› 1e7s

X-ray diffraction
1.5Å resolution

GDP 4-keto-6-deoxy-D-mannose epimerase reductase K140R

Released:
DOI: 10.2210/pdb1e7s/pdb
PDB entry 1e7s coloured by chain, front view.
PDB entry 1e7s coloured by chain, side view.
PDB entry 1e7s coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Probing the catalytic mechanism of GDP-4-keto-6-deoxy-d-mannose Epimerase/Reductase by kinetic and crystallographic characterization of site-specific mutants.
Rosano C, Bisso A, Izzo G, Tonetti M, Sturla L, De Flora A, Bolognesi M
J Mol Biol 303 77-91 (2000)
PMID: 11021971

Function and Biology Details

Reaction catalysed: 
GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + NADPH
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-152194 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GDP-L-fucose synthase Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 36.19 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P32055 (Residues: 1-321; Coverage: 100%)
Gene names: JW2037, b2052, fcl, wcaG, yefB
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
3 bound ligands:
Ligand UVW 1 x UVW
Ligand SO4 3 x SO4
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P3221
Unit cell:
a: 103.4Å b: 103.4Å c: 75.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.126 0.126 0.162
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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