› 1dbz

X-ray diffraction
2.65Å resolution

C153S MUTANT OF PEA FRUCTOSE-1,6-BISPHOSPHATASE

Released:
DOI: 10.2210/pdb1dbz/pdb
PDB entry 1dbz coloured by chain, front view.
PDB entry 1dbz coloured by chain, side view.
PDB entry 1dbz coloured by chain, top view.
Source organism: Pisum sativum
Primary publication:
Redox signalling in the chloroplast: structure of oxidized pea fructose-1,6-bisphosphate phosphatase.
Chiadmi M, Navaza A, Miginiac-Maslow M, Jacquot JP, Cherfils J
EMBO J 18 6809-15 (1999)
PMID: 10581254

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155451 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase, chloroplastic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 357 amino acids
Theoretical weight: 39.23 KDa
Source organism: Pisum sativum
Expression system: Escherichia coli
UniProt:
  • Canonical: P46275 (Residues: 51-407; Coverage: 88%)
Gene name: FBP
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE D41A
Spacegroup: P21
Unit cell:
a: 78.9Å b: 114.5Å c: 94.5Å
α: 90° β: 114.5° γ: 90°
R-values:
R R work R free
0.235 0.235 0.291
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Redox regulation: a broadening horizon.
Buchanan et al. (2005)
15 more

4 mentions without citation

Conformational changes in redox pairs of protein structures.
Fan et al. (2009)
3 more