› 1kp2

X-ray diffraction
2Å resolution

Crystal Structure of E. coli Argininosuccinate Synthetase in Complex with ATP

Released:
DOI: 10.2210/pdb1kp2/pdb
PDB entry 1kp2 coloured by chain, front view.
PDB entry 1kp2 coloured by chain, side view.
PDB entry 1kp2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Substrate induced conformational changes in argininosuccinate synthetase.
Lemke CT, Howell PL
J Biol Chem 277 13074-81 (2002)
PMID: 11809762

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

3 bound ligands:
Ligand PO4 3 x PO4
Ligand ATP 1 x ATP
Ligand GAI 1 x GAI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I222
Unit cell:
a: 78.059Å b: 104.05Å c: 128.573Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.216
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

1 mention without citation

Recognition of functional sites in protein structures.
Shulman-Peleg et al. (2004)