› 1j3u

X-ray diffraction
2.5Å resolution

Crystal structure of aspartase from Bacillus sp. YM55-1

Released:
DOI: 10.2210/pdb1j3u/pdb
PDB entry 1j3u coloured by chain, front view.
PDB entry 1j3u coloured by chain, side view.
PDB entry 1j3u coloured by chain, top view.
Source organism: Bacillus sp. YM55-1
Primary publication:
Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family.
Fujii T, Sakai H, Kawata Y, Hata Y
J Mol Biol 328 635-54 (2003)
PMID: 12706722

Function and Biology Details

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

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
Molecule details ›
Chains: A, B
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P21212
Unit cell:
a: 74.9Å b: 139.4Å c: 100.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.266
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism.
Tsai et al. (2007)
10 more

1 mention without citation

Exploring key orientations at protein-protein interfaces with small molecule probes.
Ko et al. (2013)