› 1umy

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
Trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine
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-126721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Betaine--homocysteine S-methyltransferase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 407 amino acids
Theoretical weight: 45.06 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O09171 (Residues: 1-407; Coverage: 100%)
Gene name: Bhmt
Sequence domains: Homocysteine S-methyltransferase
Structure domains: Homocysteine-binding-like domain

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand BME 2 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 57.83Å b: 149.27Å c: 96.25Å
α: 90° β: 92.92° γ: 90°
R-values:
R R work R free
0.253 0.253 0.291
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Age-related cataracts: Role of unfolded protein response, Ca2+ mobilization, epigenetic DNA modifications, and loss of Nrf2/Keap1 dependent cytoprotection.
Periyasamy et al. (2017)
1 more

4 mentions without citation

Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase.
Szegedi et al. (2008)
3 more