› 3roj

X-ray diffraction
2.3Å resolution

D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase of Synechocystis sp. PCC 6803

Released:
DOI: 10.2210/pdb3roj/pdb
PDB entry 3roj coloured by chain, front view.
PDB entry 3roj coloured by chain, side view.
PDB entry 3roj coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6803
Entry authors: Hu X, Hui D, Lingling F, Jian W

Function and Biology Details

Reactions catalysed: 
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Sedoheptulose 1,7-bisphosphate + H(2)O = sedoheptulose 7-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159912 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 379 amino acids
Theoretical weight: 40.65 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli
UniProt:
  • Canonical: P73922 (Residues: 2-345; Coverage: 100%)
Gene name: slr2094
Sequence domains: Bacterial fructose-1,6-bisphosphatase, glpX-encoded
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand MG 8 x MG
Ligand AMP 4 x AMP
Ligand SO4 17 x SO4
Ligand CL 23 x CL
Ligand GOL 1 x GOL
1 modified residue:
Ligand CSO 4 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: P65
Unit cell:
a: 144.282Å b: 144.282Å c: 168.795Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 0.204
Expression system: Escherichia coli

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