› 1u0e

X-ray diffraction
1.6Å resolution

Function and Biology Details

Reaction catalysed: 
Alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
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-139199 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-6-phosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 564 amino acids
Theoretical weight: 63.64 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06745 (Residues: 1-558; Coverage: 100%)
Gene names: Gpi, Gpi1
Sequence domains: Phosphoglucose isomerase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SO4 10 x SO4
Ligand BME 5 x BME
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 69.2Å b: 116.1Å c: 73.1Å
α: 90° β: 101.3° γ: 90°
R-values:
R R work R free
0.213 0.211 0.246
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Anticancer agents that counteract tumor glycolysis.
Granchi et al. (2012)
24 other articles

2 mentions without citation

Oxidation Resistance 1 Modulates Glycolytic Pathways in the Cerebellum via an Interaction with Glucose-6-Phosphate Isomerase.
Finelli et al. (2019)
1 more