› 1bhj

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)

Released:
DOI: 10.2210/pdb1bhj/pdb
PDB entry 1bhj coloured by chain, front view.
PDB entry 1bhj coloured by chain, side view.
PDB entry 1bhj coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of apo-glycine N-methyltransferase (GNMT).
Pattanayek R, Newcomer ME, Wagner C
Protein Sci 7 1326-31 (1998)
PMID: 9655336

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-146529 (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 BL21(DE3)
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 RUH2R
Spacegroup: P21212
Unit cell:
a: 85.39Å b: 174.21Å c: 44.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.318
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Glycine N-methyltransferase and regulation of S-adenosylmethionine levels.
Luka et al. (2009)
13 other articles

5 mentions without citation

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