› 1soo

X-ray diffraction
2.6Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate synthetase Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 47.27 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0A7D4 (Residues: 2-432; Coverage: 100%)
Gene names: JW4135, adeK, b4177, purA
Sequence domains: Adenylosuccinate synthetase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SO4 3 x SO4
Ligand NA 1 x NA
Ligand H5P 1 x H5P
Ligand BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS
Spacegroup: P43212
Unit cell:
a: 70.5Å b: 70.5Å c: 198.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 not available

Quick links

Citations

6 review citations

Pyrimidine and purine biosynthesis and degradation in plants.
Zrenner et al. (2006)
5 more

1 mention without citation

Overexpression, purification, crystallization and preliminary crystallographic studies of a hyperthermophilic adenylosuccinate synthetase from Pyrococcus horikoshii OT3.
Wang et al. (2011)