› 1fta

X-ray diffraction
2.3Å resolution

FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE, 1-PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH THE ALLOSTERIC INHIBITOR AMP

Released:
DOI: 10.2210/pdb1fta/pdb
PDB entry 1fta coloured by chain, front view.
PDB entry 1fta coloured by chain, side view.
PDB entry 1fta coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The allosteric site of human liver fructose-1,6-bisphosphatase. Analysis of six AMP site mutants based on the crystal structure.
Gidh-Jain M, Zhang Y, van Poelje PD, Liang JY, Huang S, Kim J, Elliott JT, Erion MD, Pilkis SJ, Raafat el-Maghrabi M
J Biol Chem 269 27732-8 (1994)
PMID: 7961695

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-140663 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 337 amino acids
Theoretical weight: 36.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09467 (Residues: 2-338; Coverage: 100%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand AMP 4 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 68.6Å b: 84.8Å c: 281.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Enzymes involved in l-lactate metabolism in humans.
Adeva et al. (2013)
1 more

12 mentions without citation

Deamidation of human proteins.
Robinson et al. (2001)
11 more