› 1rdz

X-ray diffraction
2.05Å resolution

T-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI

Released:
DOI: 10.2210/pdb1rdz/pdb
PDB entry 1rdz coloured by chain, front view.
PDB entry 1rdz coloured by chain, side view.
PDB entry 1rdz coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Crystal structures of the active site mutant (Arg-243-->Ala) in the T and R allosteric states of pig kidney fructose-1,6-bisphosphatase expressed in Escherichia coli.
Stec B, Abraham R, Giroux E, Kantrowitz ER
Protein Sci 5 1541-53 (1996)
PMID: 8844845

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, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 36.62 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

2 bound ligands:
Ligand F6P 2 x F6P
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21212
Unit cell:
a: 61.06Å b: 166.78Å c: 79.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.224
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Localization and regulation of muscle fructose-1,6-bisphosphatase, the key enzyme of glyconeogenesis.
Dzugaj A. (2006)
4 other articles

2 mentions without citation

A library of novel allosteric inhibitors against fructose 1,6-bisphosphatase.
Heng et al. (2009)
1 more