2wkl Summary

pdbe.org/2wkl
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VELAGLUCERASE ALFA

The structure was published by Brumshtein, B., Salinas, P., Peterson, B., et al., Savickas, P.J., Robinson, G.S., and Futerman, A.H., in 2010 in a paper entitled "Characterization of Gene-Activated Human Acid-Beta-Glucosidase: Crystal Structure, Glycan Composition and Internalization Into Macrophages." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 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 Not available
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 (CATH) Sequence family (Pfam)
A, B (P04062) Glycosidasessearch, Golgi alpha-mannosidase IIsearch PF02055: O-Glycosyl hydrolase family 30search

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

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