› 1inn

X-ray diffraction
1.8Å 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: 18.72 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RRU8 (Residues: 2-158; Coverage: 99%)
Gene names: DR_2387, luxS
Sequence domains: S-Ribosylhomocysteinase (LuxS)
Structure domains: S-ribosylhomocysteinase (LuxS)

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand MET 1 x MET
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21
Unit cell:
a: 43.78Å b: 82.26Å c: 49.52Å
α: 90° β: 102.79° γ: 90°
R-values:
R R work R free
0.209 0.206 0.24
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Making 'sense' of metabolism: autoinducer-2, LuxS and pathogenic bacteria.
Vendeville et al. (2005)
11 more

3 mentions without citation

Structural features and functional implications of proteins enabling the robustness of Deinococcus radiodurans.
Chen et al. (2020)
2 more