2azt

X-ray diffraction
2.7Å resolution

Crystal structure of H176N mutant of human Glycine N-Methyltransferase

Released:
Source organism: Homo sapiens

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-172093 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 32.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14749 (Residues: 1-295; Coverage: 100%)
Gene name: GNMT
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21212
Unit cell:
a: 76.116Å b: 83.279Å c: 115.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.236 0.282
Expression system: Escherichia coli BL21(DE3)