› 6g3d

X-ray diffraction
2.22Å resolution

Function and Biology Details

Reaction catalysed: 
2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171271 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Argininosuccinate lyase Chain: A
Molecule details ›
Chain: A
Length: 508 amino acids
Theoretical weight: 55.76 KDa
Source organism: Chelativorans sp. BNC1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q11KV9 (Residues: 1-502; Coverage: 100%)
Gene name: Meso_0564
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: F222
Unit cell:
a: 144.395Å b: 144.763Å c: 147.618Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.224
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biocatalysis: Enzymatic Synthesis for Industrial Applications.
Wu et al. (2021)
1 more

1 mention 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)