› 1o58

X-ray diffraction
1.8Å 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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194598 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 303 amino acids
Theoretical weight: 32.63 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZD3 (Residues: 1-291; Coverage: 100%)
Gene name: TM_0665
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand PO4 8 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 67.57Å b: 84.59Å c: 107.22Å
α: 90° β: 95.39° γ: 90°
R-values:
R R work R free
0.159 0.157 0.198
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
11 other articles

2 mentions without citation

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