3t2b

X-ray diffraction
1.52Å resolution

Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, ligand free

Released:

Function and Biology Details

Reactions catalysed:
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphate aldolase/phosphatase Chain: A
Molecule details ›
Chain: A
Length: 407 amino acids
Theoretical weight: 45.46 KDa
Source organism: Pyrobaculum neutrophilum V24Sta
Expression system: Escherichia coli
UniProt:
  • Canonical: B1YAL1 (Residues: 1-399; Coverage: 100%)
Gene names: Tneu_0133, fbp
Sequence domains: Fructose-1,6-bisphosphatase
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I422
Unit cell:
a: 112.532Å b: 112.532Å c: 151.126Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.188
Expression system: Escherichia coli