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PDBsum entry 4d8w

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protein ligands metals Protein-protein interface(s) links
Lyase PDB id
4d8w
Jmol
Contents
Protein chains
328 a.a.
Ligands
BEN ×3
PYR ×3
SO4 ×4
EDO ×2
Metals
_CL
Waters ×748
PDB id:
4d8w
Name: Lyase
Title: Salmonella typhimurium d-cysteine desulfhydrase soaked with shows pyruvate bound 4 a away from active site
Structure: D-cysteine desulfhydrase. Chain: a, b, c, d. Engineered: yes
Source: Salmonella typhimurium. Organism_taxid: 90371. Gene: dcyd, stm1953. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.01Å     R-factor:   0.185     R-free:   0.217
Authors: S.R.Bharath,B.Shveta,K.H.Rajesh,H.S.Savithri,M.R.N.Murthy
Key ref: S.R.Bharath et al. (2012). Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase. PLoS One, 7, e36267. PubMed id: 22574144
Date:
11-Jan-12     Release date:   30-May-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8ZNT7  (DCYD_SALTY) -  D-cysteine desulfhydrase
Seq:
Struc:
328 a.a.
328 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.4.4.1.15  - D-cysteine desulfhydrase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-cysteine + H2O = H2S + NH3 + pyruvate
D-cysteine
+ H(2)O
= H(2)S
+ NH(3)
+
pyruvate
Bound ligand (Het Group name = PYR)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     D-amino acid metabolic process   1 term 
  Biochemical function     catalytic activity     3 terms  

 

 
    Added reference    
 
 
PLoS One 7:e36267 (2012)
PubMed id: 22574144  
 
 
Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase.
S.R.Bharath, S.Bisht, R.K.Harijan, H.S.Savithri, M.R.Murthy.
 
  ABSTRACT  
 
No abstract given.