PDBe 3clh

X-ray diffraction
2.4Å resolution

Crystal structure of 3-dehydroquinate synthase (DHQS)from Helicobacter pylori

Released:
Source organism: Helicobacter pylori
Primary publication:
Structure-based inhibitor discovery of Helicobacter pylori dehydroquinate synthase.
Biochem. Biophys. Res. Commun. 373 1-7 (2008)
PMID: 18503755

Function and Biology Details

Reaction catalysed:
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-dehydroquinate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 343 amino acids
Theoretical weight: 39.18 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: P56081 (Residues: 1-343; Coverage: 100%)
Gene names: HP_0283, aroB
Sequence domains: 3-dehydroquinate synthase
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: R3
Unit cell:
a: 158.294Å b: 158.294Å c: 97.387Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.207 0.258
Expression system: Escherichia coli