› 1qfe

X-ray diffraction
2.1Å resolution

THE STRUCTURE OF TYPE I 3-DEHYDROQUINATE DEHYDRATASE FROM SALMONELLA TYPHI

Released:
DOI: 10.2210/pdb1qfe/pdb
PDB entry 1qfe coloured by chain, front view.
PDB entry 1qfe coloured by chain, side view.
PDB entry 1qfe coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhi
Primary publication:
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction.
Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L
Nat Struct Biol 6 521-5 (1999)
PMID: 10360352

Function and Biology Details

Reaction catalysed: 
3-dehydroquinate = 3-dehydroshikimate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150271 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-dehydroquinate dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 27.65 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhi
UniProt:
  • Canonical: P24670 (Residues: 1-252; Coverage: 100%)
Gene names: STY1760, aroD, t1231
Sequence domains: Type I 3-dehydroquinase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand DHS 2 x DHS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21
Unit cell:
a: 60.49Å b: 45.39Å c: 85.47Å
α: 90° β: 95.48° γ: 90°
R-values:
R R work R free
0.199 0.199 0.247

Quick links

Citations

9 review citations

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

7 mentions without citation

Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.
Tabita et al. (2007)
6 more