› 1xva

X-ray diffraction
2.2Å resolution

METHYLTRANSFERASE

Released:
DOI: 10.2210/pdb1xva/pdb
PDB entry 1xva coloured by chain, front view.
PDB entry 1xva coloured by chain, side view.
PDB entry 1xva coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of glycine N-methyltransferase from rat liver.
Fu Z, Hu Y, Konishi K, Takata Y, Ogawa H, Gomi T, Fujioka M, Takusagawa F
Biochemistry 35 11985-93 (1996)
PMID: 8810903

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: 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 2 x SAM
1 bound ligand:
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 86.4Å b: 175.7Å c: 45.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.262

Quick links

Citations

6 review citations

Bacterial tellurite resistance.
Taylor DE. (1999)
5 more

10 mentions without citation

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