Function and Biology Details
Reaction catalysed:
ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Aspartyl/Asparaginyl-tRNA synthetase, class IIb
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Asparagine-tRNA ligase
- Nucleic acid-binding, OB-fold
- Aminoacyl-tRNA synthetase, class II
- Aminoacyl-tRNA synthetase, class II (D/K/N)
- OB-fold nucleic acid binding domain, AA-tRNA synthetase-type
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Asparagine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-129652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Asparagine--tRNA ligase
Molecule details ›
Chain: A
Length: 434 amino acids
Theoretical weight: 50.23 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 434 amino acids
Theoretical weight: 50.23 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
- Canonical:
O57980 (Residues: 1-434; Coverage: 100%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL26B1
Spacegroup:
C2
Expression system: Escherichia coli
