1rfl

Solution NMR

NMR data driven structural model of G-domain of MnmE protein

Released:

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA modification GTPase MnmE Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 18.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P25522 (Residues: 210-377; Coverage: 37%)
Gene names: JW3684, b3706, mnmE, thdF, trmE
Sequence domains: 50S ribosome-binding GTPase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: NMR restraints were obtained from the backbone assignment (TALOS analysis for dihedral angle constraints) and from the 15N-edited 3D NOESY. Additional structural information was obtained from the homologous GTPAse protein structures.
Chemical shifts: BMR5861  
Expression system: Escherichia coli