› 3a9z

X-ray diffraction
1.55Å resolution

Crystal structure of ras selenocysteine lyase in complex with selenopropionate

Released:
DOI: 10.2210/pdb3a9z/pdb
PDB entry 3a9z coloured by chain, front view.
PDB entry 3a9z coloured by chain, side view.
PDB entry 3a9z coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.
Omi R, Kurokawa S, Mihara H, Hayashi H, Goto M, Miyahara I, Kurihara T, Hirotsu K, Esaki N
J Biol Chem 285 12133-9 (2010)
PMID: 20164179

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-179343 (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
2 bound ligands:
Ligand SLP 2 x SLP
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32B2
Spacegroup: P212121
Unit cell:
a: 55.416Å b: 101.206Å c: 197.356Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.209
Expression system: Escherichia coli

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Citations

6 review citations

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

1 mention without citation

Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.
Omi et al. (2010)