› 3bc8

X-ray diffraction
1.65Å resolution

Crystal structure of mouse selenocysteine synthase

Released:
DOI: 10.2210/pdb3bc8/pdb
PDB entry 3bc8 coloured by chain, front view.
PDB entry 3bc8 coloured by chain, side view.
PDB entry 3bc8 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure and catalytic mechanism of eukaryotic selenocysteine synthase.
Ganichkin OM, Xu XM, Carlson BA, Mix H, Hatfield DL, Gladyshev VN, Wahl MC
J Biol Chem 283 5849-65 (2008)
PMID: 18093968

Function and Biology Details

Reaction catalysed: 
O-phospho-L-seryl-tRNA(Sec) + selenophosphate + H(2)O = L-selenocysteinyl-tRNA(Sec) + 2 phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180132 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
O-phosphoseryl-tRNA(Sec) selenium transferase Chain: A
Molecule details ›
Chain: A
Length: 450 amino acids
Theoretical weight: 49.98 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6P6M7 (Residues: 19-468; Coverage: 89%)
Gene names: D5Ertd135e, Sepsecs
Sequence domains: O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CL 1 x CL
Ligand EDO 1 x EDO
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: I222
Unit cell:
a: 59.172Å b: 138.73Å c: 141.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.199
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Selenium in human health and disease.
Fairweather-Tait et al. (2011)
10 more