PDBe 1pyu

X-ray diffraction
1.9Å resolution

Processed Aspartate Decarboxylase Mutant with Ser25 mutated to Cys

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 alpha chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 102 amino acids
Theoretical weight: 11.04 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A790 (Residues: 25-126; Coverage: 81%)
Gene names: JW0127, b0131, panD
Structure domains: Barwin-like endoglucanases
Aspartate 1-decarboxylase beta chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 41 amino acids
Theoretical weight: 4.77 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A790 (Residues: 1-24; Coverage: 19%)
Gene names: JW0127, b0131, panD

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P6122
Unit cell:
a: 70.787Å b: 70.787Å c: 217.121Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.173 0.196
Expression system: Escherichia coli