› 4il5

X-ray diffraction
2.03Å resolution

Crystal structure of O-Acetyl Serine Sulfhydrylase from Entamoeba histolytica in complex with isoleucine

Released:
DOI: 10.2210/pdb4il5/pdb
PDB entry 4il5 coloured by chain, front view.
PDB entry 4il5 coloured by chain, side view.
PDB entry 4il5 coloured by chain, top view.
Source organism: Entamoeba histolytica
Primary publication:
Molecular basis of ligand recognition by OASS from E. histolytica: insights from structural and molecular dynamics simulation studies.
Raj I, Mazumder M, Gourinath S
Biochim Biophys Acta 1830 4573-83 (2013)
PMID: 23747298

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127538 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase beta chain-like PALP domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37 KDa
Source organism: Entamoeba histolytica
Expression system: Escherichia coli
UniProt:
  • Canonical: O15570 (Residues: 1-337; Coverage: 100%)
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand ILE 1 x ILE
Ligand SO4 1 x SO4
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P41
Unit cell:
a: 80.411Å b: 80.411Å c: 112.157Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.232
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

A consistent force field parameter set for zwitterionic amino acid residues.
Horn AH. (2014)
4 more

2 mentions without citation

Insights into multifaceted activities of CysK for therapeutic interventions.
Joshi et al. (2019)
1 more