› 1fj9

X-ray diffraction
2.5Å resolution

FRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCTS/ZN/AMP COMPLEX (T-STATE)

Released:
DOI: 10.2210/pdb1fj9/pdb
PDB entry 1fj9 coloured by chain, front view.
PDB entry 1fj9 coloured by chain, side view.
PDB entry 1fj9 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Tryptophan fluorescence reveals the conformational state of a dynamic loop in recombinant porcine fructose-1,6-bisphosphatase.
Nelson SW, Iancu CV, Choe JY, Honzatko RB, Fromm HJ
Biochemistry 39 11100-6 (2000)
PMID: 10998248

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: 36.71 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 ZN 4 x ZN
Ligand PO4 2 x PO4
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P21212
Unit cell:
a: 59.82Å b: 165.48Å c: 79.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.258
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The role of dynamics in allosteric regulation.
Kern et al. (2003)
2 more

1 mention without citation

Recovering a representative conformational ensemble from underdetermined macromolecular structural data.
Berlin et al. (2013)