Function and Biology Details
Reaction catalysed:
ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Ferrodoxin-fold anticodon-binding domain superfamily
- Phenylalanyl-tRNA synthetase
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Ferrodoxin-fold anticodon-binding domain
- Phenylalanyl-tRNA synthetase, class IIc, mitochondrial
- Aminoacyl-tRNA synthetase, class II
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Phenylalanine--tRNA ligase, mitochondrial (preferred)
PDBe Complex ID:
PDB-CPX-131898 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine--tRNA ligase, mitochondrial
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 47.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 405 amino acids
Theoretical weight: 47.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O95363 (Residues: 47-451; Coverage: 90%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID23-1
Spacegroup:
P212121
Expression system: Escherichia coli
