› 1fsa

X-ray diffraction
2.3Å resolution

THE T-STATE STRUCTURE OF LYS 42 TO ALA MUTANT OF THE PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI

Released:
DOI: 10.2210/pdb1fsa/pdb
PDB entry 1fsa coloured by chain, front view.
PDB entry 1fsa coloured by chain, side view.
PDB entry 1fsa coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity.
Lu G, Stec B, Giroux EL, Kantrowitz ER
Protein Sci 5 2333-42 (1996)
PMID: 8931152

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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132778 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 36.65 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P00636 (Residues: 2-338; Coverage: 100%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand F6P 2 x F6P
Ligand MN 2 x MN
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21212
Unit cell:
a: 61.05Å b: 166.72Å c: 79.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.232
Expression system: Escherichia coli

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Citations

8 citation in other articles

Altered subunit communication in subfamilies of trimeric dUTPases.
Fiser et al. (2000)
7 more