› 1cnq

X-ray diffraction
2.27Å resolution

FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE-6-PHOSPHATE AND ZINC IONS

Released:
DOI: 10.2210/pdb1cnq/pdb
PDB entry 1cnq coloured by chain, front view.
PDB entry 1cnq coloured by chain, side view.
PDB entry 1cnq coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase.
Choe JY, Poland BW, Fromm HJ, Honzatko RB
Biochemistry 37 11441-50 (1998)
PMID: 9708979

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 Chain: A
Molecule details ›
Chain: A
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

3 bound ligands:
Ligand F6P 2 x F6P
Ligand ZN 3 x ZN
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: I222
Unit cell:
a: 52.34Å b: 82.82Å c: 166.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 0.227
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)
19 other articles

8 mentions without citation

Crystal structures of human muscle fructose-1,6-bisphosphatase: novel quaternary states, enhanced AMP affinity, and allosteric signal transmission pathway.
Shi et al. (2013)
7 more