PDBe 1pyq

X-ray diffraction
1.9Å resolution

Unprocessed Aspartate Decarboxylase Mutant, with Alanine inserted at position 24

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:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate 1-decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 144 amino acids
Theoretical weight: 15.85 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A790 (Residues: 1-23, 24-126; Coverage: 100%)
Gene names: JW0127, b0131, panD
Sequence domains: Aspartate decarboxylase
Structure domains: Barwin-like endoglucanases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P6122
Unit cell:
a: 70.911Å b: 70.911Å c: 218.665Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.166 0.179
Expression system: Escherichia coli