› 1pt0

X-ray diffraction
2Å resolution

Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with an Alanine insertion at position 26

Released:
DOI: 10.2210/pdb1pt0/pdb
PDB entry 1pt0 coloured by chain, front view.
PDB entry 1pt0 coloured by chain, side view.
PDB entry 1pt0 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:
  • not assigned
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 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: 1-25, 26-126; Coverage: 100%)
Gene names: JW0127, b0131, panD
Sequence domains: Aspartate decarboxylase
Structure domains: Barwin-like endoglucanases

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P6122
Unit cell:
a: 70.935Å b: 70.935Å c: 217.741Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.174 0.191
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)