6tth

Electron Microscopy
2.6Å resolution

PKM2 in complex with L-threonine

Released:
Source organism: Homo sapiens
Primary publication:
Fragment-based drug discovery using cryo-EM.
Drug Discov Today 25 485-490 (2020)
PMID: 31877353
Related structures: EMD-10576

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:
Cellular component:

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: 548 amino acids
Theoretical weight: 59.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14618 (Residues: 2-531; Coverage: 100%)
Gene names: OIP3, PK2, PK3, PKM, PKM2
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.6Å
Relevant EMDB volumes: EMD-10576
Expression system: Escherichia coli