Function and Biology Details
Reaction catalysed:
ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain
- Histidine-tRNA ligase
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit
- Anticodon-binding
- Histidyl-anticodon-binding
- Anticodon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class II
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Histidine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-158128 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine--tRNA ligase
Molecule details ›
Chains: A, B, C, D
Length: 423 amino acids
Theoretical weight: 46.95 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 423 amino acids
Theoretical weight: 46.95 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P60906 (Residues: 2-424; Coverage: 100%)
Sequence domains:
Structure domains:
