PDBe 1aw8

X-ray diffraction
2.2Å resolution

PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

Released:

Function and Biology Details

Reaction catalysed:
L-aspartate = beta-alanine + CO(2). 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate 1-decarboxylase beta chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 24 amino acids
Theoretical weight: 2.84 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A790 (Residues: 1-24; Coverage: 19%)
Gene names: JW0127, b0131, panD
Aspartate 1-decarboxylase alpha chain Chains: B, E
Molecule details ›
Chains: B, E
Length: 91 amino acids
Theoretical weight: 9.87 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A790 (Residues: 26-115, 25-115; Coverage: 72%)
Gene names: JW0127, b0131, panD
Structure domains: Barwin-like endoglucanases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P6122
Unit cell:
a: 72.17Å b: 72.17Å c: 216.14Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.2 0.239
Expression system: Escherichia coli