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:
- WHEP-TRS domain
- 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)
- Anticodon-binding
- Histidyl-anticodon-binding
- Anticodon-binding domain superfamily
- Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit
2 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Histidine--tRNA ligase, cytoplasmic (preferred)
PDBe Complex ID:
PDB-CPX-146096 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine--tRNA ligase, cytoplasmic
Molecule details ›
Chains: A, B
Length: 517 amino acids
Theoretical weight: 58.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 517 amino acids
Theoretical weight: 58.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P12081 (Residues: 1-506; Coverage: 99%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRF BEAMLINE BL17U
Spacegroup:
P41212
Expression system: Escherichia coli BL21(DE3)
