› 4d92

X-ray diffraction
2.22Å resolution

Salmonella typhimurium D-Cysteine desulfhydrase soaked with beta-chloro-D-alanine shows pyruvate bound 4 A away from active site

Released:
DOI: 10.2210/pdb4d92/pdb
PDB entry 4d92 coloured by chain, front view.
PDB entry 4d92 coloured by chain, side view.
PDB entry 4d92 coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase.
Bharath SR, Bisht S, Harijan RK, Savithri HS, Murthy MR
PLoS One 7 e36267 (2012)
PMID: 22574144

Function and Biology Details

Reaction catalysed: 
D-cysteine + H(2)O = H(2)S + NH(3) + pyruvate
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-187318 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-cysteine desulfhydrase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 342 amino acids
Theoretical weight: 36.78 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ZNT7 (Residues: 1-328; Coverage: 100%)
Gene names: STM1953, dcyD
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand BEN 3 x BEN
Ligand PYR 4 x PYR
Ligand SO4 4 x SO4
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 66.34Å b: 165.46Å c: 67.96Å
α: 90° β: 118.5° γ: 90°
R-values:
R R work R free
0.178 0.176 0.222
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Ethylene, ACC, and the Plant Growth-Promoting Enzyme ACC Deaminase.
Gamalero et al. (2023)
9 other articles

1 mention without citation

Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase.
Bharath et al. (2012)