PDBsum entry 2c4u

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Transferase PDB id
Protein chains
(+ 0 more) 291 a.a. *
GOL ×11
Waters ×409
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of the apo form of the 5'-fluoro-5'- deoxyadenosine synthase enzyme from streptomyces cattleya
Structure: 5'-fluoro-5'-deoxyadenosine synthase. Chain: a, b, c, d, e, f. Engineered: yes. Other_details: apo form
Source: Streptomyces cattleya. Organism_taxid: 29303. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: de3.
Biol. unit: Hexamer (from PDB file)
2.50Å     R-factor:   0.218     R-free:   0.273
Authors: A.R.Mcewan,H.Deng,D.A.Robinson,W.Delaurentis,R.P.Mcglinchey, D.O'Hagan,J.H.Naismith
Key ref: S.L.Cobb et al. (2006). Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates. Org Biomol Chem, 4, 1458-1460. PubMed id: 16604208
22-Oct-05     Release date:   12-Apr-06    
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Protein chains
Pfam   ArchSchema ?
Q70GK9  (Q70GK9_STRCT) -  5'-fluoro-5'-deoxy-adenosine synthase
299 a.a.
291 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Adenosyl-fluoride synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine
+ fluoride
= 5'-deoxy-5'-fluoroadenosine
+ L-methionine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity     2 terms  


    Added reference    
Org Biomol Chem 4:1458-1460 (2006)
PubMed id: 16604208  
Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates.
S.L.Cobb, H.Deng, A.R.McEwan, J.H.Naismith, D.O'Hagan, D.A.Robinson.
The fluorinase enzyme from Streptomyces cattleya displays an unusual ability in biocatalysis in that it forms a C-F bond. We now report that the enzyme will accept 2'-deoxyadenosine in place of adenosine substrates, and structural evidence reveals a reorganisation in hydrogen bonding to accommodate this substrate series. It emerges from this study that the enzyme does not require a planar ribose conformation of the substrate to catalyse C-F bond formation.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20354314 P.C.Kline, H.Zhao, B.C.Noll, A.G.Oliver, and A.S.Serianni (2010).
  Acta Crystallogr C, 66, o215-o218.  
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