› 1ecx

X-ray diffraction
2.7Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194855 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cysteine desulfurase Chains: A, B
Molecule details ›
Chains: A, B
Length: 384 amino acids
Theoretical weight: 42.93 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X218 (Residues: 1-384; Coverage: 100%)
Gene name: TM_1692
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 115.41Å b: 115.41Å c: 156.95Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.207 0.256
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Structure, function, and formation of biological iron-sulfur clusters.
Johnson et al. (2005)
19 more

6 mentions without citation

The evolutionary history of Cys-tRNACys formation.
O'Donoghue et al. (2005)
5 more