PDBe 1kzh

X-ray diffraction
2.55Å resolution

Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi

Released:

Function and Biology Details

Reaction catalysed:
Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6- bisphosphate. 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 555 amino acids
Theoretical weight: 62.55 KDa
Source organism: Borreliella burgdorferi
Expression system: Escherichia coli
UniProt:
  • Canonical: P70826 (Residues: 1-555; Coverage: 100%)
Gene names: BB_0020, PFK2, pfp, pfpB
Sequence domains: Phosphofructokinase
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200HB
Spacegroup: P212121
Unit cell:
a: 85.098Å b: 97.926Å c: 148.173Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.243
Expression system: Escherichia coli