PDBe 4rh3

X-ray diffraction
3.02Å resolution

AMPPCP-bound structure of human platelet phosphofructokinase in an R-state, crystal form II

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase, platelet type Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 743 amino acids
Theoretical weight: 81.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01813 (Residues: 26-762; Coverage: 94%)
Gene names: PFKF, PFKP
Sequence domains: Phosphofructokinase
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P3221
Unit cell:
a: 132.911Å b: 132.911Å c: 397.168Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.148 0.146 0.187
Expression system: Escherichia coli