› 4d7z

X-ray diffraction
1.9Å resolution

E. coli L-aspartate-alpha-decarboxylase mutant N72Q to a resolution of 1.9 Angstroms

Released:
DOI: 10.2210/pdb4d7z/pdb
PDB entry 4d7z coloured by chain, front view.
PDB entry 4d7z coloured by chain, side view.
PDB entry 4d7z coloured by chain, top view.
Source organism: Escherichia coli
Entry authors: Bravo JPK, Monteiro DCF, Webb ME, Pearson AR

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

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141555 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate 1-decarboxylase beta chain Chain: A
Molecule details ›
Chain: A
Length: 41 amino acids
Theoretical weight: 4.77 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 Chain: B
Molecule details ›
Chain: B
Length: 95 amino acids
Theoretical weight: 10.35 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A790 (Residues: 26-119; Coverage: 75%)
Gene names: JW0127, b0131, panD
Sequence domains: Aspartate decarboxylase
Structure domains: Barwin-like endoglucanases

Ligands and Environments

2 bound ligands:
Ligand PEG 1 x PEG
Ligand SCN 2 x SCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I422
Unit cell:
a: 71.35Å b: 71.35Å c: 112.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.244
Expression system: Escherichia coli

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