› 2idj

X-ray diffraction
2.35Å resolution

Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form

Released:
DOI: 10.2210/pdb2idj/pdb
PDB entry 2idj coloured by chain, front view.
PDB entry 2idj coloured by chain, side view.
PDB entry 2idj coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
5-methyltetrahydrofolate is bound in intersubunit areas of rat liver folate-binding protein glycine N-methyltransferase.
Luka Z, Pakhomova S, Loukachevitch LV, Egli M, Newcomer ME, Wagner C
J Biol Chem 282 4069-75 (2007)
PMID: 17158459

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 BL21(DE3)
UniProt:
  • Canonical: P13255 (Residues: 2-293; Coverage: 100%)
Gene names: Fbp-cII, Gnmt
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21
Unit cell:
a: 57.869Å b: 85.223Å c: 131.861Å
α: 90° β: 91.4° γ: 90°
R-values:
R R work R free
0.222 0.222 0.272
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Glycine N-methyltransferase and regulation of S-adenosylmethionine levels.
Luka et al. (2009)
2 more

1 mention without citation

Markov models of amino acid substitution to study proteins with intrinsically disordered regions.
Szalkowski et al. (2011)