2qvr

X-ray diffraction
2.18Å resolution

E. coli Fructose-1,6-bisphosphatase: Citrate, Fru-2,6-P2, and Mg2+ bound

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
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

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I222
Unit cell:
a: 44.002Å b: 82.251Å c: 174.194Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.242
Expression system: Escherichia coli