Function and Biology Details
Reaction catalysed:
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proline-tRNA ligase, class IIa
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Anticodon-binding
- Proline--tRNA ligase, anticodon binding domain
- Anticodon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
- Aminoacyl-tRNA synthetase, class II
- Prokaryote proline-tRNA ligase core domain
2 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Proline--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-179965 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline--tRNA ligase
Molecule details ›
Chains: A, B, C
Length: 458 amino acids
Theoretical weight: 51.55 KDa
Source organism: Rhodopseudomonas palustris
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 458 amino acids
Theoretical weight: 51.55 KDa
Source organism: Rhodopseudomonas palustris
Expression system: Escherichia coli
UniProt:
- Canonical:
Q6N5P6 (Residues: 1-438; Coverage: 100%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-1, ESRF BEAMLINE ID29
Spacegroup:
C2221
Expression system: Escherichia coli
