› 3ifa

X-ray diffraction
1.93Å resolution

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

Released:
DOI: 10.2210/pdb3ifa/pdb
PDB entry 3ifa coloured by chain, front view.
PDB entry 3ifa coloured by chain, side view.
PDB entry 3ifa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase.
Zarzycki M, Kołodziejczyk R, Maciaszczyk-Dziubinska E, Wysocki R, Jaskolski M, Dzugaj A
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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126382 (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:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand AMP 4 x AMP
Ligand SO4 13 x SO4
Ligand GOL 6 x GOL
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

Quick links

Citations

1 review citation

Emerging Computational Methods for the Rational Discovery of Allosteric Drugs.
Wagner et al. (2016)
3 other articles

6 mentions without citation

T-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structure.
Barciszewski et al. (2016)
5 more