› 1e0t

X-ray diffraction
1.8Å resolution

R292D mutant of E. coli pyruvate kinase

Released:
DOI: 10.2210/pdb1e0t/pdb
PDB entry 1e0t coloured by chain, front view.
PDB entry 1e0t coloured by chain, side view.
PDB entry 1e0t coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The allosteric regulation of pyruvate kinase.
Valentini G, Chiarelli L, Fortin R, Speranza ML, Galizzi A, Mattevi A
J Biol Chem 275 18145-52 (2000)
PMID: 10751408

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate = ADP + phosphoenolpyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142330 (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
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:
Ligand SO4 4 x SO4
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

Quick links

Citations

9 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
8 more

3 mentions without citation

All DACs in a Row: Domain Architectures of Bacterial and Archaeal Diadenylate Cyclases.
Galperin MY. (2023)
2 more