1nbi

X-ray diffraction
3Å resolution

Structure of R175K mutated glycine N-methyltransferase complexed with S-adenosylmethionine, R175K:SAM.

Released:
Source organism: Rattus norvegicus
Primary publication:
Catalytic mechanism of glycine N-methyltransferase.
Biochemistry 42 8394-402 (2003)
PMID: 12859184

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-146529 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine N-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 292 amino acids
Theoretical weight: 32.43 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


Cofactor: Ligand SAM 4 x SAM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43
Unit cell:
a: 77.87Å b: 77.87Å c: 227.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.165 0.295
Expression system: Escherichia coli