› 1bxk

X-ray diffraction
1.9Å resolution

DTDP-GLUCOSE 4,6-DEHYDRATASE FROM E. COLI

Released:
DOI: 10.2210/pdb1bxk/pdb
PDB entry 1bxk coloured by chain, front view.
PDB entry 1bxk coloured by chain, side view.
PDB entry 1bxk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Molecular Structure of Dtdp-Glucose 4,6-Dehydratase from E. Coli
Thoden JB, Hegeman AD, Frey PA, Holden HM
To be published

Function and Biology Details

Reaction catalysed: 
dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + 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-151084 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dTDP-glucose 4,6-dehydratase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 355 amino acids
Theoretical weight: 39.7 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P27830 (Residues: 1-355; Coverage: 100%)
Gene names: JW5598, b3788, rffG
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 68.4Å b: 109.2Å c: 128.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 not available
Expression system: Escherichia coli

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