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› 1sg6

X-ray diffraction
1.7Å resolution

Crystal structure of Aspergillus nidulans 3-dehydroquinate synthase (AnDHQS) in complex with Zn2+ and NAD+, at 1.7D

Released:
DOI: 10.2210/pdb1sg6/pdb
Model geometry
Fit model/data
PDB entry 1sg6 coloured by chain, front view.
PDB entry 1sg6 coloured by chain, side view.
PDB entry 1sg6 coloured by chain, top view.
Source organism: Aspergillus nidulans
Primary publication:
Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover.
Nichols CE, Hawkins AR, Stammers DK
Acta Crystallogr D Biol Crystallogr 60 971-3 (2004)
PMID: 15103156

Function and Biology Details

Reactions catalysed: 
shikimate + NADP(+) = 3-dehydroshikimate + NADPH + H(+).
3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate.
shikimate + ATP = 3-phosphoshikimate + ADP + H(+).
3-dehydroquinate = 3-dehydroshikimate + H2O.
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate +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-139611 (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 N-terminal
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 90.02Å b: 104.51Å c: 177.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.195 0.25
Expression system: Escherichia coli

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Citations

2 citation in other articles

Comparison of ligand-induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases.
Nichols et al. (2004)
1 more

6 mentions without citation

Evaluating the potency of HIV-1 protease drugs to combat resistance.
Hou et al. (2008)
5 more