› 6o10

X-ray diffraction
2Å resolution

Function and Biology Details

Reactions catalysed: 
(1a) L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160167 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine desulfurase Chain: A
Molecule details ›
Chain: A
Length: 406 amino acids
Theoretical weight: 44.48 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P77444 (Residues: 1-406; Coverage: 100%)
Gene names: JW1670, b1680, csdB, sufS, ynhB
Sequence domains: Aminotransferase class-V

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P43212
Unit cell:
a: 126.4Å b: 126.4Å c: 133.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Fe-S cluster biogenesis by the bacterial Suf pathway.
Blahut et al. (2020)
1 more

2 mentions without citation

Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues.
Blahut et al. (2019)
1 more