3QT3
Analysis of a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Clostridium perfringens CPE0426 apo-structure
Summary for 3QT3
Entry DOI | 10.2210/pdb3qt3/pdb |
Related | 3QT9 |
Descriptor | Putative uncharacterized protein CPE0426, 1,2-ETHANEDIOL (3 entities in total) |
Functional Keywords | alpha-alpha six fold, glycoside hydrolase, mannosidase, clostridium perfringens, hydrolase |
Biological source | Clostridium perfringens |
Total number of polymer chains | 1 |
Total formula weight | 50149.28 |
Authors | Gregg, K.J.,Zandberg, W.F.,Hehemann, J.-H.,Whitworth, G.E.,Deng, L.E.,Vocadlo, D.J.,Boraston, A.B. (deposition date: 2011-02-22, release date: 2011-03-09, Last modification date: 2024-02-21) |
Primary citation | Gregg, K.J.,Zandberg, W.F.,Hehemann, J.H.,Whitworth, G.E.,Deng, L.,Vocadlo, D.J.,Boraston, A.B. Analysis of a New Family of Widely Distributed Metal-independent {alpha}-Mannosidases Provides Unique Insight into the Processing of N-Linked Glycans. J.Biol.Chem., 286:15586-15596, 2011 Cited by PubMed: 21388958DOI: 10.1074/jbc.M111.223172 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
Download full validation report