› 2jc3

X-ray diffraction
2.3Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151583 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine synthase B Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 303 amino acids
Theoretical weight: 32.68 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P29848 (Residues: 1-303; Coverage: 100%)
Gene names: STM2440, cysM
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 8 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P1
Unit cell:
a: 103.052Å b: 106.948Å c: 112.107Å
α: 95.59° β: 90.06° γ: 117.61°
R-values:
R R work R free
0.213 0.213 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Controlling reaction specificity in pyridoxal phosphate enzymes.
Toney MD. (2011)
2 more

3 mentions without citation

Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target.
Spyrakis et al. (2013)
2 more