› 1d2c

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-146528 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 292 amino acids
Theoretical weight: 32.46 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P13255 (Residues: 2-293; Coverage: 100%)
Gene names: Fbp-cII, Gnmt
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 86.3Å b: 175.9Å c: 45.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.233
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Glycine N-methyltransferase and regulation of S-adenosylmethionine levels.
Luka et al. (2009)
3 more

3 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
2 more