› 1q9d

X-ray diffraction
2.35Å resolution

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

Released:
DOI: 10.2210/pdb1q9d/pdb
PDB entry 1q9d coloured by chain, front view.
PDB entry 1q9d coloured by chain, side view.
PDB entry 1q9d coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric effectors.
Choe JY, Nelson SW, Arienti KL, Axe FU, Collins TL, Jones TK, Kimmich RD, Newman MJ, Norvell K, Ripka WC, Romano SJ, Short KM, Slee DH, Fromm HJ, Honzatko RB
J Biol Chem 278 51176-83 (2003)
PMID: 14530289

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

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-132777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 36.69 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P00636 (Residues: 2-338; Coverage: 100%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand F6P 2 x F6P
Ligand MG 4 x MG
Ligand PO4 4 x PO4
Ligand OI1 2 x OI1
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 58.86Å b: 166.25Å c: 80.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.191 0.246
Expression system: Escherichia coli

Quick links

Citations

4 review citations

New hepatic targets for glycaemic control in diabetes.
Agius L. (2007)
3 more

1 mention without citation

YWHA/14-3-3 proteins recognize phosphorylated TFEB by a noncanonical mode for controlling TFEB cytoplasmic localization.
Xu et al. (2019)