3a9x

X-ray diffraction
2Å resolution

Crystal structure of rat selenocysteine lyase

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Selenocysteine lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 432 amino acids
Theoretical weight: 47.31 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q68FT9 (Residues: 1-432; Coverage: 100%)
Gene name: Scly
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P212121
Unit cell:
a: 54.445Å b: 102.771Å c: 197.753Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.236
Expression system: Escherichia coli