1nr5

X-ray diffraction
2.1Å resolution

Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, NAD and carbaphosphonate

Released:

Function and Biology Details

Reactions catalysed:
3-dehydroquinate = 3-dehydroshikimate + H(2)O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate
Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
ATP + shikimate = ADP + shikimate 3-phosphate
Shikimate + NADP(+) = 3-dehydroshikimate + NADPH
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pentafunctional AROM polypeptide Chains: A, B
Molecule details ›
Chains: A, B
Length: 393 amino acids
Theoretical weight: 42.97 KDa
Source organism: Aspergillus nidulans
Expression system: Escherichia coli
UniProt:
  • Canonical: P07547 (Residues: 1-393; Coverage: 25%)
Gene names: AN0708, aroA, aroM, aromA
Sequence domains: 3-dehydroquinate synthase
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 133.99Å b: 86.56Å c: 74.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.185 0.232
Expression system: Escherichia coli