PDBe 2bif

X-ray diffraction
2.4Å resolution

6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE H256A MUTANT WITH F6P IN PHOSPHATASE ACTIVE SITE

Released:

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:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 469 amino acids
Theoretical weight: 54 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P25114 (Residues: 1-469; Coverage: 100%)
Gene name: Pfkfb4
Sequence domains:
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 61.74Å b: 73.51Å c: 76.7Å
α: 116.9° β: 99.31° γ: 105.2°
R-values:
R R work R free
0.2 0.2 0.244
Expression system: Escherichia coli