› 1k62

X-ray diffraction
2.65Å resolution

Crystal Structure of the Human Argininosuccinate Lyase Q286R Mutant

Released:
DOI: 10.2210/pdb1k62/pdb
PDB entry 1k62 coloured by chain, front view.
PDB entry 1k62 coloured by chain, side view.
PDB entry 1k62 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Three-dimensional structure of the argininosuccinate lyase frequently complementing allele Q286R.
Sampaleanu LM, Vallée F, Thompson GD, Howell PL
Biochemistry 40 15570-80 (2001)
PMID: 11747432

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: 51.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04424 (Residues: 1-464; Coverage: 100%)
Gene name: ASL
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 104.202Å b: 104.202Å c: 183.019Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.175 0.229
Expression system: Escherichia coli BL21

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Citations

17 citation in other articles

Regulation of the nitrogen transfer pathway in the arbuscular mycorrhizal symbiosis: gene characterization and the coordination of expression with nitrogen flux.
Tian et al. (2010)
16 more

7 mentions without citation

Spectrum of disease-causing mutations in protein secondary structures.
Khan et al. (2007)
6 more