PDBe 3ifa

X-ray diffraction
1.93Å resolution

Human muscle fructose-1,6-bisphosphatase E69Q mutant in complex with AMP

Released:
Source organism: Homo sapiens
Primary publication:
Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase.
Acta Crystallogr. D Biol. Crystallogr. 67 1028-34 (2011)
PMID: 22120740

Function and Biology Details

Reaction catalysed:
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase isozyme 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 338 amino acids
Theoretical weight: 36.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00757 (Residues: 2-339; Coverage: 100%)
Gene name: FBP2
Sequence domains: Fructose-1-6-bisphosphatase, N-terminal domain
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C222
Unit cell:
a: 218.11Å b: 234.26Å c: 71.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 0.199
Expression system: Escherichia coli