Function and Biology Details
Reaction catalysed:
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Tyrosine-tRNA ligase
- Aminoacyl-tRNA synthetase, class I, conserved site
- Aminoacyl-tRNA synthetase, class Ic
- Tyrosine-tRNA ligase, bacterial-type, type 1
- Tyrosine-tRNA ligase, bacterial-type
- Rossmann-like alpha/beta/alpha sandwich fold
- RNA-binding S4 domain
- Tyrosine--tRNA ligase SYY-like, C-terminal domain
1 more domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Tyrosine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-101374 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine--tRNA ligase
Molecule details ›
Chain: A
Length: 425 amino acids
Theoretical weight: 47.4 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 425 amino acids
Theoretical weight: 47.4 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
Expression system: Escherichia coli
UniProt:
- Canonical:
A0A0H2UKY9 (Residues: 3-425; Coverage: 100%)
Sequence domains:
Structure domains:
Tyrosine--tRNA ligase
Molecule details ›
Chain: B
Length: 394 amino acids
Theoretical weight: 43.53 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
Expression system: Escherichia coli
UniProt:
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:
Length: 394 amino acids
Theoretical weight: 43.53 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
Expression system: Escherichia coli
UniProt:
- Canonical: A0A0H2UKZ0 (Residues: 3-394; Coverage: 100%)
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:
