› 5et5

X-ray diffraction
1.67Å resolution

Human muscle fructose-1,6-bisphosphatase in active R-state

Released:
DOI: 10.2210/pdb5et5/pdb
PDB entry 5et5 coloured by chain, front view.
PDB entry 5et5 coloured by chain, side view.
PDB entry 5et5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
T-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structure.
Barciszewski J, Wisniewski J, Kolodziejczyk R, Jaskolski M, Rakus D, Dzugaj A
Acta Crystallogr D Struct Biol 72 536-50 (2016)
PMID: 27050133

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-126382 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase isozyme 2 Chain: A
Molecule details ›
Chain: A
Length: 338 amino acids
Theoretical weight: 36.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00757 (Residues: 2-339; Coverage: 100%)
Gene name: FBP2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: I4122
Unit cell:
a: 72.564Å b: 72.564Å c: 235.348Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.22
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Targeting FBPase is an emerging novel approach for cancer therapy.
Liu et al. (2018)
9 other articles

2 mentions without citation

T-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structure.
Barciszewski et al. (2016)
1 more