PDBe 1pqf

X-ray diffraction
2Å resolution

Glycine 24 to Serine mutation of 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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 143 amino acids
Theoretical weight: 15.83 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

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P6122
Unit cell:
a: 71.436Å b: 71.436Å c: 219.157Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.165 0.185
Expression system: Escherichia coli