› 1cg4

X-ray diffraction
2.5Å resolution

STRUCTURE OF THE MUTANT (R303L) OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI COMPLEXED WITH, GDP, 6-PHOSPHORYL-IMP, AND MG2+

Released:
DOI: 10.2210/pdb1cg4/pdb
PDB entry 1cg4 coloured by chain, front view.
PDB entry 1cg4 coloured by chain, side view.
PDB entry 1cg4 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli.
Choe JY, Poland BW, Fromm HJ, Honzatko RB
Biochemistry 38 6953-61 (1999)
PMID: 10346917

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: 47.23 KDa
Source organism: Escherichia coli K-12
Expression system: 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

3 bound ligands:
Ligand MG 1 x MG
Ligand IMO 1 x IMO
Ligand GDP 1 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P3221
Unit cell:
a: 80.21Å b: 80.21Å c: 157.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.179 0.252
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structure-function studies of adenylosuccinate synthetase from Escherichia coli.
Honzatko et al. (1999)
11 other articles

1 mention without citation

Crystal structure of glutamine receptor protein from Sulfolobus tokodaii strain 7 in complex with its effector L-glutamine: implications of effector binding in molecular association and DNA binding.
Kumarevel et al. (2008)