PDBe 1pqh

X-ray diffraction
1.29Å resolution

Serine 25 to Threonine mutation of aspartate decarboxylase


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
Aspartate 1-decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 143 amino acids
Theoretical weight: 15.81 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P0A790 (Residues: 1-126; Coverage: 100%)
Gene names: JW0127, b0131, panD
Sequence domains: Aspartate decarboxylase
Structure domains: Barwin-like endoglucanases

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P6122
Unit cell:
a: 70.46Å b: 70.46Å c: 215.299Å
α: 90° β: 90° γ: 120°
R R work R free
0.153 0.153 0.166
Expression system: Escherichia coli