› 6etj

X-ray diffraction
2.51Å resolution

Function and Biology Details

Reactions catalysed: 
ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
Beta-D-fructose 2,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Chain: A
Molecule details ›
Chain: A
Length: 520 amino acids
Theoretical weight: 59.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q16875 (Residues: 1-520; Coverage: 100%)
Gene name: PFKFB3
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand DMS 1 x DMS
Ligand F6P 1 x F6P
Ligand BWW 1 x BWW
Ligand ADP 1 x ADP
1 modified residue:
Ligand NEP 1 x NEP

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6522
Unit cell:
a: 103.774Å b: 103.774Å c: 259.563Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.192 0.235
Expression system: Escherichia coli BL21

Quick links

Citations

16 review citations

Treatment against glucose-dependent cancers through metabolic PFKFB3 targeting of glycolytic flux.
Jones et al. (2022)
15 more

1 mention without citation

Targeting PFKFB3 radiosensitizes cancer cells and suppresses homologous recombination.
Gustafsson et al. (2018)