› 5q0c

X-ray diffraction
2.4Å resolution

Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[5-(4-methoxyphenyl)thiophen-2-yl]sulfonylurea and with fructose-2,6-diphosphate

Released:
DOI: 10.2210/pdb5q0c/pdb
Model geometry
Fit model/data
PDB entry 5q0c coloured by chain, front view.
PDB entry 5q0c coloured by chain, side view.
PDB entry 5q0c coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Ruf A, Joseph C, Alker A, Banner D, Tetaz T, Benz J, Kuhn B, Rudolph MG, Yang H, Shao C, Burley SK

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, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 339 amino acids
Theoretical weight: 36.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00757 (Residues: 1-339; Coverage: 100%)
Gene name: FBP2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 96G 8 x 96G
Ligand FDP 8 x FDP
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 222.475Å b: 240.518Å c: 138.979Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.21
Expression system: Escherichia coli

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