› 4yj5

X-ray diffraction
2.41Å resolution

Function and Biology Details

Reactions catalysed: 
ATP + pyruvate = ADP + phosphoenolpyruvate
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146985 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase PKM Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 518 amino acids
Theoretical weight: 56.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14618 (Residues: 14-531; Coverage: 98%)
Gene names: OIP3, PK2, PK3, PKM, PKM2
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand PYR 4 x PYR
Ligand MG 4 x MG
Ligand SER 4 x SER
Ligand FBP 3 x FBP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21
Unit cell:
a: 73.217Å b: 140.887Å c: 108.72Å
α: 90° β: 93.97° γ: 90°
R-values:
R R work R free
0.148 0.144 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Glucose Metabolism on Tumor Plasticity, Diagnosis, and Treatment.
Lin et al. (2020)
5 more

1 mention without citation

Mutations in the PKM2 exon-10 region are associated with reduced allostery and increased nuclear translocation.
Chen et al. (2019)