› 1fpg

X-ray diffraction
2.3Å resolution

STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY

Released:
DOI: 10.2210/pdb1fpg/pdb
PDB entry 1fpg coloured by chain, front view.
PDB entry 1fpg coloured by chain, side view.
PDB entry 1fpg coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography.
Villeret V, Huang S, Zhang Y, Lipscomb WN
Biochemistry 34 4307-15 (1995)
PMID: 7703244

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132778 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 335 amino acids
Theoretical weight: 36.5 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00636 (Residues: 2-336; Coverage: 99%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MN 4 x MN
Ligand AHG 2 x AHG
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 61.1Å b: 166.5Å c: 80Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 not available
Expression system: Not provided

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Citations

3 review citations

Design and synthesis of carbohydrate-based inhibitors of protein-carbohydrate interactions.
von Itzstein et al. (1996)
2 more