› 5et6

X-ray diffraction
1.84Å resolution

Human muscle fructose-1,6-bisphosphatase in inactive T-state in complex with AMP

Released:
DOI: 10.2210/pdb5et6/pdb
PDB entry 5et6 coloured by chain, front view.
PDB entry 5et6 coloured by chain, side view.
PDB entry 5et6 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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: C222
Unit cell:
a: 218.622Å b: 234.733Å c: 71.607Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.192
Expression system: Escherichia coli

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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

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