› 1lny

X-ray diffraction
2.2Å resolution

Crystal structure of the recombinant mouse-muscle adenylosuccinate synthetase complexed with 6-phosphoryl-IMP, GDP and Mg

Released:
DOI: 10.2210/pdb1lny/pdb
PDB entry 1lny coloured by chain, front view.
PDB entry 1lny coloured by chain, side view.
PDB entry 1lny coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle adenylosuccinate synthetase.
Iancu CV, Borza T, Fromm HJ, Honzatko RB
J Biol Chem 277 26779-87 (2002)
PMID: 12004071

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-151258 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate synthetase isozyme 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 457 amino acids
Theoretical weight: 50.32 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P28650 (Residues: 1-457; Coverage: 100%)
Gene names: Adss1, Adssl1
Sequence domains: Adenylosuccinate synthetase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand IMO 2 x IMO
Ligand GDP 2 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 128.5Å b: 70.12Å c: 105.13Å
α: 90° β: 90.46° γ: 90°
R-values:
R R work R free
0.207 0.207 0.259
Expression system: Escherichia coli BL21

Quick links

Citations

11 citation in other articles

G-domain dimerization orchestrates the tRNA wobble modification reaction in the MnmE/GidA complex.
Meyer et al. (2009)
10 more

2 mentions without citation

Orthogonal dipolar interactions between amide carbonyl groups.
Fischer et al. (2008)
1 more