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1x9d
From Proteopedia
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===Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue=== | ===Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1x9d]] is a 1 chain structure of [[Mannosidase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9D OCA]. | |
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| + | ==See Also== | ||
| + | *[[Mannosidase|Mannosidase]] | ||
| + | *[[Molecular Playground/ERMan1|Molecular Playground/ERMan1]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015713668</ref><references group="xtra"/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mannosyl-oligosaccharide 1,2-alpha-mannosidase]] | [[Category: Mannosyl-oligosaccharide 1,2-alpha-mannosidase]] | ||
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[[Category: Wang, B C.]] | [[Category: Wang, B C.]] | ||
[[Category: Glycosyl hydrolase]] | [[Category: Glycosyl hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
[[Category: Mannosidase]] | [[Category: Mannosidase]] | ||
[[Category: Substrate analogue]] | [[Category: Substrate analogue]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 10:01:32 2009'' | ||
Revision as of 16:33, 27 July 2012
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| 1x9d, resolution 1.41Å () | |||||||||
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| Ligands: | , , , | ||||||||
| Gene: | MAN1B1 (Homo sapiens) | ||||||||
| Activity: | Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113 | ||||||||
| Related: | 1fmi | ||||||||
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| |||||||||
| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue
Template:ABSTRACT PUBMED 15713668
About this Structure
1x9d is a 1 chain structure of Mannosidase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Karaveg K, Siriwardena A, Tempel W, Liu ZJ, Glushka J, Wang BC, Moremen KW. Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control. J Biol Chem. 2005 Apr 22;280(16):16197-207. Epub 2005 Feb 15. PMID:15713668 doi:10.1074/jbc.M500119200
