› 3f5m

X-ray diffraction
2.7Å resolution

Crystal Structure of ATP-Bound Phosphofructokinase from Trypanosoma brucei

Released:
DOI: 10.2210/pdb3f5m/pdb
PDB entry 3f5m coloured by chain, front view.
PDB entry 3f5m coloured by chain, side view.
PDB entry 3f5m coloured by chain, top view.
Source organism: Trypanosoma brucei
Primary publication:
The crystal structure of ATP-bound phosphofructokinase from Trypanosoma brucei reveals conformational transitions different from those of other phosphofructokinases.
McNae IW, Martinez-Oyanedel J, Keillor JW, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD
J Mol Biol 385 1519-33 (2009)
PMID: 19084537

Function and Biology Details

Reaction catalysed: 
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127542 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 487 amino acids
Theoretical weight: 53.59 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: O15648 (Residues: 1-487; Coverage: 100%)
Gene name: pfk
Sequence domains: Phosphofructokinase
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ATP 4 x ATP
Ligand MG 3 x MG
Ligand GOL 2 x GOL
Ligand NA 4 x NA
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 96.578Å b: 117.57Å c: 176.587Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.224 0.286
Expression system: Escherichia coli

Quick links

Citations

3 review citations

State of the art in African trypanosome drug discovery.
Jacobs et al. (2011)
2 more

9 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
8 more