5yl5

X-ray diffraction
1.9Å resolution

Crystal structure of dodecameric Dehydroquinate dehydratase from Acinetobacter baumannii at 1.9A resolution

Released:
Entry authors: Iqbal N, Kaur P, Sharma S, Singh TP

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-107170 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-dehydroquinate dehydratase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 151 amino acids
Theoretical weight: 16.52 KDa
Source organism: Acinetobacter baumannii ATCC 17978
Expression system: Escherichia coli
UniProt:
  • Canonical: A3M692 (Residues: 1-151; Coverage: 100%)
Gene names: A1S_2009, aroQ
Sequence domains: Dehydroquinase class II
Structure domains: Dehydroquinase, class II

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 81.796Å b: 155.129Å c: 155.465Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.218
Expression system: Escherichia coli