PDBe 1pqe

X-ray diffraction
1.95Å resolution

S25A mutant of pyruvoyl dependent aspartate decarboxylase

Released:

Function and Biology Details

Reaction catalysed:
L-aspartate = beta-alanine + CO(2). 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate 1-decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 126 amino acids
Theoretical weight: 13.83 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A790 (Residues: 1-126; Coverage: 100%)
Gene names: JW0127, b0131, panD
Sequence domains: Aspartate decarboxylase
Structure domains: Barwin-like endoglucanases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: I422
Unit cell:
a: 73.056Å b: 73.056Å c: 111.114Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.205
Expression system: Escherichia coli