› 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:
DOI: 10.2210/pdb1vq1/pdb
PDB entry 1vq1 coloured by chain, front view.
PDB entry 1vq1 coloured by chain, side view.
PDB entry 1vq1 coloured by chain, top view.
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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194552 (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


Cofactor: Ligand SAM 2 x SAM
No bound ligands
1 modified residue:
Ligand MSE 10 x MSE

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

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