PDBe 2b3t

X-ray diffraction
3.1Å resolution

Structure of complex between E. coli translation termination factor RF1 and the PrmC methyltransferase


Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptide chain release factor RF1 Chain: B
Molecule details ›
Chain: B
Length: 360 amino acids
Theoretical weight: 40.56 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P0A7I0 (Residues: 1-360; Coverage: 100%)
Gene names: JW1202, b1211, prfA, sueB, uar
Sequence domains:
Structure domains:
Release factor glutamine methyltransferase Chain: A

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21212
Unit cell:
a: 113.54Å b: 77.47Å c: 89.49Å
α: 90° β: 90° γ: 90°
R R work R free
0.244 0.244 0.303
Expression system: Escherichia coli