› 3r6v

X-ray diffraction
2.6Å resolution

Crystal structure of aspartase from Bacillus sp. YM55-1 with bound L-aspartate

Released:
DOI: 10.2210/pdb3r6v/pdb
PDB entry 3r6v coloured by chain, front view.
PDB entry 3r6v coloured by chain, side view.
PDB entry 3r6v coloured by chain, top view.
Source organism: Bacillus sp. YM55-1
Primary publication:
Structural basis for the catalytic mechanism of aspartate ammonia lyase.
Fibriansah G, Veetil VP, Poelarends GJ, Thunnissen AM
Biochemistry 50 6053-62 (2011)
PMID: 21661762

Function and Biology Details

Reaction catalysed: 
L-aspartate = fumarate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192255 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate ammonia-lyase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 468 amino acids
Theoretical weight: 51.69 KDa
Source organism: Bacillus sp. YM55-1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9LCC6 (Residues: 1-468; Coverage: 100%)
Gene name: aspB
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand ASP 2 x ASP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 75.853Å b: 118.96Å c: 141.414Å
α: 89.93° β: 89.93° γ: 76.42°
R-values:
R R work R free
0.196 0.193 0.25
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Enzymatic asymmetric synthesis of chiral amino acids.
Xue et al. (2018)
2 more

2 mentions without citation

Structural Basis for the Catalytic Mechanism of Ethylenediamine- N, N'-disuccinic Acid Lyase, a Carbon-Nitrogen Bond-Forming Enzyme with a Broad Substrate Scope.
Poddar et al. (2018)
1 more