› 6su1

X-ray diffraction
3Å resolution

Trypanosoma congolense pyruvate kinase in complex with citrate and glycerol

Released:
DOI: 10.2210/pdb6su1/pdb
PDB entry 6su1 coloured by chain, front view.
PDB entry 6su1 coloured by chain, side view.
PDB entry 6su1 coloured by chain, top view.
Source organism: Trypanosoma congolense IL3000
Primary publication:
Structural and kinetic characterization of Trypanosoma congolense pyruvate kinase.
Pinto Torres JE, Yuan M, Goossens J, Versées W, Caljon G, Michels PA, Walkinshaw MD, Magez S, Sterckx YG
Mol Biochem Parasitol 236 111263 (2020)
PMID: 32084384

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-124136 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 514 amino acids
Theoretical weight: 56.42 KDa
Source organism: Trypanosoma congolense IL3000
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G0UYF4 (Residues: 1-499; Coverage: 100%)
Gene name: TCIL3000_10_12020
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand GOL 10 x GOL
Ligand CIT 6 x CIT
Ligand PGE 1 x PGE
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P1
Unit cell:
a: 83.45Å b: 107.15Å c: 148Å
α: 109.74° β: 90.51° γ: 106.78°
R-values:
R R work R free
0.21 0.208 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

PYK-SubstitutionOME: an integrated database containing allosteric coupling, ligand affinity and mutational, structural, pathological, bioinformatic and computational information about pyruvate kinase isozymes.
Swint-Kruse et al. (2023)