2v3f Summary

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ACID-BETA-GLUCOSIDASE PRODUCED IN CARROT

The structure was published by Shaaltiel, Y., Bartfeld, D., Hashmueli, S., et al., Sussman, J.L., Futerman, A.H., and Aviezer, D., in 2007 in a paper entitled "Production of Glucocerebrosidase with Terminal Mannose Glycans for Enzyme Replacement Therapy of Gaucher'S Disease Using a Plant Cell System." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.95 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) glycosphingolipid metabolic processsearch glucosylceramide catabolic processsearch cellular response to tumor necrosis factorsearch response to glucocorticoidsearch ceramide biosynthetic processsearch negative regulation of inflammatory responsesearch carbohydrate metabolic processsearch sphingolipid metabolic processsearch skin morphogenesissearch sphingosine biosynthetic processsearch negative regulation of MAP kinase activitysearch metabolic processsearch regulation of water loss via skinsearch cell deathsearch positive regulation of protein dephosphorylationsearch lipid metabolic processsearch response to estrogensearch response to thyroid hormonesearch response to pHsearch response to testosteronesearch termination of signal transductionsearch negative regulation of interleukin-6 productionsearch small molecule metabolic processsearch lysosomesearch lysosomal lumensearch lysosomal membranesearch extracellular vesicular exosomesearch membranesearch receptor bindingsearch glucosylceramidase activitysearch hydrolase activitysearch 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