PDBe 1mum

X-ray diffraction
1.9Å resolution

Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli

Released:

Function and Biology Details

Reaction catalysed:
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate. 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-methylisocitrate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 32.04 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P77541 (Residues: 2-296; Coverage: 100%)
Gene names: JW0323, b0331, prpB, yahQ
Sequence domains: Phosphoenolpyruvate phosphomutase
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 82.895Å b: 82.895Å c: 166.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.213 0.234
Expression system: Escherichia coli