› 1nbh

X-ray diffraction
2.8Å resolution

Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate, GNMT:SAM:Ace

Released:
DOI: 10.2210/pdb1nbh/pdb
PDB entry 1nbh coloured by chain, front view.
PDB entry 1nbh coloured by chain, side view.
PDB entry 1nbh coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Catalytic mechanism of glycine N-methyltransferase.
Takata Y, Huang Y, Komoto J, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F
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:
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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 292 amino acids
Theoretical weight: 32.46 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
1 bound ligand:
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 90.05Å b: 117.01Å c: 137.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.203 0.278
Expression system: Escherichia coli

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Citations

8 review citations

Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine.
Stipanuk MH. (2004)
7 more

8 mentions without citation

Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase.
De la Peña et al. (2007)
7 more