› 1db3

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142250 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GDP-mannose 4,6-dehydratase Chain: A
Molecule details ›
Chain: A
Length: 372 amino acids
Theoretical weight: 41.97 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AC88 (Residues: 2-373; Coverage: 100%)
Gene names: JW2038, b2053, gmd, yefA, yefN
Sequence domains: GDP-mannose 4,6 dehydratase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P6322
Unit cell:
a: 149.6Å b: 149.6Å c: 102.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.205 0.232
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Fucose: biosynthesis and biological function in mammals.
Becker et al. (2003)
8 more

7 mentions without citation

Prediction of catalytic residues using Support Vector Machine with selected protein sequence and structural properties.
Petrova et al. (2006)
6 more