› 4mjo

X-ray diffraction
2.4Å resolution

Human liver fructose-1,6-bisphosphatase(d-fructose-1,6-bisphosphate, 1-phosphohydrolase) (e.c.3.1.3.11) complexed with the allosteric inhibitor 3

Released:
DOI: 10.2210/pdb4mjo/pdb
PDB entry 4mjo coloured by chain, front view.
PDB entry 4mjo coloured by chain, side view.
PDB entry 4mjo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Determination of protein-ligand binding constants of a cooperatively regulated tetrameric enzyme using electrospray mass spectrometry.
Cubrilovic D, Haap W, Barylyuk K, Ruf A, Badertscher M, Gubler M, Tetaz T, Joseph C, Benz J, Zenobi R
ACS Chem Biol 9 218-26 (2014)
PMID: 24128068

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-140663 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 338 amino acids
Theoretical weight: 36.89 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P09467 (Residues: 1-338; Coverage: 100%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 2C1 8 x 2C1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 65.974Å b: 286.305Å c: 83.692Å
α: 90° β: 97.79° γ: 90°
R-values:
R R work R free
0.208 0.207 0.236

Quick links

Citations

7 review citations

Mass spectrometry of protein complexes: from origins to applications.
Mehmood et al. (2015)
6 more