› 1a3x

X-ray diffraction
3Å resolution

PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PG, MN2+ AND K+

Released:
DOI: 10.2210/pdb1a3x/pdb
PDB entry 1a3x coloured by chain, front view.
PDB entry 1a3x coloured by chain, side view.
PDB entry 1a3x coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate.
Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL
Structure 6 195-210 (1998)
PMID: 9519410

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132709 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 500 amino acids
Theoretical weight: 54.61 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00549 (Residues: 1-500; Coverage: 100%)
Gene names: CDC19, PYK1, YAL038W
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand PGA 2 x PGA
Ligand MN 2 x MN
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 108.3Å b: 106.4Å c: 105.5Å
α: 90° β: 110.8° γ: 90°
R-values:
R R work R free
0.227 0.227 0.341

Quick links

Citations

51 review citations

Aerobic glycolysis: meeting the metabolic requirements of cell proliferation.
Lunt et al. (2011)
50 more

3 mentions without citation

An overview of structure, function, and regulation of pyruvate kinases.
Schormann et al. (2019)
2 more