› 6kza

X-ray diffraction
3.1Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142255 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Replicative DNA helicase Chains: A, B
Molecule details ›
Chains: A, B
Length: 292 amino acids
Theoretical weight: 32.68 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ACB0 (Residues: 180-471; Coverage: 62%)
Gene names: JW4012, b4052, dnaB, groP, grpA
Sequence domains: DnaB-like helicase C terminal domain
DNA replication protein DnaC Chains: C, D
Molecule details ›
Chains: C, D
Length: 56 amino acids
Theoretical weight: 6.51 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEF0 (Residues: 1-56; Coverage: 23%)
Gene names: JW4325, b4361, dnaC, dnaD

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P42212
Unit cell:
a: 121.56Å b: 121.56Å c: 105.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.232 0.267
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Convergent evolution in two bacterial replicative helicase loaders.
Chase et al. (2022)
6 other articles

2 mentions without citation

Diverse Mechanisms of Helicase Loading during DNA Replication Initiation in Bacteria.
Blaine et al. (2023)
1 more