› 4kxp

X-ray diffraction
2.7Å resolution

Crystal Structure of AMP complexes of Porcine Liver Fructose-1,6-bisphosphatase Mutant I10D in T-state

Released:
DOI: 10.2210/pdb4kxp/pdb
PDB entry 4kxp coloured by chain, front view.
PDB entry 4kxp coloured by chain, side view.
PDB entry 4kxp coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Mechanism of displacement of a catalytically essential loop from the active site of mammalian fructose-1,6-bisphosphatase.
Gao Y, Iancu CV, Mukind S, Choe JY, Honzatko RB
Biochemistry 52 5206-16 (2013)
PMID: 23844654

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-132778 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 36.82 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P00636 (Residues: 1-338; Coverage: 100%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand F6P 2 x F6P
Ligand PO4 2 x PO4
Ligand MG 4 x MG
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 59.544Å b: 166.382Å c: 78.946Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.252
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Fructose 1,6-bisphosphatase: getting the message across.
Timson DJ. (2019)
3 more

1 mention without citation

Mechanism of displacement of a catalytically essential loop from the active site of mammalian fructose-1,6-bisphosphatase.
Gao et al. (2013)