3S6T

Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 V327G complexed with PUGNAc

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004563	molecular_function	beta-N-acetylhexosaminidase activity
A	0005975	biological_process	carbohydrate metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OAN A 1

Chain	Residue
A	ARG220
A	GLU526
A	HOH885
A	HIS303
A	ASP367
A	TRP424
A	TRP448
A	TYR475
A	ASP477
A	TRP490
A	TRP524

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"21106526","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Site: {"description":"Important determinant of glycosidic bond specificity","evidences":[{"source":"PubMed","id":"23300622","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Essential for chitooligosaccharide substrate binding","evidences":[{"source":"PubMed","id":"23300622","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25155420","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30135205","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3WMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y1B","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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