4qg8

X-ray diffraction
2.3Å resolution

crystal structure of PKM2-K305Q mutant

Released:
Source organism: Homo sapiens
Primary publication:
Structural insight into mechanisms for dynamic regulation of PKM2.
Protein Cell 6 275-287 (2015)
PMID: 25645022

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: 535 amino acids
Theoretical weight: 58.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14618 (Residues: 1-531; Coverage: 100%)
Gene names: OIP3, PK2, PK3, PKM, PKM2
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 94.812Å b: 117.377Å c: 110.33Å
α: 90° β: 113.21° γ: 90°
R-values:
R R work R free
0.216 0.213 0.26
Expression system: Escherichia coli