PDBe 1vq1

X-ray diffraction
2.8Å resolution

Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) (TM0488) from Thermotoga maritima at 2.80 A resolution

Released:
Source organism: Thermotoga maritima MSB8
Entry author: Joint Center for Structural Genomics (JCSG)

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Release factor glutamine methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 33.35 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYV8 (Residues: 1-282; Coverage: 100%)
Gene names: TM_0488, prmC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: C2
Unit cell:
a: 140.973Å b: 58.611Å c: 85.667Å
α: 90° β: 109.46° γ: 90°
R-values:
R R work R free
0.212 0.208 0.273
Expression system: Escherichia coli