PDBe 1e0t

X-ray diffraction
1.8Å resolution

R292D mutant of E. coli pyruvate kinase

Released:
Source organism: Escherichia coli BL21
Primary publication:
The allosteric regulation of pyruvate kinase.
J. Biol. Chem. 275 18145-52 (2000)
PMID: 10751408

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase I Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 470 amino acids
Theoretical weight: 50.75 KDa
Source organism: Escherichia coli BL21
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0AD61 (Residues: 1-470; Coverage: 100%)
Gene names: JW1666, b1676, pykF
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 74.47Å b: 129.34Å c: 240.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.246 0.315
Expression system: Escherichia coli BL21