› 3tm7

X-ray diffraction
1.7Å resolution

Processed Aspartate Decarboxylase Mutant with Asn72 mutated to Ala

Released:
DOI: 10.2210/pdb3tm7/pdb
PDB entry 3tm7 coloured by chain, front view.
PDB entry 3tm7 coloured by chain, side view.
PDB entry 3tm7 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of Escherichia coli aspartate α-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation.
Webb ME, Lobley CM, Soliman F, Kilkenny ML, Smith AG, Blundell TL, Abell C
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 414-7 (2012)
PMID: 22505409

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero octamer
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141556 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate 1-decarboxylase beta chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 26 amino acids
Theoretical weight: 2.99 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A790 (Residues: 1-24; Coverage: 19%)
Gene names: JW0127, b0131, panD
Aspartate 1-decarboxylase alpha chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 102 amino acids
Theoretical weight: 10.98 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A790 (Residues: 25-126; Coverage: 81%)
Gene names: JW0127, b0131, panD
Sequence domains: Aspartate decarboxylase
Structure domains: Barwin-like endoglucanases

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P6122
Unit cell:
a: 71.083Å b: 71.083Å c: 215.807Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.161 0.16 0.184
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli.
Nozaki et al. (2012)

1 mention without citation

Structure of Escherichia coli aspartate α-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation.
Webb et al. (2012)