› 4gyl

X-ray diffraction
1.9Å resolution

The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine

Released:
DOI: 10.2210/pdb4gyl/pdb
PDB entry 4gyl coloured by chain, front view.
PDB entry 4gyl coloured by chain, side view.
PDB entry 4gyl coloured by chain, top view.
Source organism: Bacillus sp. (in: Bacteria)
Primary publication:
The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.
Weber BW, Kimani SW, Varsani A, Cowan DA, Hunter R, Venter GA, Gumbart JC, Sewell BT
J Biol Chem 288 28514-23 (2013)
PMID: 23946488

Function and Biology Details

Reaction catalysed: 
A monocarboxylic acid amide + H(2)O = a monocarboxylate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192207 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aliphatic amidase Chain: A
Molecule details ›
Chain: A
Length: 348 amino acids
Theoretical weight: 38.62 KDa
Source organism: Bacillus sp. (in: Bacteria)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9L543 (Residues: 1-348; Coverage: 100%)
Gene names: ami, amiE
Sequence domains: Carbon-nitrogen hydrolase
Structure domains: Carbon-nitrogen hydrolase

Ligands and Environments

2 bound ligands:
Ligand ROP 1 x ROP
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P4232
Unit cell:
a: 130.49Å b: 130.49Å c: 130.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.163 0.187
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Cyanide bioremediation: the potential of engineered nitrilases.
Park et al. (2017)
1 more

2 mentions without citation

The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.
Weber et al. (2013)
1 more