› 4hyw

X-ray diffraction
2.35Å resolution

Pyruvate kinase (PYK) from Trypanosoma brucei in the presence of Magnesium and F26BP

Released:
DOI: 10.2210/pdb4hyw/pdb
PDB entry 4hyw coloured by chain, front view.
PDB entry 4hyw coloured by chain, side view.
PDB entry 4hyw coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
`In crystallo' substrate binding triggers major domain movements and reveals magnesium as a co-activator of Trypanosoma brucei pyruvate kinase.
Zhong W, Morgan HP, McNae IW, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD
Acta Crystallogr D Biol Crystallogr 69 1768-79 (2013)
PMID: 23999300

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate = ADP + phosphoenolpyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 499 amino acids
Theoretical weight: 54.54 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: P30615 (Residues: 1-499; Coverage: 100%)
Gene name: PYK1
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand MG 2 x MG
Ligand K 2 x K
Ligand FDP 2 x FDP
Ligand CL 1 x CL
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: I222
Unit cell:
a: 103.68Å b: 109Å c: 268.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.199
Expression system: Escherichia coli

Quick links

Citations

1 review citation

An overview of structure, function, and regulation of pyruvate kinases.
Schormann et al. (2019)
7 other articles

2 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)
1 more