1y7v Summary


X-ray structure of human acid-beta-glucosidase covalently bound to conduritol B epoxide

The structure was published by Premkumar, L., Sawkar, A.R., Boldin-Adamsky, S., et al., Kelly, J.W., Futerman, A.H., and Sussman, J.L., in 2005 in a paper entitled "X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2004.

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% 497 100%
B Glucosylceramidase P04062 (40-536) (GLCM_HUMAN)search Homo sapienssearch 96% 497 100%

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

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