› 1r8x

X-ray diffraction
2.95Å resolution

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

Released:
DOI: 10.2210/pdb1r8x/pdb
PDB entry 1r8x coloured by chain, front view.
PDB entry 1r8x coloured by chain, side view.
PDB entry 1r8x 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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193040 (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: 32.59 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

2 bound ligands:
Ligand BME 4 x BME
Ligand TRS 2 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS
Spacegroup: P41212
Unit cell:
a: 70.7Å b: 70.7Å c: 266.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.273
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

1 mention without citation

NHS-Esters As Versatile Reactivity-Based Probes for Mapping Proteome-Wide Ligandable Hotspots.
Ward et al. (2017)