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X-ray diffraction
2.2Å resolution

Structure of human muscle pyruvate kinase (PKM2)

Released:
Source organism: Homo sapiens
Entry authors: Choe J, Atanassova A, Arrowsmith C, Edwards A, Sundstrom M, Bochkarev A, Park H, Structural Genomics Consortium (SGC)

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 Chain: A
Molecule details ›
Chain: A
Length: 548 amino acids
Theoretical weight: 59.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14618 (Residues: 3-531; Coverage: 100%)
Gene names: OIP3, PK2, PK3, PKM, PKM2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I222
Unit cell:
a: 86.45Å b: 111.29Å c: 126.297Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.231 0.279
Expression system: Escherichia coli BL21(DE3)