PDBe 1dj3

X-ray diffraction
3Å resolution

STRUCTURES OF ADENYLOSUCCINATE SYNTHETASE FROM TRITICUM AESTIVUM AND ARABIDOPSIS THALIANA

Released:

Function and Biology Details

Reaction catalysed:
GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate synthetase, chloroplastic Chains: A, B
Molecule details ›
Chains: A, B
Length: 442 amino acids
Theoretical weight: 47.79 KDa
Source organism: Triticum aestivum
Expression system: Escherichia coli
UniProt:
  • Canonical: O24396 (Residues: 35-476; Coverage: 93%)
Sequence domains: Adenylosuccinate synthetase
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: P41212
Unit cell:
a: 151.44Å b: 151.44Å c: 91.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.303
Expression system: Escherichia coli