å
α: 90° β: 99.86° γ: 90°
R-values:
R R work R free
0.301 0.299 0.326
Expression system: Escherichia coli