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 superfamily
- Phenylalanyl tRNA synthetase beta chain, core domain
- B3/B4 tRNA-binding domain
- Nucleic acid-binding, OB-fold
- tRNA-binding domain
- Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type
12 more domains
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Phenylalanine--tRNA ligase and tRNA (preferred)
PDBe Complex ID:
PDB-CPX-161428 (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 ›
Chains: A, D
Length: 341 amino acids
Theoretical weight: 37.42 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 341 amino acids
Theoretical weight: 37.42 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P9WFU3 (Residues: 1-341; Coverage: 100%)
Sequence domains:
Phenylalanine--tRNA ligase beta subunit
Molecule details ›
Chains: B, E
Length: 835 amino acids
Theoretical weight: 88.87 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 835 amino acids
Theoretical weight: 88.87 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P9WFU1 (Residues: 1-831; Coverage: 100%)
Sequence domains:
