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:
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- tRNA synthetase, B5-domain
- Ferrodoxin-fold anticodon-binding domain
- Ferrodoxin-fold anticodon-binding domain superfamily
- Phenylalanyl tRNA synthetase beta chain, core domain
- B3/B4 tRNA-binding domain
- tRNA-binding domain
- Nucleic acid-binding, OB-fold
12 more domains
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Phenylalanine--tRNA ligase and RNA (preferred)
PDBe Complex ID:
PDB-CPX-177826 (preferred)
Entry contents:
2 distinct polypeptide molecules
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (3 distinct):
Phenylalanine--tRNA ligase alpha subunit
Molecule details ›
Chain: A
Length: 350 amino acids
Theoretical weight: 39.31 KDa
Source organism: Thermus thermophilus HB8
UniProt:
Sequence domains:
Structure domains: Bira Bifunctional Protein; Domain 2
Length: 350 amino acids
Theoretical weight: 39.31 KDa
Source organism: Thermus thermophilus HB8
UniProt:
- Canonical:
Q5SGX2 (Residues: 1-350; Coverage: 100%)
Sequence domains:
Structure domains: Bira Bifunctional Protein; Domain 2
Phenylalanine--tRNA ligase beta subunit
Molecule details ›
Chain: B
Length: 785 amino acids
Theoretical weight: 86.72 KDa
Source organism: Thermus thermophilus HB8
UniProt:
Sequence domains:
Length: 785 amino acids
Theoretical weight: 86.72 KDa
Source organism: Thermus thermophilus HB8
UniProt:
- Canonical: Q5SGX1 (Residues: 1-785; Coverage: 100%)
Sequence domains:
- B3/4 domain
- tRNA synthetase B5 domain
- Phenylalanyl tRNA synthetase beta chain CLM domain
- Ferredoxin-fold anticodon binding domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RU200
Spacegroup:
P3221
