X-ray diffraction
2.59Å resolution

Crystal Structure of O-Acetylserine Sulfhydrylase from Haemophilus influenzae in complex with high affinity inhibitory peptide from Serine acetyl transferase of Salmonella typhimurium

Entry authors: Singh AK, Ekka MK, Kaushik A, Kumaran S

Function and Biology Details

Reactions catalysed:
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cysteine synthase Chain: X
Molecule details ›
Chain: X
Length: 316 amino acids
Theoretical weight: 33.65 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
  • Canonical: P45040 (Residues: 1-316; Coverage: 100%)
Gene names: HI_1103, cysK
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold
Serine acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 8 amino acids
Theoretical weight: 901 Da
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. UK-1
Expression system: Not provided
  • Canonical: P29847 (Residues: 266-273; Coverage: 3%)
Gene names: STM3699, cysE

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I41
Unit cell:
a: 112.655Å b: 112.655Å c: 46.535Å
α: 90° β: 90° γ: 90°
R R work R free
0.2 0.197 0.248
Expression systems:
  • Escherichia coli
  • Not provided