› 1lt7

X-ray diffraction
2.15Å resolution

Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions

Released:
DOI: 10.2210/pdb1lt7/pdb
PDB entry 1lt7 coloured by chain, front view.
PDB entry 1lt7 coloured by chain, side view.
PDB entry 1lt7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Betaine-homocysteine methyltransferase: zinc in a distorted barrel.
Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML
Structure 10 1159-71 (2002)
PMID: 12220488

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187979 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Betaine--homocysteine S-methyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 406 amino acids
Theoretical weight: 44.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93088 (Residues: 1-406; Coverage: 100%)
Gene name: BHMT
Sequence domains: Homocysteine S-methyltransferase
Structure domains: Homocysteine-binding-like domain

Ligands and Environments

2 bound ligands:
Ligand SM 4 x SM
Ligand CIT 2 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: C2
Unit cell:
a: 109.99Å b: 90.085Å c: 89.085Å
α: 90° β: 122.1° γ: 90°
R-values:
R R work R free
0.218 0.203 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

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

4 mentions without citation

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