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FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE, 1-PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH THE ALLOSTERIC INHIBITOR AMP

X-ray diffraction
2.3Å resolution
PDB 1fta coloured by chain and viewed from the front.
PDB 1fta coloured by chain and viewed from the side.
PDB 1fta coloured by chain and viewed from the top.
Source organism: Homo sapiens
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Multimeric state: homo tetramer
Accessible surface area: 44200 Å2
Buried surface area: 17600 Å2
Dissociation area: 7,600 Å2
Dissociation energy (ΔGdiss): 72 kcal/mol
Dissociation entropy (TΔSdiss): 43 kcal/mol
Interface energy (ΔGint): -112 kcal/mol
Symmetry number: 4

Macromolecules

Fructose-1,6-bisphosphatase 1
Chains: A, B, C, D
Length: 337 amino acids
Theoretical weight: 36.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09467 (Residues: 2-338; Coverage: 100%)
Gene names: FBP, FBP1
Pfam:
InterPro:
CATH:
SCOP: Inositol monophosphatase/fructose-1,6-bisphosphatase-like
PDB 1fta contains 4 copies of Fructose-1,6-bisphosphatase 1 in assembly 1. This protein is highlighted and viewed from the front.
PDB 1fta contains 4 copies of Fructose-1,6-bisphosphatase 1 in assembly 1. This protein is highlighted and viewed from the side.
PDB 1fta contains 4 copies of Fructose-1,6-bisphosphatase 1 in assembly 1. This protein is highlighted and viewed from the top.
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