2wcg Summary

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X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH N-OCTYL(CYCLIC GUANIDINE)-NOJIRIMYCIN IN THE ACTIVE SITE

The structure was published by Brumshtein, B., Aguilar-Moncayo, M., Garcia-Moreno, M.I., et al., Aviezer, D., Sussman, J.L., and Futerman, A.H., in 2009 in a paper entitled "6-Amino-6-Deoxy-5,6-Di-N-(N'-Octyliminomethylidene)Nojirimycin: Synthesis, Biological Evaluation, and Crystal Structure in Complex with Acid Beta-Glucosidase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2009.

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

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