1dde

X-ray diffraction
1.7Å resolution

STRUCTURE OF THE DNAG CATALYTIC CORE

Released:
Source organism: Escherichia coli
Primary publication:
Structure of the RNA polymerase domain of E. coli primase.
Science 287 2482-6 (2000)
PMID: 10741967

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA primase Chain: A
Molecule details ›
Chain: A
Length: 338 amino acids
Theoretical weight: 38.22 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABS5 (Residues: 111-433; Coverage: 56%)
Gene names: JW3038, b3066, dnaG, dnaP, parB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 38.02Å b: 55.89Å c: 139.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.263
Expression system: Escherichia coli