5NGW
 
 | | Glycoside hydrolase-like protein | | Descriptor: | BROMIDE ION, OpGH99A | | Authors: | Robb, C.S, Hehemann, J.-H. | | Deposit date: | 2017-03-20 | | Release date: | 2018-01-31 | | Last modified: | 2024-01-17 | | Method: | X-RAY DIFFRACTION (2.4 Å) | | Cite: | Crystal structure of a marine glycoside hydrolase family 99-related protein lacking catalytic machinery.
Protein Sci., 26, 2017
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3QRY
 | | 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 1-deoxymannojirimycin complex | | Descriptor: | 1,2-ETHANEDIOL, 1-DEOXYMANNOJIRIMYCIN, Putative uncharacterized protein | | Authors: | Gregg, K.J, Zandberg, W.F, Hehemann, J.-H, Whitworth, G.E, Deng, L.E, Vocadlo, D.J, Boraston, A.B. | | Deposit date: | 2011-02-18 | | Release date: | 2011-03-09 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (1.75 Å) | | Cite: | 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, 2011
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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 | | Descriptor: | 1,2-ETHANEDIOL, Putative uncharacterized protein | | Authors: | Gregg, K.J, Zandberg, W.F, Hehemann, J.-H, Whitworth, G.E, Deng, L.E, Vocadlo, D.J. | | Deposit date: | 2011-02-12 | | Release date: | 2011-03-09 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (2.15 Å) | | Cite: | 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, 2011
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3QT9
 | | 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 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose | | Descriptor: | 1,2-ETHANEDIOL, Putative uncharacterized protein CPE0426, alpha-D-mannopyranose-(1-6)-6-thio-alpha-D-mannopyranose | | Authors: | Gregg, K.J, Zandberg, W.F, Hehemann, J.-H, Whitworth, G.E, Deng, L.E, Vocadlo, D.J, Boraston, A.B. | | Deposit date: | 2011-02-22 | | Release date: | 2011-03-09 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (2.05 Å) | | Cite: | 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, 2011
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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 | | Descriptor: | 1,2-ETHANEDIOL, Putative uncharacterized protein CPE0426 | | Authors: | Gregg, K.J, Zandberg, W.F, Hehemann, J.-H, Whitworth, G.E, Deng, L.E, Vocadlo, D.J, Boraston, A.B. | | Deposit date: | 2011-02-22 | | Release date: | 2011-03-09 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (2.35 Å) | | Cite: | 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, 2011
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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 | | Descriptor: | 1,2-ETHANEDIOL, Putative uncharacterized protein, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose | | Authors: | Gregg, K.J, Zandberg, W.F, Hehemann, J.-H, Whitworth, G.E, Deng, L.E, Vocadlo, D.J, Boraston, A.B. | | Deposit date: | 2011-02-21 | | Release date: | 2011-03-09 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (2.1 Å) | | Cite: | 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, 2011
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