› 1nht

X-ray diffraction
2.5Å resolution

ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100K

Released:
DOI: 10.2210/pdb1nht/pdb
PDB entry 1nht coloured by chain, front view.
PDB entry 1nht coloured by chain, side view.
PDB entry 1nht coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli.
Poland BW, Bruns C, Fromm HJ, Honzatko RB
J Biol Chem 272 15200-5 (1997)
PMID: 9182542

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 MG 1 x MG
Ligand GDP 1 x GDP
Ligand HDA 1 x HDA
Ligand PGS 1 x PGS
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 80.54Å b: 80.54Å c: 158.15Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.255

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Citations

2 review citations

Structure-function studies of adenylosuccinate synthetase from Escherichia coli.
Honzatko et al. (1999)
1 more