› 2r8t

X-ray diffraction
2.3Å resolution

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

Released:
DOI: 10.2210/pdb2r8t/pdb
PDB entry 2r8t coloured by chain, front view.
PDB entry 2r8t coloured by chain, side view.
PDB entry 2r8t coloured by chain, top view.
Source organism: Escherichia coli
Entry authors: Lunin VV, Skarina T, Brown G, Yakunin A, Edwards AM, Savchenko A

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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
Expression system: Escherichia coli BL21
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:
Ligand FBP 1 x FBP
Ligand UNX 3 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P422
Unit cell:
a: 91.596Å b: 91.596Å c: 85.385Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.185 0.254
Expression system: Escherichia coli BL21

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