7yom

X-ray diffraction
2.8Å resolution

Crystal structure of tetra mutant (D67E,A68P,L98I,A301S) of O-acetylserine sulfhydrylase from Salmonella typhimurium in complex with high-affinity inhibitory peptide from serine acetyltransferase of Salmonella typhimurium at 2.8 A

Released:
Entry authors: Saini N, Kumar N, Rahisuddin R, Singh AK

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-223790 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cysteine synthase Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 33.71 KDa
Source organism: Haemophilus influenzae Rd KW20
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P45040 (Residues: 1-316; Coverage: 100%)
Gene names: HI_1103, cysK
Sequence domains: Pyridoxal-phosphate dependent enzyme
peptide from serine acetyltransferase Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 901 Da
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I41
Unit cell:
a: 113.14Å b: 113.14Å c: 43.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.272
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided