PDBe 4omt

X-ray diffraction
6Å resolution

Crystal structure of human muscle phosphofructokinase (dissociated homodimer)

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase, muscle type Chain: A
Molecule details ›
Chain: A
Length: 780 amino acids
Theoretical weight: 85.29 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P08237 (Residues: 1-780; Coverage: 100%)
Gene names: PFKM, PFKX
Sequence domains: Phosphofructokinase

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6222
Unit cell:
a: 229.7Å b: 229.7Å c: 133Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.242 0.238 0.274
Expression system: Saccharomyces cerevisiae