› 6n2h

X-ray diffraction
1.72Å resolution

Function and Biology Details

Reaction catalysed: 
D-lysine = cadaverine + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187297 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-ornithine/D-lysine decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 477 amino acids
Theoretical weight: 54.29 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8ZNC4 (Residues: 1-465; Coverage: 100%)
Gene names: STM2360, dokD
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand DMS 2 x DMS
Ligand DIO 6 x DIO
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 133.74Å b: 52.28Å c: 86.7Å
α: 90° β: 127.6° γ: 90°
R-values:
R R work R free
0.165 0.164 0.193
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Oxygen reactivity with pyridoxal 5'-phosphate enzymes: biochemical implications and functional relevance.
Bisello et al. (2020)
4 other articles

2 mentions without citation

Protein-Ligand Interactions in Scarcity: The Stringent Response from Bacteria to Metazoa, and the Unanswered Questions.
Barik S. (2023)
1 more