3VPS
Structure of a novel NAD dependent-NDP-hexosamine 5,6-dehydratase, TunA, involved in tunicamycin biosynthesis
Summary for 3VPS
Entry DOI | 10.2210/pdb3vps/pdb |
Descriptor | NAD-dependent epimerase/dehydratase, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total) |
Functional Keywords | tunicamycins, biosynthesis, exo-glycal, dehydratase, rossmann fold, transferase |
Biological source | Streptomyces chartreusis |
Total number of polymer chains | 2 |
Total formula weight | 72907.21 |
Authors | Wyszynski, F.J.,Lee, S.S.,Yabe, T.,Wang, H.,Gomez-Escribano, J.P.,Bibb, M.J.,Lee, S.J.,Davies, G.J.,Davis, B.G. (deposition date: 2012-03-12, release date: 2012-04-18, Last modification date: 2024-03-20) |
Primary citation | Wyszynski, F.J.,Lee, S.S.,Yabe, T.,Wang, H.,Gomez-Escribano, J.P.,Bibb, M.J.,Lee, S.J.,Davies, G.J.,Davis, B.G. Biosynthesis of nucleoside antibiotic tunicamycin proceeds via unique exo-glycal intermediates To be published, |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report![Download](/newweb/media/icons/dl.png)
![Download](/newweb/media/icons/dl.png)