2xwd Summary

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X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6O-(N'-(N-OCTYL)IMINO)NOJIRIMYCIN IN THE ACTIVE SITE

The structure was published by Brumshtein, B., Aguilar-Moncayo, M., Benito, J.M., et al., Sussman, J.L., Futerman, A.H., and Ortiz Mellet, C., in 2011 in a paper entitled "Cyclodextrin-Mediated Crystallization of Acid Beta-Glucosidase in Complex with Amphiphilic Bicyclic Nojirimycin Analogues." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.66 Å and deposited in 2010.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of GLUCOSYLCERAMIDASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A GLUCOSYLCERAMIDASE P04062 (40-536) (GLCM_HUMAN)search Homo sapienssearch 96% 505 97%
B GLUCOSYLCERAMIDASE P04062 (40-536) (GLCM_HUMAN)search Homo sapienssearch 96% 505 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04062 (40 - 536) GLUCOSYLCERAMIDASE Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (P04062) Glycosidasessearch, Golgi alpha-mannosidase IIsearch PF02055: O-Glycosyl hydrolase family 30search

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P04062) small molecule metabolic processsearch cellular response to tumor necrosis factorsearch skin morphogenesissearch termination of signal transductionsearch metabolic processsearch response to glucocorticoidsearch regulation of water loss via skinsearch response to estrogensearch negative regulation of MAP kinase activitysearch sphingolipid metabolic processsearch response to thyroid hormonesearch response to pHsearch sphingosine biosynthetic processsearch negative regulation of inflammatory responsesearch carbohydrate metabolic processsearch glycosphingolipid metabolic processsearch glucosylceramide catabolic processsearch positive regulation of protein dephosphorylationsearch lipid metabolic processsearch ceramide biosynthetic processsearch response to testosteronesearch negative regulation of interleukin-6 productionsearch glucosylceramidase activitysearch protein bindingsearch hydrolase activitysearch receptor bindingsearch hydrolase activity, acting on glycosyl bondssearch membranesearch extracellular vesicular exosomesearch lysosomal membranesearch lysosomal lumensearch lysosomesearch

Chain InterPro annotation
A, B Glycoside hydrolase, family 30search Glycosyl hydrolase, family 13, all-betasearch Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch