› 1pqe

X-ray diffraction
1.95Å resolution

S25A mutant of pyruvoyl dependent aspartate decarboxylase

Released:
DOI: 10.2210/pdb1pqe/pdb
PDB entry 1pqe coloured by chain, front view.
PDB entry 1pqe coloured by chain, side view.
PDB entry 1pqe coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase.
Schmitzberger F, Kilkenny ML, Lobley CM, Webb ME, Vinkovic M, Matak-Vinkovic D, Witty M, Chirgadze DY, Smith AG, Abell C, Blundell TL
EMBO J 22 6193-204 (2003)
PMID: 14633979

Function and Biology Details

Reaction catalysed: 
L-aspartate = beta-alanine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141557 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate 1-decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 126 amino acids
Theoretical weight: 13.83 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: I422
Unit cell:
a: 73.056Å b: 73.056Å c: 111.114Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.205
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Elucidating biosynthetic pathways for vitamins and cofactors.
Webb et al. (2007)
3 more

1 mention without citation

Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase.
Schmitzberger et al. (2003)