› 1zuh

X-ray diffraction
1.8Å resolution

Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase

Released:
DOI: 10.2210/pdb1zuh/pdb
PDB entry 1zuh coloured by chain, front view.
PDB entry 1zuh coloured by chain, side view.
PDB entry 1zuh coloured by chain, top view.
Source organism: Helicobacter pylori 26695
Primary publication:
Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase.
Cheng WC, Chang YN, Wang WC
J Bacteriol 187 8156-63 (2005)
PMID: 16291688

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Shikimate kinase Chain: A
Molecule details ›
Chain: A
Length: 168 amino acids
Theoretical weight: 19.27 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli
UniProt:
  • Canonical: P56073 (Residues: 1-162; Coverage: 100%)
Gene names: HP_0157, aroK
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: SPRING-8 BEAMLINE BL12B2
Spacegroup: P42212
Unit cell:
a: 94.494Å b: 94.494Å c: 39.299Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.21 0.266
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural biology and drug discovery of difficult targets: the limits of ligandability.
Surade et al. (2012)
1 more

5 mentions without citation

Dynamic allostery can drive cold adaptation in enzymes.
Saavedra et al. (2018)
4 more