3big

X-ray diffraction
1.85Å resolution

Crystal structure of the fructose-1,6-bisphosphatase GlpX from E.coli in complex with inorganic phosphate

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: 36.05 KDa
Source organism: Escherichia coli K-12
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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P422
Unit cell:
a: 91.348Å b: 91.348Å c: 86.366Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.239
Expression system: Escherichia coli