› 4d8u

X-ray diffraction
3.3Å resolution

Crystal structure of D-Cysteine desulfhydrase from Salmonella typhimurium at 3.3 A in monoclinic space group with 8 subunits in the asymmetric unit

Released:
DOI: 10.2210/pdb4d8u/pdb
PDB entry 4d8u coloured by chain, front view.
PDB entry 4d8u coloured by chain, side view.
PDB entry 4d8u 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, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
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

1 bound ligand:
Ligand PO4 8 x PO4
1 modified residue:
Ligand LLP 8 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: C2
Unit cell:
a: 181.463Å b: 158.14Å c: 181.925Å
α: 90° β: 94.1° γ: 90°
R-values:
R R work R free
0.248 0.246 0.275
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)