› 3gzd

X-ray diffraction
1.8Å 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

Assemblies composition:
homo dimer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188540 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Selenocysteine lyase Chains: A, B, D
Molecule details ›
Chains: A, B, D
Length: 440 amino acids
Theoretical weight: 47.82 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:
Selenocysteine lyase Chain: C
Molecule details ›
Chain: C
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 4 x PLR
1 bound ligand:
Ligand NO3 4 x NO3
1 modified residue:
Ligand CSS 3 x CSS

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P1
Unit cell:
a: 66.64Å b: 72.2Å c: 89.43Å
α: 83.91° β: 68.39° γ: 86.96°
R-values:
R R work R free
0.185 0.184 0.217
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

3 mentions without citation

A machine learning-based chemoproteomic approach to identify drug targets and binding sites in complex proteomes.
Piazza et al. (2020)
2 more