› 1kag

X-ray diffraction
2.05Å resolution

Crystal Structure of the Escherichia coli Shikimate Kinase I (AroK)

Released:
DOI: 10.2210/pdb1kag/pdb
PDB entry 1kag coloured by chain, front view.
PDB entry 1kag coloured by chain, side view.
PDB entry 1kag coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam.
Romanowski MJ, Burley SK
Proteins 47 558-62 (2002)
PMID: 12001235

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141301 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Shikimate kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 173 amino acids
Theoretical weight: 19.57 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A6D7 (Residues: 1-173; Coverage: 100%)
Gene names: JW5947, aroK, b3390
Sequence domains: Shikimate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A
Spacegroup: P21
Unit cell:
a: 35.726Å b: 63.417Å c: 67.941Å
α: 90° β: 91.27° γ: 90°
R-values:
R R work R free
0.222 0.217 0.271
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Anaerobic catabolism of aromatic compounds: a genetic and genomic view.
Carmona et al. (2009)
2 more

6 mentions without citation

Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS).
Hura et al. (2009)
5 more