1ni9

X-ray diffraction
2Å resolution

2.0 A structure of glycerol metabolism protein from E. coli

Released:

Function and Biology Details

Reaction catalysed:
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-141867 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 class 2 Chain: A
Molecule details ›
Chain: A
Length: 338 amino acids
Theoretical weight: 36.09 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9C9 (Residues: 1-336; Coverage: 100%)
Gene names: JW3896, b3925, glpX
Sequence domains: Bacterial fructose-1,6-bisphosphatase, glpX-encoded
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P41212
Unit cell:
a: 61.453Å b: 61.453Å c: 171.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.244
Expression system: Escherichia coli