X-ray diffraction
1.7Å resolution

Structure of the E. coli ParC C-terminal domain

Source organism: Escherichia coli

Function and Biology Details

Reaction catalysed:
ATP-dependent breakage, passage and rejoining of double-stranded DNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
DNA topoisomerase 4 subunit A Chains: A, B
Molecule details ›
Chains: A, B
Length: 256 amino acids
Theoretical weight: 27.6 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
  • Canonical: P0AFI2 (Residues: 497-752; Coverage: 34%)
Gene names: JW2987, b3019, parC
Sequence domains: DNA gyrase C-terminal domain, beta-propeller

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P1
Unit cell:
a: 40.908Å b: 50.494Å c: 72.759Å
α: 86.11° β: 86.9° γ: 70.57°
R R work R free
0.185 0.184 0.215
Expression system: Escherichia coli BL21