› 1vgx

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
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-193248 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-ribosylhomocysteine lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 166 amino acids
Theoretical weight: 18.42 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RRU8 (Residues: 1-158; Coverage: 100%)
Gene names: DR_2387, luxS
Sequence domains: S-Ribosylhomocysteinase (LuxS)
Structure domains: S-ribosylhomocysteinase (LuxS)

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P1
Unit cell:
a: 42.22Å b: 42.86Å c: 49.354Å
α: 103.19° β: 90.55° γ: 114.32°
R-values:
R R work R free
0.171 0.171 0.216
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more

1 mention without citation

Exploring interfacial dynamics in homodimeric S-ribosylhomocysteine lyase (LuxS) from Vibrio cholerae through molecular dynamics simulations.
Bux et al. (2021)