2v3e Summary

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ACID-BETA-GLUCOSIDASE WITH N-NONYL-DEOXYNOJIRIMYCIN

The structure was published by Brumshtein, B., Greenblatt, H.M., Butters, T.D., et al., Silman, I., Futerman, A.H., and Sussman, J.L., in 2007 in a paper entitled "Crystal Structures of Complexes of N-Butyl- and N-Nonyl-Deoxynojirimycin Bound to Acid Beta-Glucosidase: Insights Into the Mechanism of Chemical Chaperone Action in Gaucher Disease." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2007.

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 98%
B GLUCOSYLCERAMIDASE P04062 (40-536) (GLCM_HUMAN)search Homo sapienssearch 96% 505 98%


This entry contains 1 unique UniProt protein:

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

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P04062) Composite domain of glycosyl hydrolase families 5, 30, 39 and 51search, beta-glycanasessearch Glycosidasessearch, Golgi alpha-mannosidase IIsearch PF02055: O-Glycosyl hydrolase family 30search

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

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