› 2cxq

X-ray diffraction
1.5Å 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 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: 557 amino acids
Theoretical weight: 62.69 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06745 (Residues: 1-557; Coverage: 100%)
Gene names: Gpi, Gpi1
Sequence domains: Phosphoglucose isomerase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand S6P 2 x S6P
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21
Unit cell:
a: 69.871Å b: 115.838Å c: 73.098Å
α: 90° β: 101.66° γ: 90°
R-values:
R R work R free
0.174 0.172 0.195
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Anticancer agents that counteract tumor glycolysis.
Granchi et al. (2012)
4 more

1 mention without citation

Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
Anand et al. (2010)