› 12as

X-ray diffraction
2.2Å resolution

ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP

Released:
DOI: 10.2210/pdb12as/pdb
PDB entry 12as coloured by chain, front view.
PDB entry 12as coloured by chain, side view.
PDB entry 12as coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase.
Nakatsu T, Kato H, Oda J
Nat Struct Biol 5 15-9 (1998)
PMID: 9437423

Function and Biology Details

Reaction catalysed: 
ATP + L-aspartate + NH(3) = AMP + diphosphate + L-asparagine
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-133740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate--ammonia ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 330 amino acids
Theoretical weight: 36.63 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00963 (Residues: 1-330; Coverage: 100%)
Gene names: JW3722, asnA, b3744
Sequence domains: Aspartate-ammonia ligase
Structure domains: Bira Bifunctional Protein; Domain 2

Ligands and Environments

2 bound ligands:
Ligand ASN 2 x ASN
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 53Å b: 126.13Å c: 52.86Å
α: 90° β: 105.59° γ: 90°
R-values:
R R work R free
0.164 0.164 0.287
Expression system: Escherichia coli

Quick links

Citations

9 review citations

On the evolution of structure in aminoacyl-tRNA synthetases.
O'Donoghue et al. (2003)
8 more

29 mentions without citation

Structural Biology for the Molecular Insight between Aptamers and Target Proteins.
Zhang et al. (2021)
28 more