4XWH

Crystal structure of the human N-acetyl-alpha-glucosaminidase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004561	molecular_function	alpha-N-acetylglucosaminidase activity
A	0005764	cellular_component	lysosome
A	0005773	cellular_component	vacuole
A	0007399	biological_process	nervous system development
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0030200	biological_process	heparan sulfate proteoglycan catabolic process
A	0030202	biological_process	heparin proteoglycan metabolic process
A	0043202	cellular_component	lysosomal lumen
A	0048731	biological_process	system development
A	0070062	cellular_component	extracellular exosome
A	0140315	molecular_function	iron ion sequestering activity
A	1901135	biological_process	carbohydrate derivative metabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2015","submissionDatabase":"PDB data bank","title":"Crystal structure of N-acetylglucosaminidase.","authors":["Birrane G.","Meiyappan M.","Dassier A."]}},{"source":"PDB","id":"4XWH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2015","submissionDatabase":"PDB data bank","title":"Crystal structure of N-acetylglucosaminidase.","authors":["Birrane G.","Meiyappan M.","Dassier A."]}},{"source":"PDB","id":"4XWH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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