2nt1 Summary

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Structure of acid-beta-glucosidase at neutral pH

The structure was published by Lieberman, R.L., Wustman, B.A., Huertas, P., et al., Schlossmacher, M.G., Ringe, D., and Petsko, G.A., in 2007 in a paper entitled "Structure of acid beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2006.

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%
C Glucosylceramidase P04062 (40-536) (GLCM_HUMAN)search Homo sapienssearch 96% 497 100%
D 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, C, D (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, C, D (P04062) sphingolipid metabolic processsearch carbohydrate metabolic processsearch regulation of water loss via skinsearch response to thyroid hormonesearch cellular response to tumor necrosis factorsearch ceramide biosynthetic processsearch response to glucocorticoidsearch termination of signal transductionsearch response to estrogensearch lipid metabolic processsearch skin morphogenesissearch response to testosteronesearch negative regulation of interleukin-6 productionsearch glycosphingolipid metabolic processsearch small molecule metabolic processsearch sphingosine biosynthetic processsearch positive regulation of protein dephosphorylationsearch metabolic processsearch cell deathsearch response to pHsearch negative regulation of MAP kinase activitysearch negative regulation of inflammatory responsesearch glucosylceramide catabolic processsearch hydrolase activity, acting on glycosyl bondssearch glucosylceramidase activitysearch hydrolase activitysearch receptor bindingsearch protein bindingsearch membranesearch lysosomal membranesearch lysosomesearch lysosomal lumensearch extracellular vesicular exosomesearch

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