PDBe 2z67

X-ray diffraction
2.5Å resolution

Crystal structure of archaeal O-phosphoseryl-tRNA(Sec) selenium transferase (SepSecS)


Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
O-phosphoseryl-tRNA(Sec) selenium transferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 456 amino acids
Theoretical weight: 51.15 KDa
Source organism: Methanococcus maripaludis S2
Expression system: Escherichia coli
  • Canonical: Q6LZM9 (Residues: 1-436; Coverage: 100%)
Gene names: MMP0595, spcS
Sequence domains: O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS
Structure domains: Type I PLP-dependent aspartate aminotransferase-like (Major domain)

Ligands and Environments

Cofactor: Ligand PLP 4 x PLP
1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 75.745Å b: 108.143Å c: 110.39Å
α: 90° β: 96.5° γ: 90°
R R work R free
0.208 0.208 0.27
Expression system: Escherichia coli