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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 DOI10.2210/pdb3qt3/pdb
Related3QT9
DescriptorPutative uncharacterized protein CPE0426, 1,2-ETHANEDIOL (3 entities in total)
Functional Keywordsalpha-alpha six fold, glycoside hydrolase, mannosidase, clostridium perfringens, hydrolase
Biological sourceClostridium perfringens
Total number of polymer chains1
Total formula weight50149.28
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 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 (2.35 Å)
Structure validation

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