8du1

X-ray diffraction
1.85Å resolution

Crystal Structure of NAD bound dTDP-glucose 4,6-dehydratase from Elizabethkingia anophelis

Released:
Entry authors: Seattle Structural Genomics Center for Infectious Disease, Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-100520 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dTDP-glucose 4,6-dehydratase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 367 amino acids
Theoretical weight: 42 KDa
Source organism: Elizabethkingia anophelis NUHP1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A077ELH2 (Residues: 1-359; Coverage: 100%)
Gene name: BD94_3274
Sequence domains: GDP-mannose 4,6 dehydratase

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 66.74Å b: 84.62Å c: 130.87Å
α: 90° β: 101.18° γ: 90°
R-values:
R R work R free
0.156 0.156 0.195
Expression system: Escherichia coli BL21(DE3)