› 1bif

X-ray diffraction
2Å resolution

6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE BIFUNCTIONAL ENZYME COMPLEXED WITH ATP-G-S AND PHOSPHATE

Released:
DOI: 10.2210/pdb1bif/pdb
PDB entry 1bif coloured by chain, front view.
PDB entry 1bif coloured by chain, side view.
PDB entry 1bif coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies.
Hasemann CA, Istvan ES, Uyeda K, Deisenhofer J
Structure 4 1017-29 (1996)
PMID: 8805587

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 domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 Chain: A
Molecule details ›
Chain: A
Length: 469 amino acids
Theoretical weight: 54.07 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

4 bound ligands:
Ligand MG 1 x MG
Ligand PO4 2 x PO4
Ligand AGS 1 x AGS
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P3121
Unit cell:
a: 83Å b: 83Å c: 130.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.183 0.25
Expression system: Escherichia coli

Quick links

Citations

11 review citations

PFK-2/FBPase-2: maker and breaker of the essential biofactor fructose-2,6-bisphosphate.
Okar et al. (2001)
10 more

18 mentions without citation

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis.
Rider et al. (2004)
17 more