Fructose-1,6-bisphosphatase complexed with a new allosteric site inhibitor (I-state)

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Ligands and binding sites

• F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · 2 copies · chains A, B
• OI1 · 3-(4-hydroxybenzyl)-2-[1-({[2-(4-hydroxyphenyl)ethyl]amino}carbonyl)butyl]-4-oxo-3,6,11,11A-tetrahydro-4H-pyrazino[1,2-b]isoquinolin-2-ium-1-olate · ligand · 2 copies · chains A, B
• MG · Magnesium ion · metal · 4 copies · chains A, B
• PO4 · Phosphate ion · ion · 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, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2491 Ų buried · 41 hydrogen bonds · protein-protein

Compared structures

• 1Q9D · Fructose-1,6-bisphosphatase Complexed with a New Allosteric Site Inhibitor (I-State) · 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 0.94

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 1Q9D · PDBe 1Q9D · UniProt P00636