› 1r8y

X-ray diffraction
3Å resolution

Crystal Structure of Mouse Glycine N-Methyltransferase (Monoclinic Form)

Released:
DOI: 10.2210/pdb1r8y/pdb
PDB entry 1r8y coloured by chain, front view.
PDB entry 1r8y coloured by chain, side view.
PDB entry 1r8y coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes.
Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME
Proteins 57 331-7 (2004)
PMID: 15340920

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 tetramer (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-193040 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine N-methyltransferase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 292 amino acids
Theoretical weight: 32.59 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9QXF8 (Residues: 2-293; Coverage: 100%)
Gene name: Gnmt
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand BME 10 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21
Unit cell:
a: 107.98Å b: 108.3Å c: 119.01Å
α: 90° β: 93.71° γ: 90°
R-values:
R R work R free
0.224 0.222 0.285
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

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