› 1d6s

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF THE K41A MUTANT OF O-ACETYLSERINE SULFHYDRYLASE COMPLEXED IN EXTERNAL ALDIMINE LINKAGE WITH METHIONINE

Released:
DOI: 10.2210/pdb1d6s/pdb
PDB entry 1d6s coloured by chain, front view.
PDB entry 1d6s coloured by chain, side view.
PDB entry 1d6s coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium.
Burkhard P, Tai CH, Ristroph CM, Cook PF, Jansonius JN
J Mol Biol 291 941-53 (1999)
PMID: 10452898

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140983 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine synthase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 34.41 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A1E3 (Residues: 2-323; Coverage: 100%)
Gene names: STM2430, cysK
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
Ligand MET 2 x MET
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-20
Spacegroup: P21212
Unit cell:
a: 96.94Å b: 149.93Å c: 53.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 0.223
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor protein.
Banerjee et al. (2005)
6 more

4 mentions without citation

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