2CBX
X-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with beta-D-erythrofuranosyl- adenosine
Summary for 2CBX
| Entry DOI | 10.2210/pdb2cbx/pdb |
| Related | 1RQP 1RQR 2C2W 2C4T 2C4U 2C5B 2C5H |
| Descriptor | 5'-FLUORO-5'-DEOXYADENOSINE SYNTHASE, BETA-D-ERYTHROFURANOSYL-ADENOSINE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | transferase, fluorinase, 5'-fluorodeoxyadenosine synthase, fla, inhibitor, aza, streptomyces cattleya, sam analogue |
| Biological source | STREPTOMYCES CATTLEYA |
| Total number of polymer chains | 3 |
| Total formula weight | 98744.96 |
| Authors | McEwan, A.R.,Cadicamo, C.D.,Deng, H.,McGlinchey, R.P.,Robinson, D.R.,O'Hagan, D.,Naismith, J.H.,Spencer, J. (deposition date: 2006-01-09, release date: 2007-03-06, Last modification date: 2023-12-13) |
| Primary citation | Cobb, S.L.,Deng, H.,McEwan, A.R.,Naismith, J.H.,O'Hagan, D.,Robinson, D.A. Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates. Org. Biomol. Chem., 4:1458-1460, 2006 Cited by PubMed Abstract: 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. PubMed: 16604208DOI: 10.1039/b600574h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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