4zu1

X-ray diffraction
2.2Å resolution

Crystal Structure of O-Acetylserine Sulfhydrylase from Haemophilus influenzae in complex with O-acetyl serine and peptide inhibitor

Released:
Entry authors: Ekka MK, Singh AK, 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)
PDBe Complex ID:
PDB-CPX-151581 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cysteine synthase Chain: X
Molecule details ›
Chain: X
Length: 332 amino acids
Theoretical weight: 35.46 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
Structure domains: Rossmann fold
Serine acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 10 amino acids
Theoretical weight: 1.18 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Not provided
UniProt:
  • Canonical: P29847 (Residues: 264-273; Coverage: 4%)
Gene names: STM3699, cysE

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I41
Unit cell:
a: 112.53Å b: 112.53Å c: 43.364Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.218 0.257
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided