Human liver fructose-1,6-BISPHOSPHATASE(D-fructose-1,6-bisphosphate, 1-phosphohydrolase) (E.C.3.1.3.11) complexed with the allosteric inhibitor 3

Structure

x-ray diffraction · 3 distinct chains · 39% helix, 25% strand (DSSP).

Ligands and binding sites

• 2C1 · N-({4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl}carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide · ligand · 8 copies · chains A, C, B, D, E, G, F, H

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Interfaces

14 interfaces between chains.

• A–B · 2439 Ų buried · 29 hydrogen bonds · protein-protein
• G–H · 2434 Ų buried · 30 hydrogen bonds · protein-protein
• E–F · 2426 Ų buried · 31 hydrogen bonds · protein-protein
• C–D · 2420 Ų buried · 29 hydrogen bonds · protein-protein
• F–H · 1291 Ų buried · 28 hydrogen bonds · protein-protein

Compared structures

• 4MJO · Human liver fructose-1,6-bisphosphatase(d-fructose-1,6-bisphosphate, 1-phosphohydrolase)… · the same entry in another collection · chain H against H, TM-score 1.00
• P09467 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P09467) · a predicted model of the same protein · chain F 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 P09467
• Elsewhere: RCSB PDB 4MJO · PDBe 4MJO · UniProt P09467