› 3t2d

X-ray diffraction
1.36Å resolution

Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, FBP-bound form

Released:
DOI: 10.2210/pdb3t2d/pdb
PDB 3t2d coloured by chain and viewed from the front.
PDB 3t2d coloured by chain and viewed from the side.
PDB 3t2d coloured by chain and viewed from the top.
Source organism: Pyrobaculum neutrophilum V24Sta
Primary publication:
Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase.
Du J, Say RF, Lü W, Fuchs G, Einsle O
Nature 478 534-7 (2011)
PMID: 21983965

Function and Biology Details

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

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
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand P6F 1 x P6F
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I422
Unit cell:
a: 112.291Å b: 112.291Å c: 151.348Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.105 0.104 0.126
Expression system: Escherichia coli

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Citations

5 review citations

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

1 mention without citation

Why study moonlighting proteins?
Jeffery CJ. (2015)