› 7ns5

X-ray diffraction
1.95Å resolution

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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140588 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 354 amino acids
Theoretical weight: 39.13 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09201 (Residues: 1-348; Coverage: 100%)
Gene names: FBP1, L8039.18, YLR377C
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand PO4 4 x PO4
Ligand MG 8 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 58.018Å b: 133.794Å c: 171.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini.
Sherpa et al. (2022)
3 more

1 mention without citation

GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme.
Sherpa et al. (2021)