› 6h5g

X-ray diffraction
1.04Å resolution

Crystal structure of DHQ1 from Salmonella typhi covalently modified by ligand 3

Released:
DOI: 10.2210/pdb6h5g/pdb
PDB entry 6h5g coloured by chain, front view.
PDB entry 6h5g coloured by chain, side view.
PDB entry 6h5g coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhi
Primary publication:
Hydroxylammonium Derivatives for Selective Active-site Lysine Modification in the Anti-virulence Bacterial Target DHQ1 Enzyme.
Maneiro M, Lence E, Sanz-Gaitero M, Otero JM, van Raaij MJ, Thompson P, Hawkins AR, Gonzalez-Bello C
Org Chem Front 6 3127-3135 (2019)

Function and Biology Details

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

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 Chain: A
Molecule details ›
Chain: A
Length: 252 amino acids
Theoretical weight: 27.68 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhi
Expression system: Escherichia coli
UniProt:
  • Canonical: P24670 (Residues: 1-252; Coverage: 100%)
Gene names: STY1760, aroD, t1231
Sequence domains: Type I 3-dehydroquinase

Ligands and Environments

1 bound ligand:
Ligand FQZ 1 x FQZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P21212
Unit cell:
a: 46.726Å b: 114.632Å c: 42.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.125 0.124 0.144
Expression system: Escherichia coli

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