X-ray diffraction
2.45Å resolution

Structure of ParF-ADP form 2


Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
CobQ/CobB/MinD/ParA nucleotide binding domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 206 amino acids
Theoretical weight: 22.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: B0ZE06 (Residues: 1-206; Coverage: 100%)
Gene names: CG831_004316, DNQ45_07005, EIZ93_19540, HEP30_021835, pOLA52_52, parF
Sequence domains: CobQ/CobB/MinD/ParA nucleotide binding domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 54.65Å b: 80.23Å c: 67Å
α: 90° β: 112.64° γ: 90°
R R work R free
0.203 0.203 0.252
Expression system: Escherichia coli