› 1aw8

X-ray diffraction
2.2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141559 (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
Sequence domains: Aspartate decarboxylase
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

Quick links

Citations

12 review citations

Protein posttranslational modifications: the chemistry of proteome diversifications.
Walsh et al. (2005)
11 more

10 mentions without citation

Prediction of catalytic residues using Support Vector Machine with selected protein sequence and structural properties.
Petrova et al. (2006)
9 more