4aok

X-ray diffraction
1.5Å resolution

Conformational dynamics of aspartate alpha-decarboxylase active site revealed by protein-ligand complexes: 1-methyl-L-aspartate complex

Released:
Source organism: Escherichia coli
Entry authors: Yorke BA, Monteiro DCF, Pearson AR, Webb ME

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate 1-decarboxylase beta chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 41 amino acids
Theoretical weight: 4.77 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
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: 102 amino acids
Theoretical weight: 11.14 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A790 (Residues: 26-126; Coverage: 80%)
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: DIAMOND BEAMLINE I24
Spacegroup: P6122
Unit cell:
a: 71.3Å b: 71.3Å c: 215.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.146 0.144 0.18
Expression system: Escherichia coli BL21