› 1r74

X-ray diffraction
2.55Å resolution

Crystal Structure of Human Glycine N-Methyltransferase

Released:
DOI: 10.2210/pdb1r74/pdb
PDB entry 1r74 coloured by chain, front view.
PDB entry 1r74 coloured by chain, side view.
PDB entry 1r74 coloured by chain, top view.
Source organism: Homo sapiens
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-172093 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 32.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14749 (Residues: 2-295; Coverage: 100%)
Gene name: GNMT
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 75.84Å b: 83.23Å c: 114.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.222 0.266
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

5 mentions without citation

Discovery of SARS-CoV-2 Nsp14 and Nsp16 Methyltransferase Inhibitors by High-Throughput Virtual Screening.
Bobrovs et al. (2021)
4 more