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

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).

Ligands and binding sites

• AHG · 2,5-anhydro-1,6-di-O-phosphono-D-glucitol · ligand · 2 copies · chains A, B
• AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
• MN · Manganese (II) ion · metal · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2296 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

• 1FPG · Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP… · the same entry in another collection · chain A against A, TM-score 1.00
• P00636 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P00636) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P00636
• Elsewhere: RCSB PDB 1FPG · PDBe 1FPG · UniProt P00636