3spx

X-ray diffraction
1.79Å resolution

Crystal structure of O-Acetyl Serine Sulfhydrylase from Leishmania donovani

Released:

Function and Biology Details

Reaction catalysed:
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-124171 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase beta chain-like PALP domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 35.91 KDa
Source organism: Leishmania donovani
Expression system: Escherichia coli
UniProt:
  • Canonical: G1C2I2 (Residues: 1-325; Coverage: 100%)
Gene name: OASS
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21212
Unit cell:
a: 115.266Å b: 61.974Å c: 43.427Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.216
Expression system: Escherichia coli