› 6pfk

X-ray diffraction
2.6Å resolution

PHOSPHOFRUCTOKINASE, INHIBITED T-STATE

Released:
DOI: 10.2210/pdb6pfk/pdb
Model geometry
Fit model/data
PDB entry 6pfk coloured by chain, front view.
PDB entry 6pfk coloured by chain, side view.
PDB entry 6pfk coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Structural basis of the allosteric behaviour of phosphofructokinase.
Schirmer T, Evans PR
Nature 343 140-5 (1990)
PMID: 2136935

Function and Biology Details

Reaction catalysed: 
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132577 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 319 amino acids
Theoretical weight: 34.17 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00512 (Residues: 1-319; Coverage: 100%)
Gene names: pfk, pfkA
Sequence domains: Phosphofructokinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PGA 4 x PGA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P212121
Unit cell:
a: 132Å b: 115.2Å c: 96.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.255
Expression system: Escherichia coli

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Citations

27 review citations

Molecular biology of prion diseases.
Prusiner SB. (1991)
26 more

19 mentions without citation

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
18 more