1X9D
Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue
Summary for 1X9D
Entry DOI | 10.2210/pdb1x9d/pdb |
Related | 1FMI |
Related PRD ID | PRD_900033 |
Descriptor | Endoplasmic 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 Keywords | mannosidase, substrate analogue, glycosyl hydrolase, hydrolase |
Biological source | Homo sapiens (human) |
Cellular location | Endoplasmic reticulum membrane ; Single-pass type II membrane protein : Q9UKM7 |
Total number of polymer chains | 1 |
Total formula weight | 62028.18 |
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 citation | Karaveg, 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: 15713668DOI: 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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