X-ray diffraction
2.2Å resolution

N5-glutamine methyltransferase, HemK


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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Release factor glutamine methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 284 amino acids
Theoretical weight: 31.78 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
  • Canonical: Q9WYV8 (Residues: 1-282; Coverage: 100%)
Gene names: TM_0488, prmC
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand SAM 2 x SAM
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2
Unit cell:
a: 141.489Å b: 59.062Å c: 85.605Å
α: 90° β: 109.22° γ: 90°
R R work R free
0.19 0.186 0.253
Expression system: Escherichia coli