› 5ajv

X-ray diffraction
3.01Å 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: B
Molecule details ›
Chain: B
Length: 520 amino acids
Theoretical weight: 59.69 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

3 bound ligands:
Ligand PO4 3 x PO4
Ligand 8R2 1 x 8R2
Ligand FDP 1 x FDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND
Spacegroup: P6522
Unit cell:
a: 102.63Å b: 102.63Å c: 258.21Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.182 0.225
Expression system: Escherichia coli BL21

Quick links

Citations

15 review citations

Endothelial Cell Metabolism.
Eelen et al. (2018)
14 more