› 4g1n

X-ray diffraction
2.3Å 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: 56.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14618 (Residues: 14-531; Coverage: 98%)
Gene names: OIP3, PK2, PK3, PKM, PKM2
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand OXL 4 x OXL
Ligand MG 4 x MG
Ligand NZT 2 x NZT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: C2
Unit cell:
a: 168.118Å b: 94.141Å c: 146.149Å
α: 90° β: 99.39° γ: 90°
R-values:
R R work R free
0.214 0.212 0.266
Expression system: Escherichia coli

Quick links

Citations

47 review citations

Serine, glycine and one-carbon units: cancer metabolism in full circle.
Locasale JW. (2013)
46 more

11 mentions without citation

Small molecule activation of PKM2 in cancer cells induces serine auxotrophy.
Kung et al. (2012)
10 more