› 1aos

X-ray diffraction
4.2Å resolution

HUMAN ARGININOSUCCINATE LYASE

Released:
DOI: 10.2210/pdb1aos/pdb
PDB entry 1aos coloured by chain, front view.
PDB entry 1aos coloured by chain, side view.
PDB entry 1aos coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human argininosuccinate lyase: a structural basis for intragenic complementation.
Turner MA, Simpson A, McInnes RR, Howell PL
Proc Natl Acad Sci U S A 94 9063-8 (1997)
PMID: 9256435

Function and Biology Details

Reaction catalysed: 
2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
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-137637 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Argininosuccinate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 464 amino acids
Theoretical weight: 51.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04424 (Residues: 1-464; Coverage: 100%)
Gene name: ASL
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P3121
Unit cell:
a: 104.6Å b: 104.6Å c: 183.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.298
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

Argininosuccinate lyase deficiency-argininosuccinic aciduria and beyond.
Erez et al. (2011)
7 more

8 mentions without citation

Deamidation of human proteins.
Robinson et al. (2001)
7 more