› 1tj7

X-ray diffraction
2.44Å resolution

Structure determination and refinement at 2.44 A resolution of Argininosuccinate lyase from E. coli

Released:
DOI: 10.2210/pdb1tj7/pdb
PDB entry 1tj7 coloured by chain, front view.
PDB entry 1tj7 coloured by chain, side view.
PDB entry 1tj7 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli.
Bhaumik P, Koski MK, Bergmann U, Wierenga RK
Acta Crystallogr D Biol Crystallogr 60 1964-70 (2004)
PMID: 15502303

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

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-145840 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Argininosuccinate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 457 amino acids
Theoretical weight: 50.37 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P11447 (Residues: 1-457; Coverage: 100%)
Gene names: JW3932, argH, b3960
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PO4 2 x PO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P6122
Unit cell:
a: 121.469Å b: 121.469Å c: 255.251Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.167 0.217

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Citations

1 review citation

Genes, enzymes and regulation of arginine biosynthesis in plants.
Slocum RD. (2005)
10 other articles

6 mentions without citation

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