› 1via

X-ray diffraction
1.57Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + shikimate = ADP + shikimate 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Shikimate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 175 amino acids
Theoretical weight: 20.51 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0PBC3 (Residues: 4-165; Coverage: 98%)
Gene names: Cj0387, aroK
Sequence domains: Shikimate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P1
Unit cell:
a: 41.931Å b: 43.23Å c: 52.606Å
α: 81.51° β: 76.58° γ: 77.87°
R-values:
R R work R free
0.198 0.198 0.228
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more

2 mentions without citation

Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase.
Cheng et al. (2005)
1 more