› 1k97

X-ray diffraction
2Å resolution

Crystal Structure of E. coli Argininosuccinate Synthetase in complex with Aspartate and Citrulline

Released:
DOI: 10.2210/pdb1k97/pdb
PDB entry 1k97 coloured by chain, front view.
PDB entry 1k97 coloured by chain, side view.
PDB entry 1k97 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis.
Lemke CT, Howell PL
Structure 9 1153-64 (2001)
PMID: 11738042

Function and Biology Details

Reaction catalysed: 
ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141302 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Argininosuccinate synthase Chain: A
Molecule details ›
Chain: A
Length: 455 amino acids
Theoretical weight: 50.97 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6E4 (Residues: 2-447; Coverage: 100%)
Gene names: JW3140, argG, b3172
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ASP 1 x ASP
Ligand CIR 1 x CIR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I222
Unit cell:
a: 77.996Å b: 105.336Å c: 127.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.214
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Almost all about citrulline in mammals.
Curis et al. (2005)
3 more

1 mention without citation

Multi-Body Interactions in Molecular Docking Program Devised with Key Water Molecules in Protein Binding Sites.
Xiao et al. (2018)