› › Structure analysis

CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE

X-ray diffraction
2.9Å resolution
PDB entry 1fbd coloured by chain, front view.
PDB entry 1fbd coloured by chain, side view.
PDB entry 1fbd coloured by chain, top view.
Source organism: Sus scrofa
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

Quick links

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Assembly Name: Fructose-1,6-bisphosphatase 1
hide full assembly name
Multimeric state: homo tetramer
Accessible surface area: 43887.01 Å2
Buried surface area: 17165.72 Å2
Dissociation area: 2,679.03 Å2
Dissociation energy (ΔGdiss): 24.34 kcal/mol
Dissociation entropy (TΔSdiss): 15.17 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-132778

Macromolecules

Fructose-1,6-bisphosphatase 1
Chains: A, B
Length: 335 amino acids
Theoretical weight: 36.5 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00636 (Residues: 2-336; Coverage: 99%)
Gene names: FBP, FBP1
Pfam:
InterPro:
CATH:
SCOP: Inositol monophosphatase/fructose-1,6-bisphosphatase-like
Fructose-1,6-bisphosphatase 1 in PDB entry 1fbd, assembly 1, front view.
Fructose-1,6-bisphosphatase 1 in PDB entry 1fbd, assembly 1, side view.
Fructose-1,6-bisphosphatase 1 in PDB entry 1fbd, assembly 1, top view.
Molecule details ›

Search similar proteins

Quick links