› 3gzc

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188541 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Selenocysteine lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 440 amino acids
Theoretical weight: 47.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96I15 (Residues: 8-445; Coverage: 98%)
Gene names: SCL, SCLY
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments


Cofactor: Ligand PLR 2 x PLR
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 59.218Å b: 85.813Å c: 188.578Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.179 0.235
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Selenoproteins: molecular pathways and physiological roles.
Labunskyy et al. (2014)
2 more

5 mentions without citation

Selenocysteine β-Lyase: Biochemistry, Regulation and Physiological Role of the Selenocysteine Decomposition Enzyme.
Seale LA. (2019)
4 more