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3QPF

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 apo-structure

Summary for 3QPF
Entry DOI10.2210/pdb3qpf/pdb
DescriptorPutative uncharacterized protein, 1,2-ETHANEDIOL (3 entities in total)
Functional Keywordsalpha-alpha six fold, glycoside hydrolase, mannosidase, streptococcus pneumoniae, hydrolase
Biological sourceStreptococcus pneumoniae
Total number of polymer chains2
Total formula weight99266.81
Authors
Gregg, K.J.,Zandberg, W.F.,Hehemann, J.-H.,Whitworth, G.E.,Deng, L.E.,Vocadlo, D.J. (deposition date: 2011-02-12, release date: 2011-03-09, Last modification date: 2024-02-21)
Primary citationGregg, 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: 21388958
DOI: 10.1074/jbc.M111.223172
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

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