› 5ldz

X-ray diffraction
2.2Å resolution

Quadruple space group ambiguity due to rotational and translational non-crystallographic symmetry in human liver fructose-1,6-bisphosphatase

Released:
DOI: 10.2210/pdb5ldz/pdb
PDB entry 5ldz coloured by chain, front view.
PDB entry 5ldz coloured by chain, side view.
PDB entry 5ldz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Quadruple space-group ambiguity owing to rotational and translational noncrystallographic symmetry in human liver fructose-1,6-bisphosphatase.
Ruf A, Tetaz T, Schott B, Joseph C, Rudolph MG
Acta Crystallogr D Struct Biol 72 1212-1224 (2016)
PMID: 27841754

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
Molecule details ›
Chains: A, B, C, D, E, F
Length: 338 amino acids
Theoretical weight: 36.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09467 (Residues: 1-338; Coverage: 100%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 9 x ZN
Ligand SO4 29 x SO4
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P41212
Unit cell:
a: 121.519Å b: 121.519Å c: 316.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Triple-Stage Mass Spectrometry Unravels the Heterogeneity of an Endogenous Protein Complex.
Ben-Nissan et al. (2017)
3 more

1 mention without citation

Quadruple space-group ambiguity owing to rotational and translational noncrystallographic symmetry in human liver fructose-1,6-bisphosphatase.
Ruf et al. (2016)