› 2cvp

X-ray diffraction
1.8Å 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 ACT 1 x ACT
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 69.968Å b: 115.883Å c: 73.267Å
α: 90° β: 101.76° γ: 90°
R-values:
R R work R free
0.183 0.181 0.219
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

2 mentions without citation

The in vivo ISGylome links ISG15 to metabolic pathways and autophagy upon Listeria monocytogenes infection.
Zhang et al. (2019)
1 more