PDBe 4rpp

X-ray diffraction
2.58Å resolution

crystal structure of PKM2-K422R mutant bound with FBP

Source organism: Homo sapiens
Primary publication:
Structural insight into mechanisms for dynamic regulation of PKM2.
OpenAccess logo Protein Cell (2015)
PMID: 25645022

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Pyruvate kinase PKM Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 536 amino acids
Theoretical weight: 58.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P14618 (Residues: 1-531; Coverage: 100%)
Gene names: OIP3, PK2, PK3, PKM, PKM2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 81.674Å b: 152.554Å c: 97.676Å
α: 90° β: 104.24° γ: 90°
R R work R free
0.275 0.274 0.308
Expression system: Escherichia coli