2vt0 Summary


X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells

The structure was published by Kacher, Y., Brumshtein, B., Boldin-Adamsky, S., et al., Silman, I., Sussman, J.L., and Futerman, A.H., in 2008 in a paper entitled "Acid Beta-Glucosidase: Insights from Structural Analysis and Relevance to Gaucher Disease Therapy." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.15 Å and deposited in 2008.

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

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