› 2bif

X-ray diffraction
2.4Å resolution

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

Released:
DOI: 10.2210/pdb2bif/pdb
PDB entry 2bif coloured by chain, front view.
PDB entry 2bif coloured by chain, side view.
PDB entry 2bif coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities.
Yuen MH, Mizuguchi H, Lee YH, Cook PF, Uyeda K, Hasemann CA
J Biol Chem 274 2176-84 (1999)
PMID: 9890980

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 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

6 bound ligands:
Ligand BOG 3 x BOG
Ligand F6P 2 x F6P
Ligand MG 1 x MG
Ligand PO4 3 x PO4
Ligand ANP 1 x ANP
Ligand SIN 2 x SIN
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

Quick links

Citations

3 review citations

Enzyme catalysis: removing chemically 'essential' residues by site-directed mutagenesis.
Peracchi A. (2001)
2 more

7 mentions without citation

Role of PFKFB3 and PFKFB4 in Cancer: Genetic Basis, Impact on Disease Development/Progression, and Potential as Therapeutic Targets.
Kotowski et al. (2021)
6 more