› 1mea

Solution NMR

METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS

Released:
DOI: 10.2210/pdb1mea/pdb
PDB entry 1mea coloured by chain, front view.
PDB entry 1mea coloured by chain, side view.
PDB entry 1mea coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins.
Fourmy D, Dardel F, Blanquet S
J Mol Biol 231 1078-89 (1993)
PMID: 8515466

Function and Biology Details

Reaction catalysed: 
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 28 amino acids
Theoretical weight: 2.97 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P00959 (Residues: 139-164; Coverage: 4%)
Gene names: JW2101, b2114, metG

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

4 review citations

Aminoacyl-tRNA synthesis.
Ibba et al. (2000)
3 more

8 mentions without citation

DNA repair by reversal of DNA damage.
Yi et al. (2013)
7 more