3qt3: Difference between revisions
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{{STRUCTURE_3qt3| PDB=3qt3 | SCENE= }} | {{STRUCTURE_3qt3| PDB=3qt3 | SCENE= }} | ||
===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=== | ===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=== | ||
{{ABSTRACT_PUBMED_21388958}} | {{ABSTRACT_PUBMED_21388958}} | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:021388958</ref><references group="xtra"/> | <ref group="xtra">PMID:021388958</ref><references group="xtra"/><references/> | ||
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
[[Category: Boraston, A B.]] | [[Category: Boraston, A B.]] | ||
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[[Category: Whitworth, G E.]] | [[Category: Whitworth, G E.]] | ||
[[Category: Zandberg, W F.]] | [[Category: Zandberg, W F.]] | ||
[[Category: Alpha-alpha six fold]] | |||
[[Category: Clostridium perfringen]] | |||
[[Category: Glycoside hydrolase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Mannosidase]] |
Revision as of 11:20, 8 May 2013
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-structureAnalysis 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
Template:ABSTRACT PUBMED 21388958
About this StructureAbout this Structure
3qt3 is a 1 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Gregg KJ, Zandberg WF, Hehemann JH, Whitworth GE, Deng L, Vocadlo DJ, Boraston AB. Analysis of new family of widely distributed metal-independent {alpha}-mannosidases provides unique insight into the processing of N-linked glycans. J Biol Chem. 2011 Mar 9. PMID:21388958 doi:10.1074/jbc.M111.223172