Function and Biology Details
Reaction catalysed:
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Methioninyl-tRNA synthetase core domain
- Methionyl-tRNA synthetase, anticodon-binding domain
- Methionyl/Leucyl tRNA synthetase
- Methionine-tRNA synthetase, type 2
- Aminoacyl-tRNA synthetase, class Ia, anticodon-binding
- Aminoacyl-tRNA synthetase, class I, conserved site
- Methionyl-tRNA synthetase
- Rossmann-like alpha/beta/alpha sandwich fold
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Methionine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-107730 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine--tRNA ligase
Molecule details ›
Chains: A, B
Length: 535 amino acids
Theoretical weight: 60.25 KDa
Source organism: Mycobacterium tuberculosis H37Ra
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 535 amino acids
Theoretical weight: 60.25 KDa
Source organism: Mycobacterium tuberculosis H37Ra
Expression system: Escherichia coli
UniProt:
- Canonical:
A5U150 (Residues: 1-519; Coverage: 100%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SLS BEAMLINE X06DA
Spacegroup:
P1
Expression system: Escherichia coli
