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1X9D

Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue

Summary for 1X9D
Entry DOI10.2210/pdb1x9d/pdb
Related1FMI
Related PRD IDPRD_900033
DescriptorEndoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase, alpha-D-mannopyranose-(1-2)-methyl 2-thio-alpha-D-mannopyranoside, CALCIUM ION, ... (6 entities in total)
Functional Keywordsmannosidase, substrate analogue, glycosyl hydrolase, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationEndoplasmic reticulum membrane ; Single-pass type II membrane protein : Q9UKM7
Total number of polymer chains1
Total formula weight62028.18
Authors
Karaveg, K.,Tempel, W.,Liu, Z.J.,Siriwardena, A.,Moremen, K.W.,Wang, B.C. (deposition date: 2004-08-20, release date: 2005-02-22, Last modification date: 2023-08-23)
Primary citationKaraveg, K.,Siriwardena, A.,Tempel, W.,Liu, Z.J.,Glushka, J.,Wang, B.C.,Moremen, K.W.
Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control.
J.Biol.Chem., 280:16197-16207, 2005
Cited by
PubMed: 15713668
DOI: 10.1074/jbc.M500119200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.41 Å)
Structure validation

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