› 2ox3

X-ray diffraction
2.18Å resolution

R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase

Released:
DOI: 10.2210/pdb2ox3/pdb
PDB entry 2ox3 coloured by chain, front view.
PDB entry 2ox3 coloured by chain, side view.
PDB entry 2ox3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state.
Hines JK, Fromm HJ, Honzatko RB
J Biol Chem 282 11696-704 (2007)
PMID: 17314096

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-141853 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase class 1 Chain: A
Molecule details ›
Chain: A
Length: 332 amino acids
Theoretical weight: 37.16 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A993 (Residues: 1-332; Coverage: 100%)
Gene names: JW4191, b4232, fbp, fdp
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand F6P 1 x F6P
Ligand PEP 1 x PEP
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I222
Unit cell:
a: 44.687Å b: 83.112Å c: 174.422Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.212 0.262
Expression system: Escherichia coli

Quick links

Citations

13 citation in other articles

Metabolic control of the Escherichia coli universal stress protein response through fructose-6-phosphate.
Persson et al. (2007)
12 more

5 mentions without citation

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
4 more