3QSP
Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose
Summary for 3QSP
Entry DOI | 10.2210/pdb3qsp/pdb |
Related | 3QPF 3QRY |
Descriptor | Putative uncharacterized protein, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | alpha-alpha six fold, glycoside hydrolase, mannosidase, hydrolase |
Biological source | Streptococcus pneumoniae |
Total number of polymer chains | 2 |
Total formula weight | 99268.66 |
Authors | Gregg, K.J.,Zandberg, W.F.,Hehemann, J.-H.,Whitworth, G.E.,Deng, L.E.,Vocadlo, D.J.,Boraston, A.B. (deposition date: 2011-02-21, 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 (2.1 Å) |
Structure validation
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