› 1kz8

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF PORCINE FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH A NOVEL ALLOSTERIC-SITE INHIBITOR

Released:
DOI: 10.2210/pdb1kz8/pdb
PDB entry 1kz8 coloured by chain, front view.
PDB entry 1kz8 coloured by chain, side view.
PDB entry 1kz8 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Anilinoquinazoline inhibitors of fructose 1,6-bisphosphatase bind at a novel allosteric site: synthesis, in vitro characterization, and X-ray crystallography.
Wright SW, Carlo AA, Carty MD, Danley DE, Hageman DL, Karam GA, Levy CB, Mansour MN, Mathiowetz AM, McClure LD, Nestor NB, McPherson RK, Pandit J, Pustilnik LR, Schulte GK, Soeller WC, Treadway JL, Wang IK, Bauer PH
J Med Chem 45 3865-77 (2002)
PMID: 12190310

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, F
Molecule details ›
Chains: A, F
Length: 337 amino acids
Theoretical weight: 36.7 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 MN 2 x MN
Ligand AMP 2 x AMP
Ligand PFE 2 x PFE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21212
Unit cell:
a: 59.65Å b: 165.94Å c: 79.223Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.214
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Implications of protein flexibility for drug discovery.
Teague SJ. (2003)
2 more

5 mentions without citation

Reversing allosteric communication: From detecting allosteric sites to inducing and tuning targeted allosteric response.
Tee et al. (2018)
4 more