› 6xuh

X-ray diffraction
2.38Å 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-139198 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-6-phosphate isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 556 amino acids
Theoretical weight: 62.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06744 (Residues: 2-557; Coverage: 100%)
Gene name: GPI
Sequence domains: Phosphoglucose isomerase

Ligands and Environments

2 bound ligands:
Ligand PA5 2 x PA5
Ligand O1B 2 x O1B
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P43
Unit cell:
a: 96.11Å b: 96.11Å c: 271.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.266 0.263 0.317
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications.
Enríquez-Flores et al. (2023)
4 other articles

1 mention without citation

β-Boswellic Acid Suppresses Breast Precancerous Lesions via GLUT1 Targeting-Mediated Glycolysis Inhibition and AMPK Pathway Activation.
Bie et al. (2022)