› 1a3w

X-ray diffraction
3Å resolution

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

Released:
DOI: 10.2210/pdb1a3w/pdb
PDB entry 1a3w coloured by chain, front view.
PDB entry 1a3w coloured by chain, side view.
PDB entry 1a3w 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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132710 (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

4 bound ligands:
Ligand PGA 2 x PGA
Ligand FBP 2 x FBP
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: 109.4Å b: 102.7Å c: 110.9Å
α: 90° β: 112.3° γ: 90°
R-values:
R R work R free
0.218 0.218 0.323

Quick links

Citations

50 review citations

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

10 mentions without citation

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